SAM domain of SASH1 proteins, repeat 1; SAM (sterile alpha motif) repeat 1 of SASH1 proteins is a predicted protein-protein interaction domain. Members of this subfamily are putative adaptor proteins. They appear to mediate signal transduction. SASH1 can bind 14-3-3 proteins in response to IGF1/phosphatidylinositol 3-kinase signaling. SASH1 was found upregulated in different tissues including thymus, placenta, lungs and downregulated in some breast tumors, liver metastases and colon cancers, relative to corresponding normal tissues. SASH1 is a potential candidate for a tumor suppressor gene in breast cancers. At the same time, downregulation of SASH1 in colon cancer is associated with metastasis and a poor prognosis.

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907077771  716 QPKSVEDLLDRINLKEHMPTFLFNGYEDLDTFKLLEEEDLDELNIRDPEHRAVLLTAVELLQEYD 780
Cdd:cd09559      2 QPKSVEDLLDRINLKEHMPTFLFNGYEDLDTFKLLEEEDLDELNIRDPEHRAVLLTAVELLQEYD 66

Src homology 3 domain of SAM And SH3 Domain Containing Protein 1; SASH1 is a potential tumor suppressor in breast and colon cancer. Its decreased expression is associated with aggressive tumor growth, metastasis, and poor prognosis. It is widely expressed in normal tissues (except lymphocytes and dendritic cells) and is localized in the nucleus and the cytoplasm. SASH1 interacts with the oncoprotein cortactin and is important in cell migration and adhesion. It is a member of the SLY family of proteins, which are adaptor proteins containing a central conserved region with a bipartite nuclear localization signal (NLS) as well as SAM (sterile alpha motif) and SH3 domains. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1907077771  639 GRARVHTDFTPSPYDTDSLKLKKGDIIDIISKPPMGTWMGLLNNKVGTFKFIYVDVL 695
Cdd:cd11967      1 GRARVHTDFTPSPYDTDSLKLKKGDIIDIISKPPMGTWMGLLNNKVGTFKFIYVDVL 57

transcriptional regulator ICP4; Provisional

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907077771  782 NSDQSGSQEKLLVDNQGLSGRSPRDSGCYESSENLENAKTHKPSVLSTKSSTESNLKSFTRSQPGNYPTLPlmksgevrk 861
Cdd:PHA03307    39 SQGQLVSDSAELAAVTVVAGAAACDRFEPPTGPPPGPGTEAPANESRSTPTWSLSTLAPASPAREGSPTPP--------- 109

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907077771  862 qGEEGRLGRGLAPDTAkSCDVPSVTDLSKNRRSLPVSICRSCETLEGPEPVESWPRSHSldDLQGDADVGKNVPTEMPET 941
Cdd:PHA03307   110 -GPSSPDPPPPTPPPA-SPPPSPAPDLSEMLRPVGSPGPPPAASPPAAGASPAAVASDA--ASSRQAALPLSSPEETARA 185

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907077771  942 CSQNVPEVPQKTSACTSKALPRGRDPTAdvmlltqSKRFSDPPKTMAKKLDGSVVASNLGIAPPQCIPRDFE-------- 1013
Cdd:PHA03307   186 PSSPPAEPPPSTPPAAASPRPPRRSSPI-------SASASSPAPAPGRSAADDAGASSSDSSSSESSGCGWGpenecplp 258

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907077771 1014 -AQPPVKPGLTRTSLEGLRKGHDHhPLGTKEGVDGEQSAPETRTQSRHPSQPPPVPAKKSRERLANGLHLVPSPEAPilp 1092
Cdd:PHA03307   259 rPAPITLPTRIWEASGWNGPSSRP-GPASSSSSPRERSPSPSPSSPGSGPAPSSPRASSSSSSSRESSSSSTSSSSE--- 334

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*....
gi 1907077771 1093 lKKASPASPVSPSDCPSPREPRPSSGTEPGSPAcTRPPPWLAELPESTS 1141
Cdd:PHA03307   335 -SSRGAAVSPGPSPSRSPSPSRPPPPADPSSPR-KRPRPSRAPSSPAAS 381

SAM domain of SASH1 proteins, repeat 1; SAM (sterile alpha motif) repeat 1 of SASH1 proteins is a predicted protein-protein interaction domain. Members of this subfamily are putative adaptor proteins. They appear to mediate signal transduction. SASH1 can bind 14-3-3 proteins in response to IGF1/phosphatidylinositol 3-kinase signaling. SASH1 was found upregulated in different tissues including thymus, placenta, lungs and downregulated in some breast tumors, liver metastases and colon cancers, relative to corresponding normal tissues. SASH1 is a potential candidate for a tumor suppressor gene in breast cancers. At the same time, downregulation of SASH1 in colon cancer is associated with metastasis and a poor prognosis.

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907077771  716 QPKSVEDLLDRINLKEHMPTFLFNGYEDLDTFKLLEEEDLDELNIRDPEHRAVLLTAVELLQEYD 780
Cdd:cd09559      2 QPKSVEDLLDRINLKEHMPTFLFNGYEDLDTFKLLEEEDLDELNIRDPEHRAVLLTAVELLQEYD 66

Src homology 3 domain of SAM And SH3 Domain Containing Protein 1; SASH1 is a potential tumor suppressor in breast and colon cancer. Its decreased expression is associated with aggressive tumor growth, metastasis, and poor prognosis. It is widely expressed in normal tissues (except lymphocytes and dendritic cells) and is localized in the nucleus and the cytoplasm. SASH1 interacts with the oncoprotein cortactin and is important in cell migration and adhesion. It is a member of the SLY family of proteins, which are adaptor proteins containing a central conserved region with a bipartite nuclear localization signal (NLS) as well as SAM (sterile alpha motif) and SH3 domains. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1907077771  639 GRARVHTDFTPSPYDTDSLKLKKGDIIDIISKPPMGTWMGLLNNKVGTFKFIYVDVL 695
Cdd:cd11967      1 GRARVHTDFTPSPYDTDSLKLKKGDIIDIISKPPMGTWMGLLNNKVGTFKFIYVDVL 57

SAM domain (Sterile alpha motif);

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1907077771 1253 SMSDWLISIGLPMYTSTLSDAGFSTLSQVPSLSHSCLQEAGITEERHIRKLITAARLFK 1311
Cdd:pfam07647    8 SVADWLRSIGLEQYTDNFRDQGITGAELLLRLTLEDLKRLGITSVGHRRKILKKIQELK 66

transcriptional regulator ICP4; Provisional

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907077771  782 NSDQSGSQEKLLVDNQGLSGRSPRDSGCYESSENLENAKTHKPSVLSTKSSTESNLKSFTRSQPGNYPTLPlmksgevrk 861
Cdd:PHA03307    39 SQGQLVSDSAELAAVTVVAGAAACDRFEPPTGPPPGPGTEAPANESRSTPTWSLSTLAPASPAREGSPTPP--------- 109

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907077771  862 qGEEGRLGRGLAPDTAkSCDVPSVTDLSKNRRSLPVSICRSCETLEGPEPVESWPRSHSldDLQGDADVGKNVPTEMPET 941
Cdd:PHA03307   110 -GPSSPDPPPPTPPPA-SPPPSPAPDLSEMLRPVGSPGPPPAASPPAAGASPAAVASDA--ASSRQAALPLSSPEETARA 185

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907077771  942 CSQNVPEVPQKTSACTSKALPRGRDPTAdvmlltqSKRFSDPPKTMAKKLDGSVVASNLGIAPPQCIPRDFE-------- 1013
Cdd:PHA03307   186 PSSPPAEPPPSTPPAAASPRPPRRSSPI-------SASASSPAPAPGRSAADDAGASSSDSSSSESSGCGWGpenecplp 258

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907077771 1014 -AQPPVKPGLTRTSLEGLRKGHDHhPLGTKEGVDGEQSAPETRTQSRHPSQPPPVPAKKSRERLANGLHLVPSPEAPilp 1092
Cdd:PHA03307   259 rPAPITLPTRIWEASGWNGPSSRP-GPASSSSSPRERSPSPSPSSPGSGPAPSSPRASSSSSSSRESSSSSTSSSSE--- 334

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*....
gi 1907077771 1093 lKKASPASPVSPSDCPSPREPRPSSGTEPGSPAcTRPPPWLAELPESTS 1141
Cdd:PHA03307   335 -SSRGAAVSPGPSPSRSPSPSRPPPPADPSSPR-KRPRPSRAPSSPAAS 381

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907077771  931 GKNVPTEMPETC-SQNVPEVPQKTSACTSKaLPRGRDPTADVMLLTQSKRFSDPPKTMAKKldgsvvaSNLGIAPPQCIP 1009
Cdd:pfam03154  187 PPPGTTQAATAGpTPSAPSVPPQGSPATSQ-PPNQTQSTAAPHTLIQQTPTLHPQRLPSPH-------PPLQPMTQPPPP 258

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907077771 1010 RDFEAQPPVKPGLTRTSLEG---LRKGHDH--HPLGTKEGVDGEQSA--------------PETRTQSRHPSQPPPVPAK 1070
Cdd:pfam03154  259 SQVSPQPLPQPSLHGQMPPMphsLQTGPSHmqHPVPPQPFPLTPQSSqsqvppgpspaapgQSQQRIHTPPSQSQLQSQQ 338

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907077771 1071 KSRERLANGL-----HLVPSPEAPILPLKKA---------SPASPVS-PSDCPSPREPRPSSGTEPGSPACTRPPPwLAE 1135
Cdd:pfam03154  339 PPREQPLPPAplsmpHIKPPPTTPIPQLPNPqshkhpphlSGPSPFQmNSNLPPPPALKPLSSLSTHHPPSAHPPP-LQL 417

                          250       260
                   ....*....|....*....|...
gi 1907077771 1136 LPESTSLQEHGVKlGPVLSRKVS 1158
Cdd:pfam03154  418 MPQSQQLPPPPAQ-PPVLTQSQS 439

Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related tyrosine kinases, appears to mediate cell-cell initiated signal transduction via the binding of SH2-containing proteins to a conserved tyrosine that is phosphorylated. In many cases mediates homodimerisation.

                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907077771   717 PKSVEDLLDRINLKEHMPTFLFNGYEDLDTFKLLEEEDLDELNIRDPEHRAVLLTAVELLQEY 779
Cdd:smart00454    6 PESVADWLESIGLEQYADNFRKNGIDGALLLLLTSEEDLKELGITKLGHRKKILKAIQKLKEQ 68

SAM domain of SASH1 proteins, repeat 1; SAM (sterile alpha motif) repeat 1 of SASH1 proteins is a predicted protein-protein interaction domain. Members of this subfamily are putative adaptor proteins. They appear to mediate signal transduction. SASH1 can bind 14-3-3 proteins in response to IGF1/phosphatidylinositol 3-kinase signaling. SASH1 was found upregulated in different tissues including thymus, placenta, lungs and downregulated in some breast tumors, liver metastases and colon cancers, relative to corresponding normal tissues. SASH1 is a potential candidate for a tumor suppressor gene in breast cancers. At the same time, downregulation of SASH1 in colon cancer is associated with metastasis and a poor prognosis.

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907077771  716 QPKSVEDLLDRINLKEHMPTFLFNGYEDLDTFKLLEEEDLDELNIRDPEHRAVLLTAVELLQEYD 780
Cdd:cd09559      2 QPKSVEDLLDRINLKEHMPTFLFNGYEDLDTFKLLEEEDLDELNIRDPEHRAVLLTAVELLQEYD 66

Src homology 3 domain of SAM And SH3 Domain Containing Protein 1; SASH1 is a potential tumor suppressor in breast and colon cancer. Its decreased expression is associated with aggressive tumor growth, metastasis, and poor prognosis. It is widely expressed in normal tissues (except lymphocytes and dendritic cells) and is localized in the nucleus and the cytoplasm. SASH1 interacts with the oncoprotein cortactin and is important in cell migration and adhesion. It is a member of the SLY family of proteins, which are adaptor proteins containing a central conserved region with a bipartite nuclear localization signal (NLS) as well as SAM (sterile alpha motif) and SH3 domains. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1907077771  639 GRARVHTDFTPSPYDTDSLKLKKGDIIDIISKPPMGTWMGLLNNKVGTFKFIYVDVL 695
Cdd:cd11967      1 GRARVHTDFTPSPYDTDSLKLKKGDIIDIISKPPMGTWMGLLNNKVGTFKFIYVDVL 57

Src homology 3 domain of SAM And SH3 Domain Containing Proteins; This subfamily, also called the SLY family, is composed of SAM And SH3 Domain Containing Protein 1 (SASH1), SASH2, SASH3, and similar proteins. These are adaptor proteins containing a central conserved region with a bipartite nuclear localization signal (NLS) as wells as SAM (sterile alpha motif) and SH3 domains. SASH1 is a potential tumor suppressor in breast and colon cancer. It is widely expressed in normal tissues (except lymphocytes and dendritic cells) and is localized in the nucleus and the cytoplasm. SASH1 interacts with the oncoprotein cortactin and is important in cell migration and adhesion. SASH2 (also called SAMSN-1, SLY2, HACS1 or NASH1) and SASH3 (also called SLY/SLY1) are expressed mainly in hematopoietic cells, although SASH2 is also found in endothelial cells as well as myeloid leukemias and myeloma. SASH2 was found to be differentially expressed in malignant haematopoietic cells and in colorectal tumors, and is a potential tumor suppressor in lung cancer. SASH3 is essential in the full activation of adaptive immunity and is involved in the signaling of T cell receptors. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1907077771  640 RARVHTDFTPSPYDTDSLKLKKGDIIDIISKPPMGTWMGLLNNKVGTFKFIY 691
Cdd:cd11822      1 RAKVHTDFTPSPYDTDSLKLKKGDIIDIINKPPMGIWTGMLNNKVGNFKFIY 52

SAM (Sterile alpha motif ), SASH1-like; SAM (sterile alpha motif) domain of SASH1-like proteins is a protein-protein interaction domain. Members of this subfamily are putative adaptor proteins. They appear to mediate signal transduction. Proteins of this subfamily are known to be involved in preventing DN thymocytes from premature initiation of programmed cell death and in B cells activation and differentiation. They have been found downregulated in some breast tumors, liver metastases and colon cancers if compare to corresponding normal tissues.

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907077771  716 QPKSVEDLLDRINLKEHMPTFLFNGYEDLDTFKLLEEEDLDELNIRDPEHRAVLLTAVEL 775
Cdd:cd09493      1 KPKTVEELLERINLQEHTSTLLLNGYETLEDFKDLKESHLNELNITDPEHRAKLLTAAEL 60

SAM domain of SAMSN1 subfamily; SAM (sterile alpha motif) domain of SAMSN1 (also known as HACS1 or NASH1) proteins is a predicted protein-protein interaction domain. Members of this group are putative signaling/adaptor proteins. They appear to mediate signal transduction in lymphoid tissues. Murine HACS1 protein likely plays a role in B cell activation and differentiation. Potential binding partners of HACS1 are SLAM, DEC205 and PIR-B receptors and also some unidentified tyrosine-phosphorylated proteins. Proteins of this group were found preferentially expressed in normal hematopietic tissues and in some malignancies including lymphoma, myeloid leukemia and myeloma.

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907077771  713 RPSQPKSVEDLLDRINLKEHMPTFLFNGYEDLDTFKLLEEEDLDELNIRDPEHRAVLLTAVELLQE 778
Cdd:cd09561      1 RRPKPKTLQELLERIHLQEYTSTLLLNGYETLEDLKDLKESHLIELNITDPEDRARLLSAAENLLD 66

SAM domain (Sterile alpha motif);

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1907077771 1253 SMSDWLISIGLPMYTSTLSDAGFSTLSQVPSLSHSCLQEAGITEERHIRKLITAARLFK 1311
Cdd:pfam07647    8 SVADWLRSIGLEQYTDNFRDQGITGAELLLRLTLEDLKRLGITSVGHRRKILKKIQELK 66

Second Src Homology 3 domain (SH3B) of CD2-associated protein and similar proteins; This subfamily is composed of the second SH3 domain (SH3B) of CD2AP, CIN85 (Cbl-interacting protein of 85 kDa), and similar domains. CD2AP and CIN85 are adaptor proteins that bind to protein partners and assemble complexes that have been implicated in T cell activation, kidney function, and apoptosis of neuronal cells. They also associate with endocytic proteins, actin cytoskeleton components, and other adaptor proteins involved in receptor tyrosine kinase (RTK) signaling. CD2AP and the main isoform of CIN85 contain three SH3 domains, a proline-rich region, and a C-terminal coiled-coil domain. All of these domains enable CD2AP and CIN85 to bind various protein partners and assemble complexes that have been implicated in many different functions. SH3B of both proteins have been shown to bind to Cbl. In the case of CD2AP, its SH3B binds to Cbl at a site distinct from the c-Cbl/SH3A binding site. The CIN85 SH3B also binds ubiquitin. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1907077771  640 RARVhtDFTPSPYDTDSLKLKKGDIIDIISKPPMGTWMGLLNNKVGTF 687
Cdd:cd11874      1 RCKV--LFSYTPQNEDELELKVGDTIEVLGEVEEGWWEGKLNGKVGVF 46

SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of approximately 70 amino acids. This domain is found in the Fungi/Metazoa group and in a restricted number of bacteria. Proteins with SAM domains are represented by a wide variety of domain architectures and have different intracellular localization, including nucleus, cytoplasm and membranes. SAM domains have diverse functions. They can interact with proteins, RNAs and membrane lipids, contain site of phosphorylation and/or kinase docking site, and play a role in protein homo and hetero dimerization/oligomerization in processes ranging from signal transduction to regulation of transcription. Mutations in SAM domains have been linked to several diseases.

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1907077771 1255 SDWLISIGLPMYTSTLSDAGFsTLSQVPSLSHSCLQEAGITEERHIRKLITAAR 1308
Cdd:cd09487      3 AEWLESLGLEQYADLFRKNEI-DGDALLLLTDEDLKELGITSPGHRKKILRAIQ 55

Src Homology 3 domain superfamily; Src Homology 3 (SH3) domains are protein interaction domains that bind proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. Thus, they are referred to as proline-recognition domains (PRDs). SH3 domains are less selective and show more diverse specificity compared to other PRDs. They have been shown to bind peptide sequences that lack the PxxP motif; examples include the PxxDY motif of Eps8 and the RKxxYxxY sequence in SKAP55. SH3 domain containing proteins play versatile and diverse roles in the cell, including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies, among others. Many members of this superfamily are adaptor proteins that associate with a number of protein partners, facilitating complex formation and signal transduction.

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1907077771  640 RARVHTDFTPSpyDTDSLKLKKGDIIDIISKPPMGTWMG-LLNNKVGTFKFIY 691
Cdd:cd00174      1 YARALYDYEAQ--DDDELSFKKGDIITVLEKDDDGWWEGeLNGGREGLFPANY 51

Src homology 3 domain of Nitric Oxide Synthase TRaffic INducer; Nostrin is expressed in endothelial and epithelial cells and is involved in the regulation, trafficking and targeting of endothelial NOS (eNOS). It facilitates the endocytosis of eNOS by coordinating the functions of dynamin and the Wiskott-Aldrich syndrome protein (WASP). Increased expression of Nostrin may be correlated to preeclampsia. Nostrin contains an N-terminal F-BAR domain and a C-terminal SH3 domain. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 1907077771  646 DFTPSPYDtdSLKLKKGDIIDIISKPPMGTWMGLLNNKVGTFKFIYVDV 694
Cdd:cd11823      7 SYTANRED--ELSLQPGDIIEVHEKQDDGWWLGELNGKKGIFPATYVEE 53

Third Src Homology 3 domain (SH3C) of CD2-associated protein and similar proteins; This subfamily is composed of the third SH3 domain (SH3C) of CD2AP, CIN85 (Cbl-interacting protein of 85 kDa), and similar domains. CD2AP and CIN85 are adaptor proteins that bind to protein partners and assemble complexes that have been implicated in T cell activation, kidney function, and apoptosis of neuronal cells. They also associate with endocytic proteins, actin cytoskeleton components, and other adaptor proteins involved in receptor tyrosine kinase (RTK) signaling. CD2AP and the main isoform of CIN85 contain three SH3 domains, a proline-rich region, and a C-terminal coiled-coil domain. All of these domains enable CD2AP and CIN85 to bind various protein partners and assemble complexes that have been implicated in many different functions. SH3C of both proteins have been shown to bind to ubiquitin. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1907077771  640 RARVHTDFTPSpyDTDSLKLKKGDIIDIISK--PPMGTWMGLLNNKVGTF 687
Cdd:cd11875      1 KARVLFDYEAE--NEDELTLREGDIVTILSKdcEDKGWWKGELNGKRGVF 48

SAM domain of EPH-B6 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain of EPH-B6 subfamily of receptor tyrosine kinases is a C-terminal potential protein-protein interaction domain. This domain is located in the cytoplasmic region of EPH-B6 receptors and appears to mediate cell-cell initiated signal transduction. Receptors of this type are highly expressed in embryo and adult nervous system, in thymus and also in T-cells. They are involved in regulation of cell adhesion and migration. (EPH-B6 receptor is unusual; it fails to show catalytic activity due to alteration in kinase domain). EPH-B6 may be considered as a biomarker in some types of tumors; EPH-B6 activates MAP kinase signaling in lung adenocarcinoma, suppresses metastasis formation in non-small cell lung cancer, and slows invasiveness in some breast cancer cell lines.

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907077771 1250 CVASMSDWLISIGLPMYTSTLSDAGFSTLSQVPSLSHSCLQEAGITEERHIRKLITAARLFK 1311
Cdd:cd09555      5 CLDSPQAWLSAIGLECYQDNFSKFGLCTFSDVAQLSLEDLPALGITLAGHQKKLLHHIQLLQ 66

SAM domain of caskin protein repeat 2; SAM (sterile alpha motif) domain repeat 2 of caskin1,2 proteins is a protein-protein interaction domain. Caskin has two tandem SAM domains. Caskin protein is known to interact with membrane-associated guanylate kinase CASK, and may play a role in neural development, synaptic protein targeting, and regulation of gene expression.

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1907077771 1253 SMSDWLISIGLPMYTSTLSDAGFSTLSQVPSLSHSCLQEAGITEERHIRKLITA 1306
Cdd:cd09498      9 DLLEWLSLLGLPQYHKVLVENGYDSIDFVTDLTWEDLQDIGITKLGHQKKLMLA 62

Second Src Homology 3 domain (SH3B) of CD2-associated protein; CD2AP, also called CMS (Cas ligand with Multiple SH3 domains) or METS1 (Mesenchyme-to-Epithelium Transition protein with SH3 domains), is a cytosolic adaptor protein that plays a role in regulating the cytoskeleton. It is critical in cell-to-cell union necessary for kidney function. It also stabilizes the contact between a T cell and antigen-presenting cells. It is primarily expressed in podocytes at the cytoplasmic face of the slit diaphragm and serves as a linker anchoring podocin and nephrin to the actin cytoskeleton. CD2AP contains three SH3 domains, a proline-rich region, and a C-terminal coiled-coil domain. All of these domains enable CD2AP to bind various protein partners and assemble complexes that have been implicated in many different functions. This alignment model represents the second SH3 domain (SH3B) of CD2AP. SH3B binds to c-Cbl in a site (TPSSRPLR is the core binding motif) distinct from the c-Cbl/SH3A binding site. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1907077771  651 PYDTDSLKLKKGDIIDIISKPPMGTWMGLLNNKVGTFKFIYVDVL 695
Cdd:cd12054     11 PQNEDELELKVGDIIDINEEVEEGWWSGTLNGKSGLFPSNFVKEL 55

large tegument protein UL36; Provisional

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907077771  935 PTEMPETCSQNVPEVPQKTSACTSKALPRGRDPTAdvmlltqskrfSDPPKTMAKKLDGSVVASNLGIAPPQCIPRDFEA 1014
Cdd:PHA03247  2589 PDAPPQSARPRAPVDDRGDPRGPAPPSPLPPDTHA-----------PDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPA 2657

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907077771 1015 QPPVKPGlTRTSLEGLRKGHDHHPLGTKEGVDGEQSAPETRTQSRHPSQPPPVPA-------------KKSRERLANGLH 1081
Cdd:PHA03247  2658 PGRVSRP-RRARRLGRAAQASSPPQRPRRRAARPTVGSLTSLADPPPPPPTPEPAphalvsatplppgPAAARQASPALP 2736

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907077771 1082 LVP----SPEAPILPLKKASPASPVSPSDCPSPREPRpssgTEPGSPACTRPPPWLAELPEST 1140
Cdd:PHA03247  2737 AAPappaVPAGPATPGGPARPARPPTTAGPPAPAPPA----APAAGPPRRLTRPAVASLSESR 2795

C-terminal Src homology 3 domain of Growth factor receptor-bound protein 2 (GRB2) and related proteins; This family includes the adaptor protein GRB2 and related proteins including Drosophila melanogaster Downstream of receptor kinase (DRK), Caenorhabditis elegans Sex muscle abnormal protein 5 (Sem-5), GRB2-related adaptor protein (GRAP), GRAP2, and similar proteins. Family members contain an N-terminal SH3 domain, a central SH2 domain, and a C-terminal SH3 domain. GRB2/Sem-5/DRK is a critical signaling molecule that regulates the Ras pathway by linking tyrosine kinases to the Ras guanine nucleotide releasing protein Sos (son of sevenless), which converts Ras to the active GTP-bound state. GRAP2 plays an important role in T cell receptor (TCR) signaling by promoting the formation of the SLP-76:LAT complex, which couples the TCR to the Ras pathway. GRAP acts as a negative regulator of T cell receptor (TCR)-induced lymphocyte proliferation by downregulating the signaling to the Ras/ERK pathway. The C-terminal SH3 domains (SH3c) of GRB2 and GRAP2 have been shown to bind to classical PxxP motif ligands, as well as to non-classical motifs. GRB2 SH3c binds Gab2 (Grb2-associated binder 2) through epitopes containing RxxK motifs, while the SH3c of GRAP2 binds to the phosphatase-like protein HD-PTP via a RxxxxK motif. SH3 domains are protein interaction domains that typically bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1907077771  640 RARVHTDFTPSpyDTDSLKLKKGDIIDIISKPPMGTWMGLLNNKVGTFKFIYV 692
Cdd:cd11805      1 RVQALYDFNPQ--EPGELEFRRGDIITVLDSSDPDWWKGELRGRVGIFPANYV 51

SAM domain of EPH family of tyrosine kinase receptors; SAM (sterile alpha motif) domain of EPH (erythropoietin-producing hepatocyte) family of receptor tyrosine kinases is a C-terminal signal transduction module located in the cytoplasmic region of these receptors. SAM appears to mediate cell-cell initiated signal transduction via binding proteins to a conserved tyrosine that is phosphorylated. In some cases the SAM domain mediates homodimerization/oligomerization and plays a role in the clustering process necessary for signaling. EPH kinases are the largest family of receptor tyrosine kinases. They are classified into two groups based on their abilities to bind ephrin-A and ephrin-B ligands. The EPH receptors are involved in regulation of cell movement, shape, and attachment during embryonic development; they control cell-cell interactions in the vascular, nervous, epithelial, and immune systems, and in many tumors. They are potential molecular markers for cancer diagnostics and potential targets for cancer therapy.

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1907077771 1250 CVASMSDWLISIGLPMYTSTLSDAGFSTLSQVPSLSHSCLQEAGITEERHIRKLI 1304
Cdd:cd09488      1 AFRSVGEWLESIKMGRYKENFTAAGYTSLDAVAQMTAEDLTRLGVTLVGHQKKIL 55

Src Homology 3 domain of Sdc25/Cdc25 guanine nucleotide exchange factors; This subfamily is composed of the Saccharomyces cerevisiae guanine nucleotide exchange factors (GEFs) Sdc25 and Cdc25, and similar proteins. These GEFs regulate Ras by stimulating the GDP/GTP exchange on Ras. Cdc25 is involved in the Ras/PKA pathway that plays an important role in the regulation of metabolism, stress responses, and proliferation, depending on available nutrients and conditions. Proteins in this subfamily contain an N-terminal SH3 domain as well as REM (Ras exchanger motif) and RasGEF domains at the C-terminus. SH3 domains bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs; they play a role in the regulation of enzymes by intramolecular interactions, changing the subcellular localization of signal pathway components and mediate multiprotein complex assemblies.

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1907077771  642 RVHTDFTPSpyDTDSLKLKKGDIIDIISKPPMGTWMGLLNNKVGTFK 688
Cdd:cd11883      3 VALYDFTPK--SKNQLSFKAGDIIYVLNKDPSGWWDGVIISSSGKVK 47

SAM domain of EPH-B4 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain of EPH-B4 subfamily of receptor tyrosine kinases is a C-terminal potential protein-protein interaction domain. This domain is located in the cytoplasmic region of EPH-B4 receptors and appears to mediate cell-cell initiated signal transduction. EPH-B4 protein kinase performs kinase-dependent and kinase-independent functions. These receptors play a role in the regular vascular system development during embryogenesis. They were found overexpressed in a variety of cancers, including carcinoma of the head and neck, ovarian cancer, bladder cancer, and downregulated in bone myeloma. Thus, EphB4 is a potential biomarker and a target for drug design.

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1907077771 1252 ASMSDWLISIGLPMYTSTLSDAGFSTLSQVPSLSHSCLQEAGITEERHIRKLITA 1306
Cdd:cd09554      4 GSVGEWLRAIKMERYEDSFLQAGFTTFQLVSQISTEDLLRMGVTLAGHQKKILSS 58

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907077771  931 GKNVPTEMPETC-SQNVPEVPQKTSACTSKaLPRGRDPTADVMLLTQSKRFSDPPKTMAKKldgsvvaSNLGIAPPQCIP 1009
Cdd:pfam03154  187 PPPGTTQAATAGpTPSAPSVPPQGSPATSQ-PPNQTQSTAAPHTLIQQTPTLHPQRLPSPH-------PPLQPMTQPPPP 258

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907077771 1010 RDFEAQPPVKPGLTRTSLEG---LRKGHDH--HPLGTKEGVDGEQSA--------------PETRTQSRHPSQPPPVPAK 1070
Cdd:pfam03154  259 SQVSPQPLPQPSLHGQMPPMphsLQTGPSHmqHPVPPQPFPLTPQSSqsqvppgpspaapgQSQQRIHTPPSQSQLQSQQ 338

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907077771 1071 KSRERLANGL-----HLVPSPEAPILPLKKA---------SPASPVS-PSDCPSPREPRPSSGTEPGSPACTRPPPwLAE 1135
Cdd:pfam03154  339 PPREQPLPPAplsmpHIKPPPTTPIPQLPNPqshkhpphlSGPSPFQmNSNLPPPPALKPLSSLSTHHPPSAHPPP-LQL 417

                          250       260
                   ....*....|....*....|...
gi 1907077771 1136 LPESTSLQEHGVKlGPVLSRKVS 1158
Cdd:pfam03154  418 MPQSQQLPPPPAQ-PPVLTQSQS 439

large tegument protein UL36; Provisional

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907077771  982 DPPKTMAKklDGSVVASNLGIAPPQCIPRDFE-------AQPPVKPGLTRTSLEGLRKGHDHHPlgtkegvdgeqSAPET 1054
Cdd:PHA03247  2550 DPPPPLPP--AAPPAAPDRSVPPPRPAPRPSEpavtsraRRPDAPPQSARPRAPVDDRGDPRGP-----------APPSP 2616

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907077771 1055 RTQSRHPSQPPPvPAKKSRERLANGLHLVPSPEAPILPL--------------KKASPASPVSPSDCPSPREPRPSSGT- 1119
Cdd:PHA03247  2617 LPPDTHAPDPPP-PSPSPAANEPDPHPPPTVPPPERPRDdpapgrvsrprrarRLGRAAQASSPPQRPRRRAARPTVGSl 2695

                          170       180       190
                   ....*....|....*....|....*....|....
gi 1907077771 1120 -------EPGSPACTRPPPWLAELPESTSLQEHG 1146
Cdd:PHA03247  2696 tsladppPPPPTPEPAPHALVSATPLPPGPAAAR 2729

DNA polymerase III subunit gamma/tau;

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907077771 1049 QSAPETRTQSRHPSQPPP----VPAKKSRERLANGLHLVPSPEAPILPLKKASPA-SPVSPSDCPSPREPRPSSGTEPGS 1123
Cdd:PRK12323   411 AAAAAARAVAAAPARRSPapeaLAAARQASARGPGGAPAPAPAPAAAPAAAARPAaAGPRPVAAAAAAAPARAAPAAAPA 490

                           90
                   ....*....|....*
gi 1907077771 1124 PACTRPPPWlAELPE 1138
Cdd:PRK12323   491 PADDDPPPW-EELPP 504

Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related tyrosine kinases, appears to mediate cell-cell initiated signal transduction via the binding of SH2-containing proteins to a conserved tyrosine that is phosphorylated. In many cases mediates homodimerisation.

                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907077771   717 PKSVEDLLDRINLKEHMPTFLFNGYEDLDTFKLLEEEDLDELNIRDPEHRAVLLTAVELLQEY 779
Cdd:smart00454    6 PESVADWLESIGLEQYADNFRKNGIDGALLLLLTSEEDLKELGITKLGHRKKILKAIQKLKEQ 68

large tegument protein UL36; Provisional

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907077771  864 EEGRLGRGLAPDTAKSCDVPSVTDLSKNRR-SLPVSICRSCETLEGPEPVESWPRSHSLDDLQGDADVGKNvPTEMPETC 942
Cdd:PHA03247  2637 EPDPHPPPTVPPPERPRDDPAPGRVSRPRRaRRLGRAAQASSPPQRPRRRAARPTVGSLTSLADPPPPPPT-PEPAPHAL 2715

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907077771  943 SQNVPEVPQKTSA-CTSKALPRGR----DPTADVMLLTQSKRFS--------------DPPKTMAKKLDGSVVASNLGIA 1003
Cdd:PHA03247  2716 VSATPLPPGPAAArQASPALPAAPappaVPAGPATPGGPARPARppttagppapappaAPAAGPPRRLTRPAVASLSESR 2795

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907077771 1004 PPQCIPRDFEAQP---------------PVKPGLTRTSLEGLRKGHDHHPLGTKEGVDGeQSAPETRTQSRHPSQPPP-V 1067
Cdd:PHA03247  2796 ESLPSPWDPADPPaavlapaaalppaasPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGG-SVAPGGDVRRRPPSRSPAaK 2874

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907077771 1068 PAKKSRERLANGLHLVPSPEAPILPLKKASPASPVSPSDCPSPREPRPSSGTEPGSPACTRPPPWLAELPESTSLQEHGV 1147
Cdd:PHA03247  2875 PAAPARPPVRRLARPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGE 2954

                   ....*
gi 1907077771 1148 KLGPV 1152
Cdd:PHA03247  2955 PSGAV 2959

Src Homology 3 domain of SH3 domain-containing protein 21 (SH3D21) and similar proteins; N-terminal SH3 domain of the uncharacterized protein SH3 domain-containing protein 21, and similar uncharacterized domains, it belongs to the CD2AP-like_3 subfamily of proteins. The CD2AP-like_3 subfamily is composed of the third SH3 domain (SH3C) of CD2AP, CIN85 (Cbl-interacting protein of 85 kDa), and similar domains. CD2AP and CIN85 are adaptor proteins that bind to protein partners and assemble complexes that have been implicated in T cell activation, kidney function, and apoptosis of neuronal cells. They also associate with endocytic proteins, actin cytoskeleton components, and other adaptor proteins involved in receptor tyrosine kinase (RTK) signaling. CD2AP and the main isoform of CIN85 contain three SH3 domains, a proline-rich region, and a C-terminal coiled-coil domain. All of these domains enable CD2AP and CIN85 to bind various protein partners and assemble complexes that have been implicated in many different functions. SH3C of both proteins have been shown to bind to ubiquitin. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 1907077771  647 FTPSPYDTDSLKLKKGDIIDIISKPP--MGTWMGLLNNKVGTF 687
Cdd:cd12142      6 FDYNPVAPDELALKKGDVIEVISKETedEGWWEGELNGRRGFF 48

SAM domain of Arap1,2,3 (angiotensin receptor-associated protein); SAM (sterile alpha motif) domain of Arap1,2,3 subfamily proteins (angiotensin receptor-associated) is a protein-protein interaction domain. Arap1,2,3 proteins are phosphatidylinositol-3,4,5-trisphosphate-dependent GTPase-activating proteins. They are involved in phosphatidylinositol-3 kinase (PI3K) signaling pathways. In addition to SAM domain, Arap1,2,3 proteins contain ArfGap, PH-like, RhoGAP and UBQ domains. SAM domain of Arap3 protein was shown to interact with SAM domain of Ship2 phosphatidylinositol-trisphosphate phosphatase proteins. Such interaction apparently plays a role in inhibition of PI3K regulated pathways since Ship2 converts PI(3,4,5)P3 into PI(3,4)P2. Proteins of this subfamily participate in regulation of signaling and trafficking associated with a number of different receptors (including EGFR, TRAIL-R1/DR4, TRAIL-R2/DR5) in normal and cancer cells; they are involved in regulation of actin cytoskeleton remodeling, cell spreading and formation of lamellipodia.

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1907077771 1251 VASMSDWLISIGLPMYTSTLSDAGFSTLSQVPSLSHSCLQEAGITEERHIRKLI 1304
Cdd:cd09490      3 DLDIAEWLASIHLEQYLDLFREHGYVTATDCQGINDSRLKQIGISPTGHRRRIL 56

SAM domain of AIDA1AB-like proteins, repeat 2; SAM (sterile alpha motif) domain repeat 2 of AIDA1AB-like proteins is a protein-protein interaction domain. AIDA1AB-like proteins have two tandem SAM domains. They may form an intramolecular head-to-tail homodimer. One of two basic motifs of the nuclear localization signal (NLS) is located within helix 5 of the SAM2 (motif HKRK). This signal plays a role in decoupling of SAM2 from SAM1, thus facilitating translocation of this type proteins into the nucleus. SAM domains of the AIDA1AB-like subfamily can directly bind ubiquitin and participate in regulating the degradation of ubiquitinated EphA receptors, particularly EPH-A8 receptor. Additionally AIDA1AB-like proteins may participate in the regulation of nucleoplasmic coilin protein interactions.

                           10        20        30
                   ....*....|....*....|....*....|..
gi 1907077771  717 PKSVEDLLDRINLKEHMPTFLFNGYEDLDTFK 748
Cdd:cd09500      5 PASVSEWLDSIGLGDYIETFLKHGYTSMERVK 36