CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-014431
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Sorbin and SH3 domain-containing protein 1 
Protein Synonyms/Alias
 Ponsin; SH3 domain protein 5; SH3P12; c-Cbl-associated protein; CAP 
Gene Name
 Sorbs1 
Gene Synonyms/Alias
 Kiaa1296; Sh3d5 
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
260YSFSDDTKSPLSVPRubiquitination[1]
269PLSVPRSKSEMNYIEubiquitination[1]
352SPEEIDLKNEPWYKFubiquitination[1]
467LQGLSGLKRPSSSASubiquitination[1]
1111ELLPPAEKAQPRKLAubiquitination[1]
1116AEKAQPRKLAPVQVLubiquitination[1]
Reference
 [1] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023] 
Functional Description
 Plays a role in tyrosine phosphorylation of CBL by linking CBL to the insulin receptor. Required for insulin- stimulated glucose transport. Involved in formation of actin stress fibers and focal adhesions. 
Sequence Annotation
 DOMAIN 202 247 SoHo.
 DOMAIN 1049 1108 SH3 1.
 DOMAIN 1123 1184 SH3 2.
 DOMAIN 1236 1290 SH3 3.
 MOD_RES 55 55 Phosphoserine (By similarity).
 MOD_RES 58 58 Phosphoserine.
 MOD_RES 89 89 Phosphothreonine.
 MOD_RES 103 103 Phosphotyrosine.
 MOD_RES 184 184 Phosphothreonine.
 MOD_RES 261 261 Phosphoserine (By similarity).
 MOD_RES 270 270 Phosphoserine.
 MOD_RES 286 286 Phosphothreonine.
 MOD_RES 325 325 Phosphotyrosine; by ABL1.
 MOD_RES 345 345 Phosphoserine.
 MOD_RES 407 407 Phosphoserine.
 MOD_RES 421 421 Phosphotyrosine; by ABL1.
 MOD_RES 432 432 Phosphoserine.
 MOD_RES 533 533 Phosphoserine.
 MOD_RES 1201 1201 Phosphoserine (By similarity).
 MOD_RES 1238 1238 Phosphotyrosine; by ABL1.  
Keyword
 Alternative splicing; Cell junction; Cell membrane; Complete proteome; Cytoplasm; Cytoskeleton; Glycoprotein; Membrane; Nucleus; Phosphoprotein; Reference proteome; Repeat; SH3 domain; Transport. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1290 AA 
Protein Sequence
MSSECDVGSS KAVVNGLASG NHGPDKDMDP TKICTGKGTV TLRASSSYRG TPSSSPVSPQ 60
ESPKHESKSG LEPEDPSADE WKLSSSADTN GNAQPSPLAA KGYRSVHPSL SADKPQGSPL 120
LNEVSSSHIE TDSQDFPPTS RPSSAYPSTT IVNPTIVLLQ HNRDPASERR AGEQDPVPTP 180
AELTSPGRAS ERRAKDASRR VVRSAQDLSD VSTDEVGIPL RNTERSKDWY KTMFKQIHKL 240
NRDDDSDVHS PRYSFSDDTK SPLSVPRSKS EMNYIEGEKV VKRSATLPLP ARSSSLKSSP 300
ERNDWEPLDK KVDTRKYRAE PKSIYEYQPG KSSVLTNEKM SRDISPEEID LKNEPWYKFF 360
SELEFGRPTN LEKDLSFCQA ELEADLEKVE TVNKSPSANS PQSSAVSPTP DITSEPPGYI 420
YSSNFHAVKR ESDGTPGGLA SLENERQIYK SVLEGGDIPL QGLSGLKRPS SSASTKVDRK 480
GGNAHMISSS SVHSRTFHTS NALGPGCKHK KPLSAAKACI SEILPSKFKP RLSAPSALLQ 540
EQKSVLLPSE KAQSCENLCV SLNDSKRGLP LRVGGSIENL LMRSRRDYDS KSSSTMSLQE 600
YGTSSRRPCP LSRKAGLHFS MFYRDMHQIN RAGLSLGSIS SSSVRDLASH FERSSLTLAR 660
GELGASQEGS EHIPKHTVSS RITAFEQLIQ RSRSMPSLDF SGRLSKSPTP VLSRSGLTSA 720
RSAESLLEST KLRPREMDGM DSGGVYASPT CSNMADHALS FRSLVPSEPL SICSDELDHC 780
SNVSNDSREG SGGSVHGDFP KHRLNKCKGT CPASYTRFTT IRKHEQQSSR QSDWRSDSRG 840
DKNSLLRNIH LMSPLPFRLK KPLQQHPRQP PPSDSSESPA GQKADLPCHD PQDQPHSAGK 900
PQVPTRLSSR HTMARLSHNS EPPLDRPAGL EDCTRAINNG NPVPYSDHGL DRNNNPQSEL 960
AAAHGDSESP RHFIPADYLE STEEFIRRRH DDKEKLLADQ RRLKREQEEA DIAARRHTGV 1020
IPTHHQFITN ERFGDLLNID DTAKRKSGLE MRPARAKFDF KAQTLKELPL QKGDVVYIYR 1080
QIDQNWYEGE HHGRVGIFPR TYIELLPPAE KAQPRKLAPV QVLEYGEAIA KFNFNGDTQV 1140
EMSFRKGERI TLLRQVDENW YEGRIPGTSR QGIFPITYVD VLKRPLVKTP VDYIDLPYSS 1200
SPSRSATVSP QQPQAQQRRV TPDRSQPSLD LCSYQALYSY VPQNDDELEL RDGDIVDVME 1260
KCDDGWFVGT SRRTRQFGTF PGNYVKPLYL 1290 
Gene Ontology
 GO:0005913; C:cell-cell adherens junction; IDA:UniProtKB.
 GO:0005924; C:cell-substrate adherens junction; IDA:UniProtKB.
 GO:0005829; C:cytosol; IDA:BHF-UCL.
 GO:0005925; C:focal adhesion; IEA:UniProtKB-SubCell.
 GO:0045121; C:membrane raft; IDA:UniProtKB.
 GO:0016363; C:nuclear matrix; IDA:UniProtKB.
 GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
 GO:0001725; C:stress fiber; IDA:UniProtKB.
 GO:0005158; F:insulin receptor binding; IDA:UniProtKB.
 GO:0019901; F:protein kinase binding; IDA:MGI.
 GO:0048041; P:focal adhesion assembly; IDA:UniProtKB.
 GO:0015758; P:glucose transport; IDA:UniProtKB.
 GO:0008286; P:insulin receptor signaling pathway; IDA:UniProtKB.
 GO:0090004; P:positive regulation of establishment of protein localization to plasma membrane; IMP:BHF-UCL.
 GO:0046326; P:positive regulation of glucose import; IMP:BHF-UCL.
 GO:0045725; P:positive regulation of glycogen biosynthetic process; IMP:BHF-UCL.
 GO:0046889; P:positive regulation of lipid biosynthetic process; IMP:BHF-UCL.
 GO:0043149; P:stress fiber assembly; IDA:UniProtKB. 
Interpro
 IPR000108; p67phox.
 IPR011511; SH3_2.
 IPR001452; SH3_domain.
 IPR003127; Sorb. 
Pfam
 PF00018; SH3_1
 PF07653; SH3_2
 PF02208; Sorb 
SMART
 SM00326; SH3
 SM00459; Sorb 
PROSITE
 PS50002; SH3
 PS50831; SOHO 
PRINTS
 PR00499; P67PHOX.
 PR00452; SH3DOMAIN.