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Protein

Sorbin and SH3 domain-containing protein 1

Gene

Sorbs1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.3 Publications

GO - Molecular functioni

  • insulin receptor binding Source: UniProtKB
  • protein kinase binding Source: MGI
  • SH3/SH2 adaptor activity Source: BHF-UCL
  • transcription factor binding Source: UniProtKB

GO - Biological processi

  • cellular response to insulin stimulus Source: BHF-UCL
  • focal adhesion assembly Source: UniProtKB
  • glucose transport Source: UniProtKB
  • insulin receptor signaling pathway Source: UniProtKB
  • positive regulation of establishment of protein localization to plasma membrane Source: BHF-UCL
  • positive regulation of glucose import Source: BHF-UCL
  • positive regulation of glycogen biosynthetic process Source: BHF-UCL
  • positive regulation of lipid biosynthetic process Source: BHF-UCL
  • stress fiber assembly Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Transport

Names & Taxonomyi

Protein namesi
Recommended name:
Sorbin and SH3 domain-containing protein 1
Alternative name(s):
Ponsin
SH3 domain protein 5
SH3P12
c-Cbl-associated protein
Short name:
CAP
Gene namesi
Name:Sorbs1Imported
Synonyms:Kiaa1296Imported, Sh3d51 Publication
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Unplaced

Organism-specific databases

MGIiMGI:700014. Sorbs1.

Subcellular locationi

GO - Cellular componenti

  • cell-cell adherens junction Source: UniProtKB
  • cell-substrate adherens junction Source: UniProtKB
  • centrosome Source: MGI
  • cytoplasm Source: MGI
  • cytoskeleton Source: UniProtKB
  • cytosol Source: BHF-UCL
  • focal adhesion Source: MGI
  • membrane Source: BHF-UCL
  • membrane raft Source: UniProtKB
  • nuclear matrix Source: UniProtKB
  • nucleoplasm Source: MGI
  • nucleus Source: UniProtKB
  • plasma membrane Source: MGI
  • stress fiber Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Cytoplasm, Cytoskeleton, Membrane, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 12901290Sorbin and SH3 domain-containing protein 1PRO_0000072186Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei51 – 511PhosphothreonineCombined sources
Modified residuei55 – 551PhosphoserineCombined sources
Modified residuei58 – 581PhosphoserineCombined sources
Modified residuei62 – 621PhosphoserineCombined sources
Modified residuei179 – 1791PhosphothreonineCombined sources
Modified residuei185 – 1851PhosphoserineCombined sources
Modified residuei204 – 2041PhosphoserineCombined sources
Modified residuei209 – 2091PhosphoserineCombined sources
Modified residuei254 – 2541PhosphoserineBy similarity
Modified residuei261 – 2611PhosphoserineCombined sources
Modified residuei270 – 2701PhosphoserineCombined sources
Modified residuei325 – 3251Phosphotyrosine; by ABL11 Publication
Modified residuei345 – 3451PhosphoserineCombined sources
Modified residuei376 – 3761PhosphoserineCombined sources
Modified residuei407 – 4071PhosphoserineCombined sources
Modified residuei421 – 4211Phosphotyrosine; by ABL11 Publication
Modified residuei432 – 4321PhosphoserineCombined sources
Modified residuei475 – 4751PhosphothreonineBy similarity
Modified residuei969 – 9691PhosphoserineCombined sources
Modified residuei1189 – 11891PhosphothreonineCombined sources
Modified residuei1193 – 11931PhosphotyrosineBy similarity
Modified residuei1198 – 11981PhosphotyrosineCombined sources
Modified residuei1201 – 12011PhosphoserineCombined sources
Modified residuei1209 – 12091PhosphoserineCombined sources
Modified residuei1238 – 12381Phosphotyrosine; by ABL11 Publication
Isoform 21 Publication (identifier: Q62417-2)
Modified residuei164 – 1641PhosphoserineCombined sources
Modified residuei346 – 3461PhosphoserineCombined sources
Isoform 52 Publications (identifier: Q62417-5)
Modified residuei164 – 1641PhosphoserineCombined sources
Modified residuei346 – 3461PhosphoserineCombined sources
Isoform 6Curated (identifier: Q62417-6)
Modified residuei175 – 1751PhosphoserineCombined sourcesCurated
Modified residuei357 – 3571PhosphoserineCombined sourcesCurated
Isoform 41 Publication (identifier: Q62417-4)
Modified residuei194 – 1941PhosphoserineCombined sources
Modified residuei376 – 3761PhosphoserineCombined sources
Isoform 7Curated (identifier: Q62417-7)
Modified residuei288 – 2881PhosphoserineCombined sourcesCurated
Modified residuei470 – 4701PhosphoserineCombined sourcesCurated

Post-translational modificationi

O-glycosylated.1 Publication

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

EPDiQ62417.
MaxQBiQ62417.
PeptideAtlasiQ62417.
PRIDEiQ62417.

PTM databases

iPTMnetiQ62417.
PhosphoSiteiQ62417.

Expressioni

Tissue specificityi

Expressed in all tissues tested: heart, brain, spleen, lung, liver, muscle, kidney and testis. Expressed in 3T3-L1 adipocytes but not in 3T3-L1 fibroblasts.2 Publications

Gene expression databases

CleanExiMM_SORBS1.

Interactioni

Subunit structurei

Interacts (via SH3 domain 2) with PXN (By similarity). Interacts with the long isoform of MLLT4/afadin and with VCL. MLLT4 and VCL bind to SORBS1 in a competitive manner and do not form a ternary complex. Interacts with ABL1, CBL, CBLB and INPPL1/SHIP2 through the third SH3 domain. Interaction with ABL1 occurs only after insulin stimulation while this has no effect on the interaction with INPPL1. Interacts with the insulin receptor but dissociates from it following insulin stimulation. Also interacts with SCA7, PTK2/FAK1 and flotillin. Interacts (via third SH3 domain) with the Ten-1 ICD form of TENM1; the interaction induces the translocation of SORBS1 to the nucleus. Interacts with INSM1.By similarity7 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
PXNP490238EBI-7072893,EBI-702209From a different organism.
VCLP182063EBI-7072893,EBI-716775From a different organism.

GO - Molecular functioni

  • insulin receptor binding Source: UniProtKB
  • protein kinase binding Source: MGI
  • SH3/SH2 adaptor activity Source: BHF-UCL
  • transcription factor binding Source: UniProtKB

Protein-protein interaction databases

BioGridi203213. 9 interactions.
IntActiQ62417. 6 interactions.
MINTiMINT-1342490.

Structurei

3D structure databases

ProteinModelPortaliQ62417.
SMRiQ62417. Positions 1047-1186, 1226-1290.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini202 – 24746SoHoPROSITE-ProRule annotationAdd
BLAST
Domaini1049 – 110860SH3 1PROSITE-ProRule annotationAdd
BLAST
Domaini1123 – 118462SH3 2PROSITE-ProRule annotationAdd
BLAST
Domaini1236 – 129055SH3 3PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 3 SH3 domains.PROSITE-ProRule annotation
Contains 1 SoHo domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, SH3 domain

Phylogenomic databases

HOVERGENiHBG053053.
InParanoidiQ62417.
KOiK06086.
PhylomeDBiQ62417.

Family and domain databases

InterProiIPR028506. CAP/ponsin.
IPR011511. SH3_2.
IPR001452. SH3_domain.
IPR003127. SoHo_dom.
[Graphical view]
PANTHERiPTHR10663:SF202. PTHR10663:SF202. 1 hit.
PfamiPF00018. SH3_1. 1 hit.
PF07653. SH3_2. 1 hit.
PF14604. SH3_9. 1 hit.
PF02208. Sorb. 1 hit.
[Graphical view]
PRINTSiPR00452. SH3DOMAIN.
SMARTiSM00326. SH3. 3 hits.
SM00459. Sorb. 1 hit.
[Graphical view]
SUPFAMiSSF50044. SSF50044. 3 hits.
PROSITEiPS50002. SH3. 3 hits.
PS50831. SOHO. 1 hit.
[Graphical view]

Sequences (7)i

Sequence statusi: Complete.

This entry describes 7 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1Curated (identifier: Q62417-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MSSECDVGSS KAVVNGLASG NHGPDKDMDP TKICTGKGTV TLRASSSYRG
60 70 80 90 100
TPSSSPVSPQ ESPKHESKSG LEPEDPSADE WKLSSSADTN GNAQPSPLAA
110 120 130 140 150
KGYRSVHPSL SADKPQGSPL LNEVSSSHIE TDSQDFPPTS RPSSAYPSTT
160 170 180 190 200
IVNPTIVLLQ HNRDPASERR AGEQDPVPTP AELTSPGRAS ERRAKDASRR
210 220 230 240 250
VVRSAQDLSD VSTDEVGIPL RNTERSKDWY KTMFKQIHKL NRDDDSDVHS
260 270 280 290 300
PRYSFSDDTK SPLSVPRSKS EMNYIEGEKV VKRSATLPLP ARSSSLKSSP
310 320 330 340 350
ERNDWEPLDK KVDTRKYRAE PKSIYEYQPG KSSVLTNEKM SRDISPEEID
360 370 380 390 400
LKNEPWYKFF SELEFGRPTN LEKDLSFCQA ELEADLEKVE TVNKSPSANS
410 420 430 440 450
PQSSAVSPTP DITSEPPGYI YSSNFHAVKR ESDGTPGGLA SLENERQIYK
460 470 480 490 500
SVLEGGDIPL QGLSGLKRPS SSASTKVDRK GGNAHMISSS SVHSRTFHTS
510 520 530 540 550
NALGPGCKHK KPLSAAKACI SEILPSKFKP RLSAPSALLQ EQKSVLLPSE
560 570 580 590 600
KAQSCENLCV SLNDSKRGLP LRVGGSIENL LMRSRRDYDS KSSSTMSLQE
610 620 630 640 650
YGTSSRRPCP LSRKAGLHFS MFYRDMHQIN RAGLSLGSIS SSSVRDLASH
660 670 680 690 700
FERSSLTLAR GELGASQEGS EHIPKHTVSS RITAFEQLIQ RSRSMPSLDF
710 720 730 740 750
SGRLSKSPTP VLSRSGLTSA RSAESLLEST KLRPREMDGM DSGGVYASPT
760 770 780 790 800
CSNMADHALS FRSLVPSEPL SICSDELDHC SNVSNDSREG SGGSVHGDFP
810 820 830 840 850
KHRLNKCKGT CPASYTRFTT IRKHEQQSSR QSDWRSDSRG DKNSLLRNIH
860 870 880 890 900
LMSPLPFRLK KPLQQHPRQP PPSDSSESPA GQKADLPCHD PQDQPHSAGK
910 920 930 940 950
PQVPTRLSSR HTMARLSHNS EPPLDRPAGL EDCTRAINNG NPVPYSDHGL
960 970 980 990 1000
DRNNNPQSEL AAAHGDSESP RHFIPADYLE STEEFIRRRH DDKEKLLADQ
1010 1020 1030 1040 1050
RRLKREQEEA DIAARRHTGV IPTHHQFITN ERFGDLLNID DTAKRKSGLE
1060 1070 1080 1090 1100
MRPARAKFDF KAQTLKELPL QKGDVVYIYR QIDQNWYEGE HHGRVGIFPR
1110 1120 1130 1140 1150
TYIELLPPAE KAQPRKLAPV QVLEYGEAIA KFNFNGDTQV EMSFRKGERI
1160 1170 1180 1190 1200
TLLRQVDENW YEGRIPGTSR QGIFPITYVD VLKRPLVKTP VDYIDLPYSS
1210 1220 1230 1240 1250
SPSRSATVSP QQPQAQQRRV TPDRSQPSLD LCSYQALYSY VPQNDDELEL
1260 1270 1280 1290
RDGDIVDVME KCDDGWFVGT SRRTRQFGTF PGNYVKPLYL
Note: No experimental confirmation available.Curated
Length:1,290
Mass (Da):143,070
Last modified:August 16, 2004 - v2
Checksum:i07C9A74BD794E390
GO
Isoform 21 Publication (identifier: Q62417-2) [UniParc]FASTAAdd to basket

Also known as: CAPsm1 Publication

The sequence of this isoform differs from the canonical sequence as follows:
     70-78: Missing.
     163-163: R → REQQKRLSSLS
     341-402: Missing.
     477-965: Missing.

Show »
Length:740
Mass (Da):82,861
Checksum:i9C221599664DB85C
GO
Isoform 31 Publication (identifier: Q62417-3) [UniParc]FASTAAdd to basket

Also known as: Ponsin-21 Publication

The sequence of this isoform differs from the canonical sequence as follows:
     70-78: Missing.
     369-402: TNLEKDLSFCQAELEADLEKVETVNKSPSANSPQ → PPKKIWDYTPGDCSILPREDRK
     477-965: Missing.
     994-1049: Missing.

Show »
Length:724
Mass (Da):81,221
Checksum:iFF4207C056D47054
GO
Isoform 41 Publication (identifier: Q62417-4) [UniParc]FASTAAdd to basket

Also known as: Ponsin-11 Publication

The sequence of this isoform differs from the canonical sequence as follows:
     26-26: K → KADPFRARSISAVKIIPVKTVKSPSGLVLPP
     70-78: Missing.
     163-163: R → REQQKRLSSLS
     341-402: Missing.
     477-965: Missing.
     994-1049: Missing.

Show »
Length:714
Mass (Da):79,497
Checksum:iE2804F966844351A
GO
Isoform 52 Publications (identifier: Q62417-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     70-78: Missing.
     163-163: R → REQQKRLSSLS
     341-402: Missing.
     477-965: Missing.
     994-1049: Missing.

Show »
Length:684
Mass (Da):76,370
Checksum:i8451FC615848E3FC
GO
Isoform 6Curated (identifier: Q62417-6) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     70-78: Missing.
     117-117: G → GATSSSSAPSEG
     163-163: R → REQQKRLSSLS
     341-402: Missing.
     477-965: Missing.
     994-1049: Missing.

Note: No experimental confirmation available.Combined sourcesCurated
Show »
Length:695
Mass (Da):77,332
Checksum:iF48F3C7A8FBC1296
GO
Isoform 7Curated (identifier: Q62417-7) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     70-78: Missing.
     117-117: G → GATSSSSAPS...DLPGAVSSTG
     163-163: R → REQQKRLSSLS
     341-402: Missing.
     477-965: Missing.
     1212-1290: QPQAQQRRVT...PGNYVKPLYL → VSKLSNSACS...FFSYMSVAFS

Note: No experimental confirmation available.Combined sourcesCurated
Show »
Length:836
Mass (Da):92,037
Checksum:iF00A88619166D705
GO

Sequence cautioni

The sequence BAC65769.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti205 – 2051A → T in BAC28980 (PubMed:16141072).Curated
Sequence conflicti308 – 3081L → P in BAC28980 (PubMed:16141072).Curated
Sequence conflicti1004 – 10041K → M in AAM77354 (PubMed:15047181).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei26 – 261K → KADPFRARSISAVKIIPVKT VKSPSGLVLPP in isoform 4. 1 PublicationVSP_050885
Alternative sequencei70 – 789Missing in isoform 2, isoform 3, isoform 4, isoform 5, isoform 6 and isoform 7. 6 PublicationsVSP_050886
Alternative sequencei117 – 1171G → GATSSSSAPSEG in isoform 6. 1 PublicationVSP_050887
Alternative sequencei117 – 1171G → GATSSSSAPSEVIVVPLYLV NTDRGQGQEGTARTPASLGP LGCVHTVPATTPAASPLTFP TLDDFIPPHLQRRPHHSQPA SACGSLSPASQTSPPSPPPP LVPPVPEDLHRGLEPDLPGA VSSTG in isoform 7. 1 PublicationVSP_050888
Alternative sequencei163 – 1631R → REQQKRLSSLS in isoform 2, isoform 4, isoform 5, isoform 6 and isoform 7. 6 PublicationsVSP_050889
Alternative sequencei341 – 40262Missing in isoform 2, isoform 4, isoform 5, isoform 6 and isoform 7. 6 PublicationsVSP_050890Add
BLAST
Alternative sequencei369 – 40234TNLEK…ANSPQ → PPKKIWDYTPGDCSILPRED RK in isoform 3. 1 PublicationVSP_050891Add
BLAST
Alternative sequencei477 – 965489Missing in isoform 2, isoform 3, isoform 4, isoform 5, isoform 6 and isoform 7. 6 PublicationsVSP_050892Add
BLAST
Alternative sequencei994 – 104956Missing in isoform 3, isoform 4, isoform 5 and isoform 6. 4 PublicationsVSP_050893Add
BLAST
Alternative sequencei1212 – 129079QPQAQ…KPLYL → VSKLSNSACSFHPQLCQRHT ALLGLLFHALIKSYLEQAGW EFFSYMSVAFS in isoform 7. 1 PublicationVSP_050894Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U58883 mRNA. Translation: AAC71776.1.
AF078666 mRNA. Translation: AAD16007.1.
AF078667 mRNA. Translation: AAD16008.1.
AF521593 mRNA. Translation: AAM77354.1.
AK122487 mRNA. Translation: BAC65769.2. Different initiation.
AK035212 mRNA. Translation: BAC28980.1.
BC012703 mRNA. Translation: AAH12703.1.
CCDSiCCDS37978.1. [Q62417-3]
CCDS37979.1. [Q62417-2]
CCDS37981.1. [Q62417-4]
RefSeqiNP_001030134.1. NM_001034962.1.
NP_001030135.1. NM_001034963.1.
NP_001030136.1. NM_001034964.1.
UniGeneiMm.210815.
Mm.440351.
Mm.489013.

Genome annotation databases

GeneIDi20411.
KEGGimmu:20411.
UCSCiuc008hkr.1. mouse. [Q62417-1]
uc008hks.1. mouse. [Q62417-6]
uc008hkt.1. mouse. [Q62417-7]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U58883 mRNA. Translation: AAC71776.1.
AF078666 mRNA. Translation: AAD16007.1.
AF078667 mRNA. Translation: AAD16008.1.
AF521593 mRNA. Translation: AAM77354.1.
AK122487 mRNA. Translation: BAC65769.2. Different initiation.
AK035212 mRNA. Translation: BAC28980.1.
BC012703 mRNA. Translation: AAH12703.1.
CCDSiCCDS37978.1. [Q62417-3]
CCDS37979.1. [Q62417-2]
CCDS37981.1. [Q62417-4]
RefSeqiNP_001030134.1. NM_001034962.1.
NP_001030135.1. NM_001034963.1.
NP_001030136.1. NM_001034964.1.
UniGeneiMm.210815.
Mm.440351.
Mm.489013.

3D structure databases

ProteinModelPortaliQ62417.
SMRiQ62417. Positions 1047-1186, 1226-1290.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi203213. 9 interactions.
IntActiQ62417. 6 interactions.
MINTiMINT-1342490.

PTM databases

iPTMnetiQ62417.
PhosphoSiteiQ62417.

Proteomic databases

EPDiQ62417.
MaxQBiQ62417.
PeptideAtlasiQ62417.
PRIDEiQ62417.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi20411.
KEGGimmu:20411.
UCSCiuc008hkr.1. mouse. [Q62417-1]
uc008hks.1. mouse. [Q62417-6]
uc008hkt.1. mouse. [Q62417-7]

Organism-specific databases

CTDi10580.
MGIiMGI:700014. Sorbs1.
RougeiSearch...

Phylogenomic databases

HOVERGENiHBG053053.
InParanoidiQ62417.
KOiK06086.
PhylomeDBiQ62417.

Miscellaneous databases

ChiTaRSiSorbs1. mouse.
PROiQ62417.
SOURCEiSearch...

Gene expression databases

CleanExiMM_SORBS1.

Family and domain databases

InterProiIPR028506. CAP/ponsin.
IPR011511. SH3_2.
IPR001452. SH3_domain.
IPR003127. SoHo_dom.
[Graphical view]
PANTHERiPTHR10663:SF202. PTHR10663:SF202. 1 hit.
PfamiPF00018. SH3_1. 1 hit.
PF07653. SH3_2. 1 hit.
PF14604. SH3_9. 1 hit.
PF02208. Sorb. 1 hit.
[Graphical view]
PRINTSiPR00452. SH3DOMAIN.
SMARTiSM00326. SH3. 3 hits.
SM00459. Sorb. 1 hit.
[Graphical view]
SUPFAMiSSF50044. SSF50044. 3 hits.
PROSITEiPS50002. SH3. 3 hits.
PS50831. SOHO. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning of ligand targets: systematic isolation of SH3 domain-containing proteins."
    Sparks A.B., Hoffman N.G., McConnell S.J., Fowlkes D.M., Kay B.K.
    Nat. Biotechnol. 14:741-744(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5).
    Tissue: Embryo1 Publication.
  2. "A novel, multifunctional c-Cbl binding protein in insulin receptor signaling in 3T3-L1 adipocytes."
    Ribon V., Printen J.A., Hoffman N.G., Kay B.K., Saltiel A.R.
    Mol. Cell. Biol. 18:872-879(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5), FUNCTION, TISSUE SPECIFICITY, INTERACTION WITH CBL AND INSULIN RECEPTOR.
  3. "Ponsin/SH3P12: an l-afadin- and vinculin-binding protein localized at cell-cell and cell-matrix adherens junctions."
    Mandai K., Nakanishi H., Satoh A., Takahashi K., Satoh K., Nishioka H., Mizoguchi A., Takai Y.
    J. Cell Biol. 144:1001-1017(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3 AND 4), SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INTERACTION WITH MLLT4 AND VCL.
    Tissue: Brain1 Publication.
  4. "cDNA cloning and functional characterization of a novel splice variant of c-Cbl-associated protein from mouse skeletal muscle."
    Alcazar O., Ho R.C., Fujii N., Goodyear L.J.
    Biochem. Biophys. Res. Commun. 317:285-293(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
  5. "Prediction of the coding sequences of mouse homologues of KIAA gene: II. The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
    Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S., Nakajima D., Nagase T., Ohara O., Koga H.
    DNA Res. 10:35-48(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Fetal brain.
  6. Okazaki N., Kikuno R., Nagase T., Ohara O., Koga H.
    Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION.
  7. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 7).
    Strain: C57BL/6J.
    Tissue: Urinary bladder.
  8. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 6).
    Strain: FVB/NImported.
    Tissue: Mammary glandImported.
  9. "A role for CAP, a novel, multifunctional Src homology 3 domain-containing protein in formation of actin stress fibers and focal adhesions."
    Ribon V., Herrera R., Kay B.K., Saltiel A.R.
    J. Biol. Chem. 273:4073-4080(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH PTK2/FAK1.
  10. "CAP defines a second signalling pathway required for insulin-stimulated glucose transport."
    Baumann C.A., Ribon V., Kanzaki M., Thurmond D.C., Mora S., Shigematsu S., Bickel P.E., Pessin J.E., Saltiel A.R.
    Nature 407:202-207(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH FLOTILLIN.
  11. "The zinc-finger transcription factor INSM1 is expressed during embryo development and interacts with the Cbl-associated protein."
    Xie J., Cai T., Zhang H., Lan M.S., Notkins A.L.
    Genomics 80:54-61(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH INSM1.
  12. "The roles of Cbl-b and c-Cbl in insulin-stimulated glucose transport."
    Liu J., DeYoung S.M., Hwang J.B., O'Leary E.E., Saltiel A.R.
    J. Biol. Chem. 278:36754-36762(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CBLB.
  13. "The intracellular domain of teneurin-1 interacts with MBD1 and CAP/ponsin resulting in subcellular codistribution and translocation to the nuclear matrix."
    Nunes S.M., Ferralli J., Choi K., Brown-Luedi M., Minet A.D., Chiquet-Ehrismann R.
    Exp. Cell Res. 305:122-132(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TENM1, SUBCELLULAR LOCATION.
  14. "Comprehensive identification of phosphorylation sites in postsynaptic density preparations."
    Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.
    Mol. Cell. Proteomics 5:914-922(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain.
  15. "O-linked N-acetylglucosamine proteomics of postsynaptic density preparations using lectin weak affinity chromatography and mass spectrometry."
    Vosseller K., Trinidad J.C., Chalkley R.J., Specht C.G., Thalhammer A., Lynn A.J., Snedecor J.O., Guan S., Medzihradszky K.F., Maltby D.A., Schoepfer R., Burlingame A.L.
    Mol. Cell. Proteomics 5:923-934(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS].
    Tissue: Brain.
  16. "Qualitative and quantitative analyses of protein phosphorylation in naive and stimulated mouse synaptosomal preparations."
    Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F., Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B., Panse C., Schlapbach R., Mansuy I.M.
    Mol. Cell. Proteomics 6:283-293(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain cortex.
  17. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-204, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  18. "Cbl-associated protein is tyrosine phosphorylated by c-Abl and c-Src kinases."
    Fernow I., Tomasovic A., Siehoff-Icking A., Tikkanen R.
    BMC Cell Biol. 10:80-80(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT TYR-325; TYR-421 AND TYR-1238.
  19. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-51; SER-55; SER-58; SER-62; THR-179; SER-185; SER-204; SER-209; SER-261; SER-270; SER-345; SER-376; SER-407; SER-432; SER-969; THR-1189; TYR-1198; SER-1201 AND SER-1209, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-164 AND SER-346 (ISOFORMS 2 AND 5), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-194 AND SER-376 (ISOFORM 4), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-175 AND SER-357 (ISOFORM 6), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-288 AND SER-470 (ISOFORM 7), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.

Entry informationi

Entry nameiSRBS1_MOUSE
AccessioniPrimary (citable) accession number: Q62417
Secondary accession number(s): Q80TF8
, Q8BZI3, Q8K3Y2, Q921F8, Q9Z0Z8, Q9Z0Z9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 31, 2004
Last sequence update: August 16, 2004
Last modified: July 6, 2016
This is version 141 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.