Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q9BX66 (SRBS1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 134. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:SORBS1
Synonyms:KIAA0894, KIAA1296, SH3D5
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1292 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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 By similarity. UniProtKB Q62417

Subunit structure

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 similarity. Interacts with the long isoform ofMLLT4/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 SH3 domain 2) with PXN. Ref.1 Ref.2 Ref.4 Ref.5

Subcellular location

Cell junctionadherens junction. Cell membrane. Cytoplasmcytoskeleton. Cell junctionfocal adhesion. Nucleus By similarity. Nucleus matrix By similarity. Note: Colocalizes with the Ten-1 ICD form of TENM1 in the nucleus By similarity. Colocalizes with actin stress fibers. Also detected at the plasma membrane and in neuronal intranuclear inclusions. Colocalized with PXN at focal adhesions during myogenic differentiation. Ref.2 Ref.5

Tissue specificity

Detected in skeletal muscle (at protein level). Widely expressed with highest levels in heart and skeletal muscle. Ref.1 Ref.5

Post-translational modification

O-glycosylated By similarity.

Sequence similarities

Contains 3 SH3 domains.

Contains 1 SoHo domain.

Sequence caution

The sequence AAB93496.1 differs from that shown. Reason: Frameshift at positions 861, 867 and 885.

The sequence BAA92534.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
   Biological processTransport
   Cellular componentCell junction
Cell membrane
Cytoplasm
Cytoskeleton
Membrane
Nucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainRepeat
SH3 domain
   PTMGlycoprotein
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcell-matrix adhesion

Traceable author statement PubMed 10085297. Source: ProtInc

cellular response to insulin stimulus

Inferred from sequence or structural similarity PubMed 11001060. Source: BHF-UCL

focal adhesion assembly

Inferred from sequence or structural similarity. Source: UniProtKB

glucose transport

Inferred from sequence or structural similarity. Source: UniProtKB

insulin receptor signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

muscle contraction

Traceable author statement. Source: Reactome

positive regulation of establishment of protein localization to plasma membrane

Inferred from sequence or structural similarity. Source: BHF-UCL

positive regulation of glucose import

Inferred from sequence or structural similarity PubMed 11001060. Source: BHF-UCL

positive regulation of glycogen biosynthetic process

Inferred from sequence or structural similarity PubMed 11001060. Source: BHF-UCL

positive regulation of lipid biosynthetic process

Inferred from sequence or structural similarity PubMed 11001060. Source: BHF-UCL

positive regulation of signal transduction

Inferred from sequence or structural similarity PubMed 9447983. Source: GOC

stress fiber assembly

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentcell-cell adherens junction

Inferred from sequence or structural similarity. Source: UniProtKB

cell-substrate adherens junction

Inferred from sequence or structural similarity. Source: UniProtKB

cytosol

Inferred from sequence or structural similarity PubMed 9447983. Source: BHF-UCL

focal adhesion

Inferred from electronic annotation. Source: UniProtKB-SubCell

membrane raft

Inferred from sequence or structural similarity. Source: UniProtKB

nuclear matrix

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred from direct assay Ref.2. Source: UniProtKB

plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

stress fiber

Inferred from sequence or structural similarity. Source: UniProtKB

zonula adherens

Traceable author statement PubMed 10085297. Source: ProtInc

   Molecular_functionSH3/SH2 adaptor activity

Inferred from sequence or structural similarity PubMed 9447983. Source: BHF-UCL

actin binding

Traceable author statement PubMed 10085297. Source: ProtInc

cytoskeletal protein binding

Traceable author statement PubMed 10085297. Source: ProtInc

insulin receptor binding

Inferred from direct assay Ref.1. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 12 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 Ref.1 (identifier: Q9BX66-1)

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.
Isoform 2 Ref.1 (identifier: Q9BX66-2)

The sequence of this isoform differs from the canonical sequence as follows:
     434-453: DNPYTPTYQFPASTPSPKSE → TKSCSVMSPRLECSGTVIAHCSLKLLDSSNPPTSASQVAGTA
     955-1117: Missing.
Note: Ref.1 (AAK37564) sequence is in conflict in positions: 435:K->E, 452-455:AHCS->SRCG, 463:N->D.
Isoform 3 Ref.1 (identifier: Q9BX66-3)

The sequence of this isoform differs from the canonical sequence as follows:
     147-215: Missing.
     408-453: Missing.
     602-635: Missing.
     956-975: FSSHSKLITPAPSSLPHSRR → LSHHSLRAGPDLTESEKSYV
     976-1213: Missing.
Isoform 4 Ref.1 (identifier: Q9BX66-4)

The sequence of this isoform differs from the canonical sequence as follows:
     26-57: Missing.
     101-109: Missing.
     148-270: Missing.
     408-453: Missing.
     552-635: Missing.
     738-793: Missing.
     955-1212: Missing.
Note: Contains a phosphoserine at position 346. Contains a phosphoserine at position 603.
Isoform 5 Ref.3 (identifier: Q9BX66-5)

The sequence of this isoform differs from the canonical sequence as follows:
     101-109: Missing.
     431-451: Missing.
     955-1212: Missing.
Note: Contains a phosphoserine at position 923.
Isoform 6 Ref.4 (identifier: Q9BX66-6)

The sequence of this isoform differs from the canonical sequence as follows:
     101-109: Missing.
     148-270: Missing.
     580-635: Missing.
     955-1212: Missing.
Note: Contains a phosphoserine at position 765.
Isoform 7 (identifier: Q9BX66-7)

The sequence of this isoform differs from the canonical sequence as follows:
     26-57: Missing.
     101-109: Missing.
     408-453: Missing.
     552-635: Missing.
     795-799: MRPAR → KYDWA
     800-1292: Missing.
Note: No experimental confirmation available. Contains a phosphoserine at position 469.
Isoform 8 Ref.2 (identifier: Q9BX66-8)

The sequence of this isoform differs from the canonical sequence as follows:
     26-57: Missing.
     148-270: Missing.
     408-453: Missing.
     580-601: Missing.
     955-1212: Missing.
Note: Contains a phosphoserine at position 730.
Isoform 9 (identifier: Q9BX66-9)

The sequence of this isoform differs from the canonical sequence as follows:
     148-270: Missing.
     408-453: Missing.
     552-635: Missing.
     955-1212: Missing.
Note: Contains a phosphoserine at position 387. Contains a phosphoserine at position 700.
Isoform 10 (identifier: Q9BX66-10)

The sequence of this isoform differs from the canonical sequence as follows:
     26-57: Missing.
     408-453: Missing.
     552-635: Missing.
     738-793: Missing.
     955-1212: Missing.
Note: No experimental confirmation available. Contains a phosphoserine at position 478. Contains a phosphoserine at position 735.
Isoform 11 (identifier: Q9BX66-11)

The sequence of this isoform differs from the canonical sequence as follows:
     408-453: Missing.
     1213-1213: Q → QLSHHSLRAGPDLTESEKSYV
Isoform 12 (identifier: Q9BX66-12)

The sequence of this isoform differs from the canonical sequence as follows:
     26-57: Missing.
     148-270: Missing.
     319-328: Missing.
     408-453: Missing.
     580-601: Missing.
     709-709: K → KVDRKGGNAH...PQSELAPSRG
     955-1212: Missing.
Note: No experimental confirmation available. Derived from mouse ortholog data. Contains a phosphoserine at position 1213.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 12921292Sorbin and SH3 domain-containing protein 1
PRO_0000072185

Regions

Domain366 – 469104SoHo
Domain793 – 85260SH3 1
Domain867 – 92862SH3 2
Domain1231 – 129262SH3 3

Amino acid modifications

Modified residue861Phosphoserine Ref.12
Modified residue891Phosphoserine Ref.12
Modified residue3691Phosphoserine By similarity
Modified residue4721Phosphoserine Ref.12
Modified residue4811Phosphoserine Ref.15
Modified residue5361Phosphotyrosine; by ABL1 By similarity
Modified residue6541Phosphotyrosine; by ABL1 By similarity
Modified residue6651Phosphoserine Ref.12
Modified residue8621Phosphothreonine Ref.12
Modified residue9451Phosphoserine Ref.12
Modified residue12401Phosphotyrosine; by ABL1 By similarity

Natural variations

Alternative sequence26 – 5732Missing in isoform 4, isoform 7, isoform 8, isoform 10 and isoform 12. Ref.1 Ref.2
VSP_050895
Alternative sequence101 – 1099Missing in isoform 4, isoform 5, isoform 6 and isoform 7. Ref.4
VSP_050896
Alternative sequence147 – 21569Missing in isoform 3. Ref.1
VSP_050898
Alternative sequence148 – 270123Missing in isoform 4, isoform 6, isoform 8, isoform 9 and isoform 12. Ref.1 Ref.2 Ref.4
VSP_050899
Alternative sequence319 – 32810Missing in isoform 12.
VSP_041193
Alternative sequence408 – 45346Missing in isoform 3, isoform 4, isoform 7, isoform 8, isoform 9, isoform 10, isoform 11 and isoform 12. Ref.1 Ref.2
VSP_050900
Alternative sequence431 – 45121Missing in isoform 5. Ref.1 Ref.2
VSP_050901
Alternative sequence434 – 45320DNPYT…SPKSE → TKSCSVMSPRLECSGTVIAH CSLKLLDSSNPPTSASQVAG TA in isoform 2. Ref.1
VSP_050902
Alternative sequence552 – 63584Missing in isoform 4, isoform 7, isoform 9 and isoform 10. Ref.1
VSP_050903
Alternative sequence580 – 63556Missing in isoform 6. Ref.4
VSP_050905
Alternative sequence580 – 60122Missing in isoform 8 and isoform 12. Ref.2
VSP_050904
Alternative sequence602 – 63534Missing in isoform 3. Ref.1
VSP_050906
Alternative sequence7091K → KVDRKGGNAHMISSSSVHSR TFNTSNALGPVCKHKKPLSA AKACISEILPSKFKPRLSAP SALLQEQKSILLPSEKAQSC ENLCVSGSLNDSKRGLPLQV GGSIENLLMRSRRDYDSKSS STMSLQEYSTSGRRPCPLSR KAGMQFTMLYRDMHQINRSG LFLGSISSSSSVRDLASHFE KSSLALSRGELGPSQEGSEH IPKHTVSSRITAFEQLIQRS RSMPSLDLSGRLSKSPTPVL SRGSLTSARSAESLLESTKL HPKEMDGMNSSGVYASPTCS NMAHHALSFRGLVPSEPLST CSDDVDRCSNISTDSREGSG GSVHGDFPKHRLNKCKGTCP ASYTRFTTIRKHEQQQTSRQ PEWRLDARGDKSTLLRNIYL MSPLPFRLKKPLHHHPRQPS PGDSSGLLVGQKPDLPSQPH QDQPPSGGKPVVPTRLSSRH TMARLSRSSEPSQERPTALE DYPRAINNGNSVPYSDHSLD RNNNPQSELAPSRG in isoform 12.
VSP_041194
Alternative sequence738 – 79356Missing in isoform 4 and isoform 10. Ref.1
VSP_050907
Alternative sequence795 – 7995MRPAR → KYDWA in isoform 7.
VSP_050908
Alternative sequence800 – 1292493Missing in isoform 7.
VSP_050909
Alternative sequence955 – 1212258Missing in isoform 4, isoform 5, isoform 6, isoform 8, isoform 9, isoform 10 and isoform 12. Ref.1 Ref.2 Ref.3 Ref.4
VSP_050911
Alternative sequence955 – 1117163Missing in isoform 2. Ref.1
VSP_050910
Alternative sequence956 – 97520FSSHS…PHSRR → LSHHSLRAGPDLTESEKSYV in isoform 3. Ref.1
VSP_050912
Alternative sequence976 – 1213238Missing in isoform 3. Ref.1
VSP_050913
Alternative sequence12131Q → QLSHHSLRAGPDLTESEKSY V in isoform 11.
VSP_039210
Natural variant611L → P. Ref.1 Ref.2 Ref.3 Ref.4 Ref.5 Ref.6 Ref.7 Ref.10
Corresponds to variant rs943542 [ dbSNP | Ensembl ].
VAR_047652
Natural variant741R → W. Ref.3
VAR_019653
Natural variant1751G → V.
Corresponds to variant rs7081076 [ dbSNP | Ensembl ].
VAR_047653
Natural variant1951T → A in a breast cancer sample; somatic mutation. Ref.18
VAR_035661
Natural variant2371T → A Has a protective role in both obesity and diabetes. Ref.3
Corresponds to variant rs2281939 [ dbSNP | Ensembl ].
VAR_019654
Natural variant4851Y → C.
Corresponds to variant rs35808802 [ dbSNP | Ensembl ].
VAR_047654

Experimental info

Sequence conflict91S → P in CAJ97431. Ref.5
Sequence conflict181P → S in AAD27647. Ref.1
Sequence conflict181P → S in AAF22175. Ref.3
Sequence conflict1101D → G in AAD27647. Ref.1
Sequence conflict1101D → G in AAF22175. Ref.3
Sequence conflict1131R → K in AAD27647. Ref.1
Sequence conflict1131R → K in AAF22175. Ref.3
Sequence conflict1311A → V in AAD27647. Ref.1
Sequence conflict1311A → V in AAF22175. Ref.3
Sequence conflict1341Y → S in AAD27647. Ref.1
Sequence conflict1341Y → S in AAF22175. Ref.3
Sequence conflict226 – 2283RAS → SAC in AAF22175. Ref.3
Sequence conflict2641T → P in AAF22175. Ref.3
Sequence conflict292 – 2954PSVS → SSEC in AAD27647. Ref.1
Sequence conflict292 – 2954PSVS → SSEC in AAF22175. Ref.3
Sequence conflict4811S → R in AAF22175. Ref.3
Sequence conflict4891E → V in AAD27647. Ref.1
Sequence conflict4891E → V in AAF22175. Ref.3
Sequence conflict6071D → E in AAF22175. Ref.3
Sequence conflict6101L → F in AAF22175. Ref.3
Sequence conflict6441E → G in AAD27647. Ref.1
Sequence conflict6441E → G in AAF22175. Ref.3
Sequence conflict6791R → S in AAD27647. Ref.1
Sequence conflict6791R → S in AAF22175. Ref.3
Sequence conflict6901D → V in AAD27647. Ref.1
Sequence conflict6901D → V in AAF22175. Ref.3
Sequence conflict6941Q → R in CAJ97431. Ref.5
Sequence conflict6951G → D in AAD27647. Ref.1
Sequence conflict6951G → D in AAF22175. Ref.3
Sequence conflict7101D → N in AAD27647. Ref.1
Sequence conflict7101D → N in AAF22175. Ref.3
Sequence conflict11561V → G in AAK37563. Ref.1
Sequence conflict11561V → G in AAK37564. Ref.1

Secondary structure

.................................... 1292
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified January 11, 2011. Version 3.
Checksum: 70DA4169B6D82F06

FASTA1,292142,513
        10         20         30         40         50         60 
MSSECDGGSK AVMNGLAPGS NGQDKATADP LRARSISAVK IIPVKTVKNA SGLVLPTDMD 

        70         80         90        100        110        120 
LTKICTGKGA VTLRASSSYR ETPSSSPASP QETRQHESKP GLEPEPSSAD EWRLSSSADA 

       130        140        150        160        170        180 
NGNAQPSSLA AKGYRSVHPN LPSDKSQDAT SSSAAQPEVI VVPLYLVNTD RGQEGTARPP 

       190        200        210        220        230        240 
TPLGPLGCVP TIPATASAAS PLTFPTLDDF IPPHLQRWPH HSQPARASGS FAPISQTPPS 

       250        260        270        280        290        300 
FSPPPPLVPP APEDLRRVSE PDLTGAVSST DSSPLLNEVS SSLIGTDSQA FPSVSKPSSA 

       310        320        330        340        350        360 
YPSTTIVNPT IVLLQHNREQ QKRLSSLSDP VSERRVGEQD SAPTQEKPTS PGKAIEKRAK 

       370        380        390        400        410        420 
DDSRRVVKST QDLSDVSMDE VGIPLRNTER SKDWYKTMFK QIHKLNRDTP EENPYFPTYK 

       430        440        450        460        470        480 
FPELPEIQQT SEEDNPYTPT YQFPASTPSP KSEDDDSDLY SPRYSFSEDT KSPLSVPRSK 

       490        500        510        520        530        540 
SEMSYIDGEK VVKRSATLPL PARSSSLKSS SERNDWEPPD KKVDTRKYRA EPKSIYEYQP 

       550        560        570        580        590        600 
GKSSVLTNEK MSRDISPEEI DLKNEPWYKF FSELEFGKPP PKKIWDYTPG DCSILPREDR 

       610        620        630        640        650        660 
KTNLDKDLSL CQTELEADLE KMETLNKAPS ANVPQSSAIS PTPEISSETP GYIYSSNFHA 

       670        680        690        700        710        720 
VKRESDGAPG DLTSLENERQ IYKSVLEGGD IPLQGLSGLK RPSSSASTKD SESPRHFIPA 

       730        740        750        760        770        780 
DYLESTEEFI RRRHDDKEKL LADQRRLKRE QEEADIAARR HTGVIPTHHQ FITNERFGDL 

       790        800        810        820        830        840 
LNIDDTAKRK SGSEMRPARA KFDFKAQTLK ELPLQKGDIV YIYKQIDQNW YEGEHHGRVG 

       850        860        870        880        890        900 
IFPRTYIELL PPAEKAQPKK LTPVQVLEYG EAIAKFNFNG DTQVEMSFRK GERITLLRQV 

       910        920        930        940        950        960 
DENWYEGRIP GTSRQGIFPI TYVDVIKRPL VKNPVDYMDL PFSSSPSRSA TASPQFSSHS 

       970        980        990       1000       1010       1020 
KLITPAPSSL PHSRRALSPE MHAVTSEWIS LTVGVPGRRS LALTPPLPPL PEASIYNTDH 

      1030       1040       1050       1060       1070       1080 
LALSPRASPS LSLSLPHLSW SDRPTPRSVA SPLALPSPHK TYSLAPTSQA SLHMNGDGGV 

      1090       1100       1110       1120       1130       1140 
HTPSSGIHQD SFLQLPLGSS DSVISQLSDA FSSQSKRQPW REESGQYERK AERGAGERGP 

      1150       1160       1170       1180       1190       1200 
GGPKISKKSC LKPSDVVRCL STEQRLSDLN TPEESRPGKP LGSAFPGSEA EQTERHRGGE 

      1210       1220       1230       1240       1250       1260 
QAGRKAARRG GSQQPQAQQR RVTPDRSQTS QDLFSYQALY SYIPQNDDEL ELRDGDIVDV 

      1270       1280       1290 
MEKCDDGWFV GTSRRTKQFG TFPGNYVKPL YL 

« Hide

Isoform 2 [UniParc].

Checksum: C1BD7AD5D5BE1300
Show »

FASTA1,151127,276
Isoform 3 [UniParc].

Checksum: C44DB4C9B0526933
Show »

FASTA905101,082
Isoform 4 [UniParc].

Checksum: 9A417161477CB810
Show »

FASTA68476,596
Isoform 5 [UniParc].

Checksum: 45A17463F7373E8B
Show »

FASTA1,004111,791
Isoform 6 [UniParc].

Checksum: 61FC1B8026A7D9A1
Show »

FASTA84695,036
Isoform 7 [UniParc].

Checksum: 4B5BD67EF6355537
Show »

FASTA62868,745
Isoform 8 [UniParc].

Checksum: 019F4E7E811AFDF5
Show »

FASTA81191,055
Isoform 9 [UniParc].

Checksum: EDB752BF6DB3E4E1
Show »

FASTA78187,199
Isoform 10 [UniParc].

Checksum: 490FCF5615BF69DB
Show »

FASTA81690,218
Isoform 11 [UniParc].

Checksum: 857F07CDCB13B97E
Show »

FASTA1,266139,401
Isoform 12 [UniParc].

Checksum: 770EBDC6412A6C03
Show »

FASTA1,294143,741

References

« Hide 'large scale' references
[1]"Cloning, mapping, and characterization of the human sorbin and SH3 domain containing 1 (SORBS1) gene: a protein associated with c-Abl during insulin signaling in the hepatoma cell line Hep3B."
Lin W.-H., Huang C.-J., Liu M.-W., Chang H.-M., Chen Y.-J., Tai T.-Y., Chuang L.-M.
Genomics 74:12-20(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3 AND 4), TISSUE SPECIFICITY, INTERACTION WITH ABL1 AND INSULIN RECEPTOR, VARIANT PRO-61.
Tissue: Liver and Skeletal muscle.
[2]"Ataxin-7 interacts with a Cbl-associated protein that it recruits into neuronal intranuclear inclusions."
Lebre A.-S., Jamot L., Takahashi J., Spassky N., Leprince C., Ravise N., Zander C., Fujigasaki H., Kussel-Andermann P., Duyckaerts C., Camonis J.H., Brice A.
Hum. Mol. Genet. 10:1201-1213(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 8), SUBCELLULAR LOCATION, INTERACTION WITH SCA7, VARIANT PRO-61.
Tissue: Retina.
[3]"Molecular scanning of the human sorbin and SH3-domain-containing-1 (SORBS1) gene: positive association of the T228A polymorphism with obesity and type 2 diabetes."
Lin W.-H., Chiu K.C., Chang H.-M., Lee K.C., Tai T.-Y., Chuang L.-M.
Hum. Mol. Genet. 10:1753-1760(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5), VARIANTS PRO-61; TRP-74 AND ALA-237.
Tissue: Skeletal muscle.
[4]"The c-Cbl-associated protein and c-Cbl are two new partners of the SH2-containing inositol polyphosphate 5-phosphatase SHIP2."
Vandenbroere I., Paternotte N., Dumont J.E., Erneux C., Pirson I.
Biochem. Biophys. Res. Commun. 300:494-500(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 6), INTERACTION WITH INPPL1, VARIANT PRO-61.
Tissue: Brain.
[5]"Paxillin and ponsin interact in nascent costameres of muscle cells."
Gehmlich K., Pinotsis N., Hayess K., van der Ven P.F., Milting H., El Banayosy A., Korfer R., Wilmanns M., Ehler E., Furst D.O.
J. Mol. Biol. 369:665-682(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 11), INTERACTION WITH PXN, X-RAY CRYSTALLOGRAPHY (0.83 ANGSTROMS) OF 870-930 IN COMPLEX WITH PXN PEPTIDE, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, VARIANT PRO-61.
Tissue: Skeletal muscle.
[6]"Prediction of the coding sequences of unidentified human genes. XVI. The complete sequences of 150 new cDNA clones from brain which code for large proteins in vitro."
Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.
DNA Res. 7:65-73(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 9), VARIANT PRO-61.
Tissue: Brain.
[7]"Towards a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs."
Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S., Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W., Ottenwaelder B., Obermaier B. expand/collapse author list , Tampe J., Heubner D., Wambutt R., Korn B., Klein M., Poustka A.
Genome Res. 11:422-435(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 10), VARIANT PRO-61.
Tissue: Uterus.
[8]"The DNA sequence and comparative analysis of human chromosome 10."
Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J. expand/collapse author list , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[9]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[10]"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] (ISOFORMS 7 AND 9), VARIANT PRO-61.
Tissue: Testis.
[11]"A Fas-ligand associated factor 2, FLAF2, potentiates Fas-ligand stability."
Hachiya T., Kobayasi A., Touji S., Tamai K.
Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 752-888.
Tissue: Placenta.
[12]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-86; SER-89; SER-472; SER-665; THR-862 AND SER-945, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-478 AND SER-735 (ISOFORM 10), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1213 (ISOFORM 12), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-346 AND SER-603 (ISOFORM 4), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-923 (ISOFORM 5), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-765 (ISOFORM 6), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-469 (ISOFORM 7), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-730 (ISOFORM 8), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-387 AND SER-700 (ISOFORM 9), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[13]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[15]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-481, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[16]"Second SH3 domain of ponsin solved from powder diffraction."
Margiolaki I., Wright J.P., Wilmanns M., Fitch A.N., Pinotsis N.
J. Am. Chem. Soc. 129:11865-11871(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 870-930.
[17]"Solution structure of SH3 domains of human Sorbin and SH3 domain-containing protein 1."
RIKEN structural genomics initiative (RSGI)
Submitted (FEB-2009) to the PDB data bank
Cited for: STRUCTURE BY NMR OF 796-926.
[18]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] ALA-195.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF136380 mRNA. Translation: AAD27647.1.
AF356525 mRNA. Translation: AAK37563.1.
AF356526 mRNA. Translation: AAK37564.1.
AF356527 mRNA. Translation: AAK37565.1.
AF330623 mRNA. Translation: AAK57479.1.
AF330624 mRNA. Translation: AAK57480.1.
AF136381 mRNA. Translation: AAF22175.1.
AJ489942 mRNA. Translation: CAD34588.1.
AM260536 mRNA. Translation: CAJ97431.1.
AB037717 mRNA. Translation: BAA92534.1. Different initiation.
AL117472 mRNA. Translation: CAB55947.1.
AL158165 Genomic DNA. Translation: CAI14378.1.
AL158165 Genomic DNA. Translation: CAI14379.1.
AL158165 Genomic DNA. Translation: CAI14380.1.
AL158165 Genomic DNA. Translation: CAI14381.1.
AL158165 Genomic DNA. Translation: CAI14382.1.
AL158165 Genomic DNA. Translation: CAI14383.1.
AL158165 Genomic DNA. Translation: CAI14384.1.
AL158165 Genomic DNA. Translation: CAI14385.1.
CH471066 Genomic DNA. Translation: EAW49999.1.
CH471066 Genomic DNA. Translation: EAW50007.1.
BC042612 mRNA. Translation: AAH42612.1.
BC152463 mRNA. Translation: AAI52464.1.
U70668 mRNA. Translation: AAB93496.1. Frameshift.
PIRT17257.
RefSeqNP_001030126.1. NM_001034954.1.
NP_001030127.1. NM_001034955.1.
NP_001030128.1. NM_001034956.1.
NP_001030129.1. NM_001034957.1.
NP_006425.2. NM_006434.2.
NP_056200.1. NM_015385.2.
NP_079267.1. NM_024991.1.
XP_005269484.1. XM_005269427.1.
UniGeneHs.38621.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2DL3NMR-A791-850[»]
2ECZNMR-A870-926[»]
2LJ0NMR-A1228-1292[»]
2LJ1NMR-A1228-1291[»]
2O2WX-ray2.27A870-930[»]
2O31X-ray1.50A870-930[»]
2O9SX-ray0.83A870-930[»]
2O9VX-ray1.63A870-930[»]
ProteinModelPortalQ9BX66.
SMRQ9BX66. Positions 791-930, 1228-1292.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115831. 27 interactions.
IntActQ9BX66. 25 interactions.
MINTMINT-2792261.

PTM databases

PhosphoSiteQ9BX66.

Polymorphism databases

DMDM317373504.

Proteomic databases

PaxDbQ9BX66.
PRIDEQ9BX66.

Protocols and materials databases

DNASU10580.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000277982; ENSP00000277982; ENSG00000095637. [Q9BX66-2]
ENST00000306402; ENSP00000302556; ENSG00000095637. [Q9BX66-9]
ENST00000347291; ENSP00000277985; ENSG00000095637. [Q9BX66-6]
ENST00000353505; ENSP00000343998; ENSG00000095637. [Q9BX66-3]
ENST00000354106; ENSP00000277984; ENSG00000095637. [Q9BX66-5]
ENST00000361941; ENSP00000355136; ENSG00000095637. [Q9BX66-1]
ENST00000371227; ENSP00000360271; ENSG00000095637. [Q9BX66-11]
ENST00000371239; ENSP00000360283; ENSG00000095637. [Q9BX66-8]
ENST00000371241; ENSP00000360285; ENSG00000095637. [Q9BX66-4]
ENST00000371245; ENSP00000360291; ENSG00000095637. [Q9BX66-3]
ENST00000371246; ENSP00000360292; ENSG00000095637. [Q9BX66-2]
ENST00000371247; ENSP00000360293; ENSG00000095637. [Q9BX66-1]
ENST00000371249; ENSP00000360295; ENSG00000095637. [Q9BX66-10]
ENST00000393949; ENSP00000377521; ENSG00000095637. [Q9BX66-5]
ENST00000607232; ENSP00000475901; ENSG00000095637. [Q9BX66-12]
GeneID10580.
KEGGhsa:10580.
UCSCuc001kkl.3. human. [Q9BX66-5]
uc001kkm.3. human. [Q9BX66-6]
uc001kkn.3. human. [Q9BX66-8]
uc001kko.3. human. [Q9BX66-2]
uc001kkp.3. human. [Q9BX66-1]
uc001kkq.3. human. [Q9BX66-3]
uc001kkr.3. human. [Q9BX66-9]
uc001kks.3. human. [Q9BX66-4]
uc001kkv.3. human. [Q9BX66-10]
uc001kkw.3. human. [Q9BX66-11]

Organism-specific databases

CTD10580.
GeneCardsGC10M097061.
HGNCHGNC:14565. SORBS1.
HPAHPA027559.
HPA036994.
HPA043084.
MIM605264. gene.
neXtProtNX_Q9BX66.
PharmGKBPA37899.
HUGESearch...
Search...
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG256936.
HOVERGENHBG053053.
InParanoidQ9BX66.
KOK06086.
OMAITSEWIS.
OrthoDBEOG75XGKP.
PhylomeDBQ9BX66.
TreeFamTF320680.

Enzyme and pathway databases

ReactomeREACT_17044. Muscle contraction.
SignaLinkQ9BX66.

Gene expression databases

ArrayExpressQ9BX66.
BgeeQ9BX66.
GenevestigatorQ9BX66.

Family and domain databases

InterProIPR028506. CAP/ponsin.
IPR011511. SH3_2.
IPR001452. SH3_domain.
IPR003127. Sorb.
[Graphical view]
PANTHERPTHR10661:SF4. PTHR10661:SF4. 1 hit.
PfamPF07653. SH3_2. 1 hit.
PF02208. Sorb. 1 hit.
[Graphical view]
SMARTSM00326. SH3. 3 hits.
SM00459. Sorb. 1 hit.
[Graphical view]
SUPFAMSSF50044. SSF50044. 3 hits.
PROSITEPS50002. SH3. 3 hits.
PS50831. SOHO. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSSORBS1. human.
EvolutionaryTraceQ9BX66.
GeneWikiSORBS1.
GenomeRNAi10580.
NextBio40165.
PROQ9BX66.
SOURCESearch...

Entry information

Entry nameSRBS1_HUMAN
AccessionPrimary (citable) accession number: Q9BX66
Secondary accession number(s): A0AED4 expand/collapse secondary AC list , A6NEK3, A6NID8, A6NJS4, A7MD40, D3DR42, O43857, Q5T923, Q5T924, Q5T927, Q5T928, Q5T929, Q5T930, Q5T931, Q5T932, Q7LBE5, Q8IVK0, Q8IVQ4, Q96KF3, Q96KF4, Q9BX64, Q9BX65, Q9P2Q0, Q9UFT2, Q9UHN7, Q9Y338
Entry history
Integrated into UniProtKB/Swiss-Prot: August 31, 2004
Last sequence update: January 11, 2011
Last modified: April 16, 2014
This is version 134 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 10

Human chromosome 10: entries, gene names and cross-references to MIM