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Protein

Sorbin and SH3 domain-containing protein 1

Gene

SORBS1

Organism
Homo sapiens (Human)
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 (By similarity).By similarity

GO - Molecular functioni

  1. actin binding Source: ProtInc
  2. cytoskeletal protein binding Source: ProtInc
  3. insulin receptor binding Source: UniProtKB
  4. SH3/SH2 adaptor activity Source: BHF-UCL

GO - Biological processi

  1. cell-matrix adhesion Source: ProtInc
  2. cellular response to insulin stimulus Source: BHF-UCL
  3. focal adhesion assembly Source: UniProtKB
  4. glucose transport Source: UniProtKB
  5. insulin receptor signaling pathway Source: UniProtKB
  6. muscle contraction Source: Reactome
  7. positive regulation of establishment of protein localization to plasma membrane Source: BHF-UCL
  8. positive regulation of glucose import Source: BHF-UCL
  9. positive regulation of glycogen biosynthetic process Source: BHF-UCL
  10. positive regulation of lipid biosynthetic process Source: BHF-UCL
  11. positive regulation of signal transduction Source: GOC
  12. stress fiber assembly Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Transport

Enzyme and pathway databases

ReactomeiREACT_20558. Smooth Muscle Contraction.
SignaLinkiQ9BX66.

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:KIAA0894, KIAA1296, SH3D5
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 10

Organism-specific databases

HGNCiHGNC:14565. SORBS1.

Subcellular locationi

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.By similarity

GO - Cellular componenti

  1. cell-cell adherens junction Source: UniProtKB
  2. cell-substrate adherens junction Source: UniProtKB
  3. centrosome Source: HPA
  4. cytoplasm Source: HPA
  5. cytosol Source: BHF-UCL
  6. focal adhesion Source: HPA
  7. membrane raft Source: UniProtKB
  8. nuclear matrix Source: UniProtKB-SubCell
  9. nucleoplasm Source: HPA
  10. nucleus Source: UniProtKB
  11. plasma membrane Source: HPA
  12. stress fiber Source: UniProtKB
  13. zonula adherens Source: ProtInc
Complete GO annotation...

Keywords - Cellular componenti

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

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA37899.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 12921292Sorbin and SH3 domain-containing protein 1PRO_0000072185Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei86 – 861Phosphoserine1 Publication
Modified residuei89 – 891Phosphoserine1 Publication
Modified residuei242 – 2421Phosphoserine1 Publication
Modified residuei259 – 2591Phosphoserine1 Publication
Modified residuei341 – 3411Phosphoserine1 Publication
Modified residuei350 – 3501Phosphoserine1 Publication
Modified residuei369 – 3691PhosphoserineBy similarity
Modified residuei472 – 4721Phosphoserine1 Publication
Modified residuei481 – 4811Phosphoserine1 Publication
Modified residuei536 – 5361Phosphotyrosine; by ABL1By similarity
Modified residuei556 – 5561Phosphoserine1 Publication
Modified residuei654 – 6541Phosphotyrosine; by ABL1By similarity
Modified residuei665 – 6651Phosphoserine2 Publications
Modified residuei708 – 7081Phosphothreonine1 Publication
Modified residuei862 – 8621Phosphothreonine2 Publications
Modified residuei937 – 9371Phosphotyrosine1 Publication
Modified residuei945 – 9451Phosphoserine1 Publication
Modified residuei1240 – 12401Phosphotyrosine; by ABL1By similarity

Post-translational modificationi

O-glycosylated.By similarity

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiQ9BX66.
PaxDbiQ9BX66.
PRIDEiQ9BX66.

PTM databases

PhosphoSiteiQ9BX66.

Expressioni

Tissue specificityi

Detected in skeletal muscle (at protein level). Widely expressed with highest levels in heart and skeletal muscle.2 Publications

Gene expression databases

BgeeiQ9BX66.
ExpressionAtlasiQ9BX66. baseline and differential.
GenevestigatoriQ9BX66.

Organism-specific databases

HPAiHPA027559.
HPA043084.

Interactioni

Subunit structurei

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 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 SH3 domain 2) with PXN.By similarity4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ABL1P005192EBI-433642,EBI-375543
ATXN7O1526515EBI-433642,EBI-708350
Dnm2P390525EBI-433642,EBI-349613From a different organism.
HTTP428584EBI-433642,EBI-466029
INPPL1O153575EBI-433642,EBI-1384248
PAK2Q131772EBI-433642,EBI-1045887

Protein-protein interaction databases

BioGridi115831. 27 interactions.
IntActiQ9BX66. 25 interactions.
MINTiMINT-2792261.

Structurei

Secondary structure

1
1292
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi796 – 8027Combined sources
Beta strandi808 – 8114Combined sources
Beta strandi819 – 8257Combined sources
Beta strandi827 – 8359Combined sources
Beta strandi838 – 8436Combined sources
Helixi844 – 8463Combined sources
Beta strandi847 – 8493Combined sources
Beta strandi863 – 8653Combined sources
Beta strandi870 – 8745Combined sources
Beta strandi882 – 8854Combined sources
Beta strandi893 – 8997Combined sources
Beta strandi901 – 9088Combined sources
Turni910 – 9123Combined sources
Beta strandi915 – 9195Combined sources
Helixi920 – 9223Combined sources
Beta strandi923 – 9275Combined sources
Beta strandi1230 – 12334Combined sources
Beta strandi1235 – 12406Combined sources
Beta strandi1257 – 12637Combined sources
Beta strandi1267 – 12737Combined sources
Turni1274 – 12763Combined sources
Beta strandi1279 – 12835Combined sources
Beta strandi1286 – 12894Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2DL3NMR-A796-850[»]
2ECZNMR-A870-926[»]
2LJ0NMR-A1228-1292[»]
2LJ1NMR-A1228-1291[»]
2MOXNMR-A791-930[»]
2O2WX-ray2.27A870-930[»]
2O31X-ray1.50A870-930[»]
2O9SX-ray0.83A870-930[»]
2O9VX-ray1.63A870-930[»]
4LN2X-ray1.00A866-930[»]
4LNPX-ray1.41A794-854[»]
ProteinModelPortaliQ9BX66.
SMRiQ9BX66. Positions 791-930, 1228-1292.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9BX66.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini366 – 469104SoHoPROSITE-ProRule annotationAdd
BLAST
Domaini793 – 85260SH3 1PROSITE-ProRule annotationAdd
BLAST
Domaini867 – 92862SH3 2PROSITE-ProRule annotationAdd
BLAST
Domaini1231 – 129262SH3 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

eggNOGiNOG256936.
GeneTreeiENSGT00760000119190.
HOVERGENiHBG053053.
InParanoidiQ9BX66.
KOiK06086.
OMAiXNTERSK.
OrthoDBiEOG75XGKP.
PhylomeDBiQ9BX66.
TreeFamiTF320680.

Family and domain databases

InterProiIPR028506. CAP/ponsin.
IPR011511. SH3_2.
IPR001452. SH3_domain.
IPR003127. Sorb.
[Graphical view]
PANTHERiPTHR10661:SF4. PTHR10661:SF4. 1 hit.
PfamiPF07653. SH3_2. 1 hit.
PF14604. SH3_9. 2 hits.
PF02208. Sorb. 1 hit.
[Graphical view]
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 (12)i

Sequence statusi: Complete.

This entry describes 12 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 11 Publication (identifier: Q9BX66-1) [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
MSSECDGGSK AVMNGLAPGS NGQDKATADP LRARSISAVK IIPVKTVKNA
60 70 80 90 100
SGLVLPTDMD LTKICTGKGA VTLRASSSYR ETPSSSPASP QETRQHESKP
110 120 130 140 150
GLEPEPSSAD EWRLSSSADA NGNAQPSSLA AKGYRSVHPN LPSDKSQDAT
160 170 180 190 200
SSSAAQPEVI VVPLYLVNTD RGQEGTARPP TPLGPLGCVP TIPATASAAS
210 220 230 240 250
PLTFPTLDDF IPPHLQRWPH HSQPARASGS FAPISQTPPS FSPPPPLVPP
260 270 280 290 300
APEDLRRVSE PDLTGAVSST DSSPLLNEVS SSLIGTDSQA FPSVSKPSSA
310 320 330 340 350
YPSTTIVNPT IVLLQHNREQ QKRLSSLSDP VSERRVGEQD SAPTQEKPTS
360 370 380 390 400
PGKAIEKRAK DDSRRVVKST QDLSDVSMDE VGIPLRNTER SKDWYKTMFK
410 420 430 440 450
QIHKLNRDTP EENPYFPTYK FPELPEIQQT SEEDNPYTPT YQFPASTPSP
460 470 480 490 500
KSEDDDSDLY SPRYSFSEDT KSPLSVPRSK SEMSYIDGEK VVKRSATLPL
510 520 530 540 550
PARSSSLKSS SERNDWEPPD KKVDTRKYRA EPKSIYEYQP GKSSVLTNEK
560 570 580 590 600
MSRDISPEEI DLKNEPWYKF FSELEFGKPP PKKIWDYTPG DCSILPREDR
610 620 630 640 650
KTNLDKDLSL CQTELEADLE KMETLNKAPS ANVPQSSAIS PTPEISSETP
660 670 680 690 700
GYIYSSNFHA VKRESDGAPG DLTSLENERQ IYKSVLEGGD IPLQGLSGLK
710 720 730 740 750
RPSSSASTKD SESPRHFIPA DYLESTEEFI RRRHDDKEKL LADQRRLKRE
760 770 780 790 800
QEEADIAARR HTGVIPTHHQ FITNERFGDL LNIDDTAKRK SGSEMRPARA
810 820 830 840 850
KFDFKAQTLK ELPLQKGDIV YIYKQIDQNW YEGEHHGRVG IFPRTYIELL
860 870 880 890 900
PPAEKAQPKK LTPVQVLEYG EAIAKFNFNG DTQVEMSFRK GERITLLRQV
910 920 930 940 950
DENWYEGRIP GTSRQGIFPI TYVDVIKRPL VKNPVDYMDL PFSSSPSRSA
960 970 980 990 1000
TASPQFSSHS KLITPAPSSL PHSRRALSPE MHAVTSEWIS LTVGVPGRRS
1010 1020 1030 1040 1050
LALTPPLPPL PEASIYNTDH LALSPRASPS LSLSLPHLSW SDRPTPRSVA
1060 1070 1080 1090 1100
SPLALPSPHK TYSLAPTSQA SLHMNGDGGV HTPSSGIHQD SFLQLPLGSS
1110 1120 1130 1140 1150
DSVISQLSDA FSSQSKRQPW REESGQYERK AERGAGERGP GGPKISKKSC
1160 1170 1180 1190 1200
LKPSDVVRCL STEQRLSDLN TPEESRPGKP LGSAFPGSEA EQTERHRGGE
1210 1220 1230 1240 1250
QAGRKAARRG GSQQPQAQQR RVTPDRSQTS QDLFSYQALY SYIPQNDDEL
1260 1270 1280 1290
ELRDGDIVDV MEKCDDGWFV GTSRRTKQFG TFPGNYVKPL YL
Length:1,292
Mass (Da):142,513
Last modified:January 11, 2011 - v3
Checksum:i70DA4169B6D82F06
GO
Isoform 21 Publication (identifier: Q9BX66-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     434-453: DNPYTPTYQFPASTPSPKSE → TKSCSVMSPRLECSGTVIAHCSLKLLDSSNPPTSASQVAGTA
     955-1117: Missing.

Show »
Length:1,151
Mass (Da):127,276
Checksum:iC1BD7AD5D5BE1300
GO
Isoform 31 Publication (identifier: Q9BX66-3) [UniParc]FASTAAdd to basket

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.

Show »
Length:905
Mass (Da):101,082
Checksum:iC44DB4C9B0526933
GO
Isoform 41 Publication (identifier: Q9BX66-4) [UniParc]FASTAAdd to basket

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. Contains a phosphoserine at position 105.2 Publications

Show »
Length:684
Mass (Da):76,596
Checksum:i9A417161477CB810
GO
Isoform 51 Publication (identifier: Q9BX66-5) [UniParc]FASTAAdd to basket

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 923.1 Publication

Show »
Length:1,004
Mass (Da):111,791
Checksum:i45A17463F7373E8B
GO
Isoform 61 Publication (identifier: Q9BX66-6) [UniParc]FASTAAdd to basket

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. Contains a phosphoserine at position 137. Contains a phosphoserine at position 452.2 Publications

Show »
Length:846
Mass (Da):95,036
Checksum:i61FC1B8026A7D9A1
GO
Isoform 7Curated (identifier: Q9BX66-7) [UniParc]FASTAAdd to basket

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 469.1 Publication

Show »
Length:628
Mass (Da):68,745
Checksum:i4B5BD67EF6355537
GO
Isoform 81 Publication (identifier: Q9BX66-8) [UniParc]FASTAAdd to basket

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. Contains a phosphoserine at position 114.2 Publications

Show »
Length:811
Mass (Da):91,055
Checksum:i019F4E7E811AFDF5
GO
Isoform 9Curated (identifier: Q9BX66-9) [UniParc]FASTAAdd to basket

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. Contains a phosphoserine at position 146.2 Publications

Show »
Length:781
Mass (Da):87,199
Checksum:iEDB752BF6DB3E4E1
GO
Isoform 10Curated (identifier: Q9BX66-10) [UniParc]FASTAAdd to basket

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 735.1 Publication

Show »
Length:816
Mass (Da):90,218
Checksum:i490FCF5615BF69DB
GO
Isoform 11 (identifier: Q9BX66-11) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     408-453: Missing.
     1213-1213: Q → QLSHHSLRAGPDLTESEKSYV

Show »
Length:1,266
Mass (Da):139,401
Checksum:i857F07CDCB13B97E
GO
Isoform 12 (identifier: Q9BX66-12) [UniParc]FASTAAdd to basket

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. Contains a phosphoserine at position 114.2 Publications

Show »
Length:1,294
Mass (Da):143,741
Checksum:i770EBDC6412A6C03
GO

Sequence cautioni

The sequence AAB93496.1 differs from that shown. Reason: Frameshift at positions 861, 867 and 885. Curated
The sequence BAA92534.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti9 – 91S → P in CAJ97431 (PubMed:17462669).Curated
Sequence conflicti18 – 181P → S in AAD27647 (PubMed:11374898).Curated
Sequence conflicti18 – 181P → S in AAF22175 (PubMed:11532984).Curated
Sequence conflicti110 – 1101D → G in AAD27647 (PubMed:11374898).Curated
Sequence conflicti110 – 1101D → G in AAF22175 (PubMed:11532984).Curated
Sequence conflicti113 – 1131R → K in AAD27647 (PubMed:11374898).Curated
Sequence conflicti113 – 1131R → K in AAF22175 (PubMed:11532984).Curated
Sequence conflicti131 – 1311A → V in AAD27647 (PubMed:11374898).Curated
Sequence conflicti131 – 1311A → V in AAF22175 (PubMed:11532984).Curated
Sequence conflicti134 – 1341Y → S in AAD27647 (PubMed:11374898).Curated
Sequence conflicti134 – 1341Y → S in AAF22175 (PubMed:11532984).Curated
Sequence conflicti226 – 2283RAS → SAC in AAF22175 (PubMed:11532984).Curated
Sequence conflicti264 – 2641T → P in AAF22175 (PubMed:11532984).Curated
Sequence conflicti292 – 2954PSVS → SSEC in AAD27647 (PubMed:11374898).Curated
Sequence conflicti292 – 2954PSVS → SSEC in AAF22175 (PubMed:11532984).Curated
Sequence conflicti481 – 4811S → R in AAF22175 (PubMed:11532984).Curated
Sequence conflicti489 – 4891E → V in AAD27647 (PubMed:11374898).Curated
Sequence conflicti489 – 4891E → V in AAF22175 (PubMed:11532984).Curated
Sequence conflicti607 – 6071D → E in AAF22175 (PubMed:11532984).Curated
Sequence conflicti610 – 6101L → F in AAF22175 (PubMed:11532984).Curated
Sequence conflicti644 – 6441E → G in AAD27647 (PubMed:11374898).Curated
Sequence conflicti644 – 6441E → G in AAF22175 (PubMed:11532984).Curated
Sequence conflicti679 – 6791R → S in AAD27647 (PubMed:11374898).Curated
Sequence conflicti679 – 6791R → S in AAF22175 (PubMed:11532984).Curated
Sequence conflicti690 – 6901D → V in AAD27647 (PubMed:11374898).Curated
Sequence conflicti690 – 6901D → V in AAF22175 (PubMed:11532984).Curated
Sequence conflicti694 – 6941Q → R in CAJ97431 (PubMed:17462669).Curated
Sequence conflicti695 – 6951G → D in AAD27647 (PubMed:11374898).Curated
Sequence conflicti695 – 6951G → D in AAF22175 (PubMed:11532984).Curated
Sequence conflicti710 – 7101D → N in AAD27647 (PubMed:11374898).Curated
Sequence conflicti710 – 7101D → N in AAF22175 (PubMed:11532984).Curated
Sequence conflicti1156 – 11561V → G in AAK37563 (PubMed:11374898).Curated
Sequence conflicti1156 – 11561V → G in AAK37564 (PubMed:11374898).Curated
Isoform 21 Publication (identifier: Q9BX66-2)
Sequence conflicti435 – 4351K → E in AAK37564 (PubMed:11374898).Curated
Sequence conflicti452 – 4554AHCS → SRCG in AAK37564 (PubMed:11374898).Curated
Sequence conflicti463 – 4631N → D in AAK37564 (PubMed:11374898).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti61 – 611L → P.8 Publications
Corresponds to variant rs943542 [ dbSNP | Ensembl ].
VAR_047652
Natural varianti74 – 741R → W.1 Publication
VAR_019653
Natural varianti175 – 1751G → V.
Corresponds to variant rs7081076 [ dbSNP | Ensembl ].
VAR_047653
Natural varianti195 – 1951T → A in a breast cancer sample; somatic mutation. 1 Publication
VAR_035661
Natural varianti237 – 2371T → A Has a protective role in both obesity and diabetes. 1 Publication
Corresponds to variant rs2281939 [ dbSNP | Ensembl ].
VAR_019654
Natural varianti485 – 4851Y → C.
Corresponds to variant rs35808802 [ dbSNP | Ensembl ].
VAR_047654

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei26 – 5732Missing in isoform 4, isoform 7, isoform 8, isoform 10 and isoform 12. 4 PublicationsVSP_050895Add
BLAST
Alternative sequencei101 – 1099Missing in isoform 4, isoform 5, isoform 6 and isoform 7. 4 PublicationsVSP_050896
Alternative sequencei147 – 21569Missing in isoform 3. 1 PublicationVSP_050898Add
BLAST
Alternative sequencei148 – 270123Missing in isoform 4, isoform 6, isoform 8, isoform 9 and isoform 12. 5 PublicationsVSP_050899Add
BLAST
Alternative sequencei319 – 32810Missing in isoform 12. CuratedVSP_041193
Alternative sequencei408 – 45346Missing in isoform 3, isoform 4, isoform 7, isoform 8, isoform 9, isoform 10, isoform 11 and isoform 12. 6 PublicationsVSP_050900Add
BLAST
Alternative sequencei431 – 45121Missing in isoform 5. 3 PublicationsVSP_050901Add
BLAST
Alternative sequencei434 – 45320DNPYT…SPKSE → TKSCSVMSPRLECSGTVIAH CSLKLLDSSNPPTSASQVAG TA in isoform 2. 1 PublicationVSP_050902Add
BLAST
Alternative sequencei552 – 63584Missing in isoform 4, isoform 7, isoform 9 and isoform 10. 4 PublicationsVSP_050903Add
BLAST
Alternative sequencei580 – 63556Missing in isoform 6. 1 PublicationVSP_050905Add
BLAST
Alternative sequencei580 – 60122Missing in isoform 8 and isoform 12. 1 PublicationVSP_050904Add
BLAST
Alternative sequencei602 – 63534Missing in isoform 3. 1 PublicationVSP_050906Add
BLAST
Alternative sequencei709 – 7091K → 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. CuratedVSP_041194
Alternative sequencei738 – 79356Missing in isoform 4 and isoform 10. 2 PublicationsVSP_050907Add
BLAST
Alternative sequencei795 – 7995MRPAR → KYDWA in isoform 7. 1 PublicationVSP_050908
Alternative sequencei800 – 1292493Missing in isoform 7. 1 PublicationVSP_050909Add
BLAST
Alternative sequencei955 – 1212258Missing in isoform 4, isoform 5, isoform 6, isoform 8, isoform 9, isoform 10 and isoform 12. 7 PublicationsVSP_050911Add
BLAST
Alternative sequencei955 – 1117163Missing in isoform 2. 1 PublicationVSP_050910Add
BLAST
Alternative sequencei956 – 97520FSSHS…PHSRR → LSHHSLRAGPDLTESEKSYV in isoform 3. 1 PublicationVSP_050912Add
BLAST
Alternative sequencei976 – 1213238Missing in isoform 3. 1 PublicationVSP_050913Add
BLAST
Alternative sequencei1213 – 12131Q → QLSHHSLRAGPDLTESEKSY V in isoform 11. 1 PublicationVSP_039210

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS31252.1. [Q9BX66-4]
CCDS31253.1. [Q9BX66-9]
CCDS31254.1. [Q9BX66-2]
CCDS31255.1. [Q9BX66-1]
CCDS31256.1. [Q9BX66-3]
CCDS73169.1. [Q9BX66-11]
CCDS7442.1. [Q9BX66-10]
PIRiT17257.
RefSeqiNP_001030126.1. NM_001034954.1.
NP_001030127.1. NM_001034955.1.
NP_001030128.1. NM_001034956.1.
NP_001030129.1. NM_001034957.1.
NP_001277223.1. NM_001290294.1.
NP_001277224.1. NM_001290295.1.
NP_001277225.1. NM_001290296.1.
NP_001277226.1. NM_001290297.1.
NP_001277227.1. NM_001290298.1.
NP_006425.2. NM_006434.2.
NP_056200.1. NM_015385.3.
NP_079267.1. NM_024991.2.
XP_006717644.1. XM_006717581.1. [Q9BX66-1]
XP_006717652.1. XM_006717589.1. [Q9BX66-5]
XP_006717654.1. XM_006717591.1. [Q9BX66-6]
XP_006717655.1. XM_006717592.1. [Q9BX66-8]
XP_006717658.1. XM_006717595.1. [Q9BX66-4]
UniGeneiHs.38621.

Genome annotation databases

EnsembliENST00000277982; ENSP00000277982; ENSG00000095637. [Q9BX66-2]
ENST00000306402; ENSP00000302556; ENSG00000095637. [Q9BX66-9]
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]
ENST00000607232; ENSP00000475901; ENSG00000095637. [Q9BX66-12]
GeneIDi10580.
KEGGihsa:10580.
UCSCiuc001kkl.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]

Polymorphism databases

DMDMi317373504.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS31252.1. [Q9BX66-4]
CCDS31253.1. [Q9BX66-9]
CCDS31254.1. [Q9BX66-2]
CCDS31255.1. [Q9BX66-1]
CCDS31256.1. [Q9BX66-3]
CCDS73169.1. [Q9BX66-11]
CCDS7442.1. [Q9BX66-10]
PIRiT17257.
RefSeqiNP_001030126.1. NM_001034954.1.
NP_001030127.1. NM_001034955.1.
NP_001030128.1. NM_001034956.1.
NP_001030129.1. NM_001034957.1.
NP_001277223.1. NM_001290294.1.
NP_001277224.1. NM_001290295.1.
NP_001277225.1. NM_001290296.1.
NP_001277226.1. NM_001290297.1.
NP_001277227.1. NM_001290298.1.
NP_006425.2. NM_006434.2.
NP_056200.1. NM_015385.3.
NP_079267.1. NM_024991.2.
XP_006717644.1. XM_006717581.1. [Q9BX66-1]
XP_006717652.1. XM_006717589.1. [Q9BX66-5]
XP_006717654.1. XM_006717591.1. [Q9BX66-6]
XP_006717655.1. XM_006717592.1. [Q9BX66-8]
XP_006717658.1. XM_006717595.1. [Q9BX66-4]
UniGeneiHs.38621.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2DL3NMR-A796-850[»]
2ECZNMR-A870-926[»]
2LJ0NMR-A1228-1292[»]
2LJ1NMR-A1228-1291[»]
2MOXNMR-A791-930[»]
2O2WX-ray2.27A870-930[»]
2O31X-ray1.50A870-930[»]
2O9SX-ray0.83A870-930[»]
2O9VX-ray1.63A870-930[»]
4LN2X-ray1.00A866-930[»]
4LNPX-ray1.41A794-854[»]
ProteinModelPortaliQ9BX66.
SMRiQ9BX66. Positions 791-930, 1228-1292.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115831. 27 interactions.
IntActiQ9BX66. 25 interactions.
MINTiMINT-2792261.

PTM databases

PhosphoSiteiQ9BX66.

Polymorphism databases

DMDMi317373504.

Proteomic databases

MaxQBiQ9BX66.
PaxDbiQ9BX66.
PRIDEiQ9BX66.

Protocols and materials databases

DNASUi10580.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000277982; ENSP00000277982; ENSG00000095637. [Q9BX66-2]
ENST00000306402; ENSP00000302556; ENSG00000095637. [Q9BX66-9]
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]
ENST00000607232; ENSP00000475901; ENSG00000095637. [Q9BX66-12]
GeneIDi10580.
KEGGihsa:10580.
UCSCiuc001kkl.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

CTDi10580.
GeneCardsiGC10M097061.
HGNCiHGNC:14565. SORBS1.
HPAiHPA027559.
HPA043084.
MIMi605264. gene.
neXtProtiNX_Q9BX66.
PharmGKBiPA37899.
HUGEiSearch...
Search...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG256936.
GeneTreeiENSGT00760000119190.
HOVERGENiHBG053053.
InParanoidiQ9BX66.
KOiK06086.
OMAiXNTERSK.
OrthoDBiEOG75XGKP.
PhylomeDBiQ9BX66.
TreeFamiTF320680.

Enzyme and pathway databases

ReactomeiREACT_20558. Smooth Muscle Contraction.
SignaLinkiQ9BX66.

Miscellaneous databases

ChiTaRSiSORBS1. human.
EvolutionaryTraceiQ9BX66.
GeneWikiiSORBS1.
GenomeRNAii10580.
NextBioi40165.
PROiQ9BX66.
SOURCEiSearch...

Gene expression databases

BgeeiQ9BX66.
ExpressionAtlasiQ9BX66. baseline and differential.
GenevestigatoriQ9BX66.

Family and domain databases

InterProiIPR028506. CAP/ponsin.
IPR011511. SH3_2.
IPR001452. SH3_domain.
IPR003127. Sorb.
[Graphical view]
PANTHERiPTHR10661:SF4. PTHR10661:SF4. 1 hit.
PfamiPF07653. SH3_2. 1 hit.
PF14604. SH3_9. 2 hits.
PF02208. Sorb. 1 hit.
[Graphical view]
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, 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: LiverImported and Skeletal muscleImported.
  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: RetinaImported.
  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 muscleImported.
  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: BrainImported.
  5. 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: BrainImported.
  7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 10), VARIANT PRO-61.
    Tissue: UterusImported.
  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.
    , 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. 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: TestisImported.
  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. 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. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-242; SER-259; SER-341; SER-350; SER-556; SER-665; THR-708; THR-862 AND TYR-937, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114 (ISOFORMS 12 AND 8), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-105 (ISOFORM 4), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-137 AND SER-452 (ISOFORM 6), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-146 (ISOFORM 9), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  17. Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 870-930.
  18. "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.
  19. Cited for: VARIANT [LARGE SCALE ANALYSIS] ALA-195.

Entry informationi

Entry nameiSRBS1_HUMAN
AccessioniPrimary (citable) accession number: Q9BX66
Secondary accession number(s): A0AED4
, 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 historyi
Integrated into UniProtKB/Swiss-Prot: August 31, 2004
Last sequence update: January 11, 2011
Last modified: March 4, 2015
This is version 144 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 10
    Human chromosome 10: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.