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Sorbin and SH3 domain-containing protein 1 (Ponsin) (SH3 domain protein 5) (SH3P12) (c-Cbl-associated protein) (CAP)

 SRBS1_HUMAN             Reviewed;        1292 AA.
Q9BX66; 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;
31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
11-JAN-2011, sequence version 3.
30-AUG-2017, entry version 164.
RecName: Full=Sorbin and SH3 domain-containing protein 1;
AltName: Full=Ponsin;
AltName: Full=SH3 domain protein 5;
AltName: Full=SH3P12;
AltName: Full=c-Cbl-associated protein;
Short=CAP;
Name=SORBS1 {ECO:0000312|HGNC:HGNC:14565};
Synonyms=KIAA0894, KIAA1296, SH3D5;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1] {ECO:0000305, ECO:0000312|EMBL:AAK37563.1}
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3 AND 4), TISSUE
SPECIFICITY, INTERACTION WITH ABL1 AND INSULIN RECEPTOR, AND VARIANT
PRO-61.
TISSUE=Liver {ECO:0000312|EMBL:AAD27647.1}, and
Skeletal muscle {ECO:0000312|EMBL:AAK37563.1};
PubMed=11374898; DOI=10.1006/geno.2001.6541;
Lin W.-H., Huang C.-J., Liu M.-W., Chang H.-M., Chen Y.-J., Tai T.-Y.,
Chuang L.-M.;
"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.";
Genomics 74:12-20(2001).
[2] {ECO:0000305, ECO:0000312|EMBL:AAK57480.1}
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 8), SUBCELLULAR LOCATION,
INTERACTION WITH SCA7, AND VARIANT PRO-61.
TISSUE=Retina {ECO:0000312|EMBL:AAK57480.1};
PubMed=11371513; DOI=10.1093/hmg/10.11.1201;
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.;
"Ataxin-7 interacts with a Cbl-associated protein that it recruits
into neuronal intranuclear inclusions.";
Hum. Mol. Genet. 10:1201-1213(2001).
[3] {ECO:0000305, ECO:0000312|EMBL:AAF22175.1}
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5), AND VARIANTS PRO-61; TRP-74
AND ALA-237.
TISSUE=Skeletal muscle {ECO:0000312|EMBL:AAF22175.1};
PubMed=11532984; DOI=10.1093/hmg/10.17.1753;
Lin W.-H., Chiu K.C., Chang H.-M., Lee K.C., Tai T.-Y., Chuang L.-M.;
"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.";
Hum. Mol. Genet. 10:1753-1760(2001).
[4] {ECO:0000305, ECO:0000312|EMBL:CAD34588.1}
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 6), INTERACTION WITH INPPL1, AND
VARIANT PRO-61.
TISSUE=Brain {ECO:0000312|EMBL:CAD34588.1};
PubMed=12504111; DOI=10.1016/S0006-291X(02)02894-2;
Vandenbroere I., Paternotte N., Dumont J.E., Erneux C., Pirson I.;
"The c-Cbl-associated protein and c-Cbl are two new partners of the
SH2-containing inositol polyphosphate 5-phosphatase SHIP2.";
Biochem. Biophys. Res. Commun. 300:494-500(2003).
[5]
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, AND VARIANT PRO-61.
TISSUE=Skeletal muscle;
PubMed=17462669; DOI=10.1016/j.jmb.2007.03.050;
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.;
"Paxillin and ponsin interact in nascent costameres of muscle cells.";
J. Mol. Biol. 369:665-682(2007).
[6] {ECO:0000305, ECO:0000312|EMBL:BAA92534.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 9), AND VARIANT
PRO-61.
TISSUE=Brain {ECO:0000312|EMBL:BAA92534.1};
PubMed=10718198; DOI=10.1093/dnares/7.1.65;
Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.;
"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.";
DNA Res. 7:65-73(2000).
[7] {ECO:0000305, ECO:0000312|EMBL:CAB55947.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 10), AND VARIANT
PRO-61.
TISSUE=Uterus {ECO:0000312|EMBL:CAB55947.1};
PubMed=11230166; DOI=10.1101/gr.GR1547R;
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., Tampe J., Heubner D.,
Wambutt R., Korn B., Klein M., Poustka A.;
"Towards a catalog of human genes and proteins: sequencing and
analysis of 500 novel complete protein coding human cDNAs.";
Genome Res. 11:422-435(2001).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15164054; DOI=10.1038/nature02462;
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.;
"The DNA sequence and comparative analysis of human chromosome 10.";
Nature 429:375-381(2004).
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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., 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.
[10] {ECO:0000305, ECO:0000312|EMBL:AAH42612.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 7 AND 9), AND VARIANT
PRO-61.
TISSUE=Testis {ECO:0000312|EMBL:AAH42612.1};
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[11]
NUCLEOTIDE SEQUENCE [MRNA] OF 752-888.
TISSUE=Placenta;
Hachiya T., Kobayasi A., Touji S., Tamai K.;
"A Fas-ligand associated factor 2, FLAF2, potentiates Fas-ligand
stability.";
Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases.
[12]
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), AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[13]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[14]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
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.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-481, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-89; SER-350 AND SER-665,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[17]
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), AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[18]
X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 870-930.
PubMed=17784760; DOI=10.1021/ja073846c;
Margiolaki I., Wright J.P., Wilmanns M., Fitch A.N., Pinotsis N.;
"Second SH3 domain of ponsin solved from powder diffraction.";
J. Am. Chem. Soc. 129:11865-11871(2007).
[19]
STRUCTURE BY NMR OF 796-926.
RIKEN structural genomics initiative (RSGI);
"Solution structure of SH3 domains of human Sorbin and SH3 domain-
containing protein 1.";
Submitted (FEB-2009) to the PDB data bank.
[20]
VARIANT [LARGE SCALE ANALYSIS] ALA-195.
PubMed=16959974; DOI=10.1126/science.1133427;
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., 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.;
"The consensus coding sequences of human breast and colorectal
cancers.";
Science 314:268-274(2006).
-!- 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).
{ECO:0000250|UniProtKB:Q62417}.
-!- SUBUNIT: 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 AFDN and with VCL. AFDN 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.
{ECO:0000250, ECO:0000269|PubMed:11371513,
ECO:0000269|PubMed:11374898, ECO:0000269|PubMed:12504111,
ECO:0000269|PubMed:17462669}.
-!- INTERACTION:
P00519:ABL1; NbExp=2; IntAct=EBI-433642, EBI-375543;
O15265:ATXN7; NbExp=15; IntAct=EBI-433642, EBI-708350;
P39052:Dnm2 (xeno); NbExp=5; IntAct=EBI-433642, EBI-349613;
A0A061I5T4:H671_4g13114 (xeno); NbExp=2; IntAct=EBI-433642, EBI-2504267;
P42858:HTT; NbExp=4; IntAct=EBI-433642, EBI-466029;
O15357:INPPL1; NbExp=5; IntAct=EBI-433642, EBI-1384248;
Q13177:PAK2; NbExp=2; IntAct=EBI-433642, EBI-1045887;
-!- SUBCELLULAR LOCATION: Cell junction, adherens junction. Cell
membrane. Cytoplasm, cytoskeleton. Cell junction, focal adhesion.
Nucleus {ECO:0000250}. Nucleus matrix {ECO:0000250}.
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. {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=12;
Name=1 {ECO:0000269|PubMed:11374898};
IsoId=Q9BX66-1; Sequence=Displayed;
Name=2 {ECO:0000269|PubMed:11374898};
IsoId=Q9BX66-2; Sequence=VSP_050902, VSP_050910;
Note=Ref.1 (AAK37564) sequence is in conflict in position:
435:K->E. Ref.1 (AAK37564) sequence is in conflict in positions:
452:AHCS->SRCG. Ref.1 (AAK37564) sequence is in conflict in
position: 463:N->D. {ECO:0000305};
Name=3 {ECO:0000269|PubMed:11374898};
IsoId=Q9BX66-3; Sequence=VSP_050898, VSP_050900, VSP_050906,
VSP_050912, VSP_050913;
Name=4 {ECO:0000269|PubMed:11374898};
IsoId=Q9BX66-4; Sequence=VSP_050895, VSP_050896, VSP_050899,
VSP_050900, VSP_050903, VSP_050907,
VSP_050911;
Note=Contains a phosphoserine at position 105. Contains a
phosphoserine at position 346. Contains a phosphoserine at
position 603. {ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:24275569};
Name=5 {ECO:0000269|PubMed:11532984};
IsoId=Q9BX66-5; Sequence=VSP_050896, VSP_050901, VSP_050911;
Note=Contains a phosphoserine at position 923.
{ECO:0000244|PubMed:18669648};
Name=6 {ECO:0000269|PubMed:12504111};
IsoId=Q9BX66-6; Sequence=VSP_050896, VSP_050899, VSP_050905,
VSP_050911;
Note=Contains a phosphoserine at position 137. Contains a
phosphoserine at position 452. Contains a phosphoserine at
position 765. {ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:24275569};
Name=7 {ECO:0000305};
IsoId=Q9BX66-7; Sequence=VSP_050895, VSP_050896, VSP_050900,
VSP_050903, VSP_050908, VSP_050909;
Note=No experimental confirmation available. Contains a
phosphoserine at position 469. {ECO:0000244|PubMed:18669648};
Name=8 {ECO:0000269|PubMed:11371513};
IsoId=Q9BX66-8; Sequence=VSP_050895, VSP_050899, VSP_050900,
VSP_050904, VSP_050911;
Note=Contains a phosphoserine at position 114. Contains a
phosphoserine at position 730. {ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:24275569};
Name=9 {ECO:0000305};
IsoId=Q9BX66-9; Sequence=VSP_050899, VSP_050900, VSP_050903,
VSP_050911;
Note=Contains a phosphoserine at position 146. Contains a
phosphoserine at position 387. Contains a phosphoserine at
position 700. {ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:24275569};
Name=10 {ECO:0000305};
IsoId=Q9BX66-10; Sequence=VSP_050895, VSP_050900, VSP_050903,
VSP_050907, VSP_050911;
Note=No experimental confirmation available. Contains a
phosphoserine at position 478. Contains a phosphoserine at
position 735. {ECO:0000244|PubMed:18669648};
Name=11;
IsoId=Q9BX66-11; Sequence=VSP_050900, VSP_039210;
Name=12;
IsoId=Q9BX66-12; Sequence=VSP_050895, VSP_050899, VSP_041193,
VSP_050900, VSP_050904, VSP_041194,
VSP_050911;
Note=No experimental confirmation available. Derived from mouse
ortholog data. Contains a phosphoserine at position 114.
Contains a phosphoserine at position 1213.
{ECO:0000244|PubMed:18669648, ECO:0000244|PubMed:24275569};
-!- TISSUE SPECIFICITY: Detected in skeletal muscle (at protein
level). Widely expressed with highest levels in heart and skeletal
muscle. {ECO:0000269|PubMed:11374898,
ECO:0000269|PubMed:17462669}.
-!- PTM: O-glycosylated. {ECO:0000250}.
-!- SEQUENCE CAUTION:
Sequence=AAB93496.1; Type=Frameshift; Positions=861, 867, 885; Evidence={ECO:0000305};
Sequence=BAA92534.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
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EMBL; AF136380; AAD27647.1; -; mRNA.
EMBL; AF356525; AAK37563.1; -; mRNA.
EMBL; AF356526; AAK37564.1; -; mRNA.
EMBL; AF356527; AAK37565.1; -; mRNA.
EMBL; AF330623; AAK57479.1; -; mRNA.
EMBL; AF330624; AAK57480.1; -; mRNA.
EMBL; AF136381; AAF22175.1; -; mRNA.
EMBL; AJ489942; CAD34588.1; -; mRNA.
EMBL; AM260536; CAJ97431.1; -; mRNA.
EMBL; AB037717; BAA92534.1; ALT_INIT; mRNA.
EMBL; AL117472; CAB55947.1; -; mRNA.
EMBL; AL158165; CAI14378.1; -; Genomic_DNA.
EMBL; AL158165; CAI14379.1; -; Genomic_DNA.
EMBL; AL158165; CAI14380.1; -; Genomic_DNA.
EMBL; AL158165; CAI14381.1; -; Genomic_DNA.
EMBL; AL158165; CAI14382.1; -; Genomic_DNA.
EMBL; AL158165; CAI14383.1; -; Genomic_DNA.
EMBL; AL158165; CAI14384.1; -; Genomic_DNA.
EMBL; AL158165; CAI14385.1; -; Genomic_DNA.
EMBL; CH471066; EAW49999.1; -; Genomic_DNA.
EMBL; CH471066; EAW50007.1; -; Genomic_DNA.
EMBL; BC042612; AAH42612.1; -; mRNA.
EMBL; BC152463; AAI52464.1; -; mRNA.
EMBL; U70668; AAB93496.1; ALT_FRAME; mRNA.
CCDS; CCDS31252.1; -. [Q9BX66-4]
CCDS; CCDS31253.1; -. [Q9BX66-9]
CCDS; CCDS31254.1; -. [Q9BX66-2]
CCDS; CCDS31255.1; -. [Q9BX66-1]
CCDS; CCDS31256.1; -. [Q9BX66-3]
CCDS; CCDS73169.1; -. [Q9BX66-11]
CCDS; CCDS7442.1; -. [Q9BX66-10]
CCDS; CCDS76326.1; -. [Q9BX66-8]
CCDS; CCDS76327.1; -. [Q9BX66-5]
PIR; T17257; T17257.
RefSeq; NP_001030126.1; NM_001034954.1.
RefSeq; NP_001030127.1; NM_001034955.1.
RefSeq; NP_001030128.1; NM_001034956.1.
RefSeq; NP_001030129.1; NM_001034957.1.
RefSeq; NP_001277223.1; NM_001290294.1.
RefSeq; NP_001277224.1; NM_001290295.1.
RefSeq; NP_001277225.1; NM_001290296.1.
RefSeq; NP_001277226.1; NM_001290297.1.
RefSeq; NP_001277227.1; NM_001290298.1.
RefSeq; NP_006425.2; NM_006434.2.
RefSeq; NP_056200.1; NM_015385.3.
RefSeq; NP_079267.1; NM_024991.2.
RefSeq; XP_006717652.1; XM_006717589.1. [Q9BX66-5]
UniGene; Hs.38621; -.
PDB; 2DL3; NMR; -; A=796-850.
PDB; 2ECZ; NMR; -; A=870-926.
PDB; 2LJ0; NMR; -; A=1228-1292.
PDB; 2LJ1; NMR; -; A=1228-1291.
PDB; 2MOX; NMR; -; A=791-930.
PDB; 2O2W; X-ray; 2.27 A; A=870-930.
PDB; 2O31; X-ray; 1.50 A; A=870-930.
PDB; 2O9S; X-ray; 0.83 A; A=870-930.
PDB; 2O9V; X-ray; 1.63 A; A=870-930.
PDB; 4LN2; X-ray; 1.00 A; A=866-930.
PDB; 4LNP; X-ray; 1.41 A; A=794-854.
PDBsum; 2DL3; -.
PDBsum; 2ECZ; -.
PDBsum; 2LJ0; -.
PDBsum; 2LJ1; -.
PDBsum; 2MOX; -.
PDBsum; 2O2W; -.
PDBsum; 2O31; -.
PDBsum; 2O9S; -.
PDBsum; 2O9V; -.
PDBsum; 4LN2; -.
PDBsum; 4LNP; -.
ProteinModelPortal; Q9BX66; -.
SMR; Q9BX66; -.
BioGrid; 115831; 37.
IntAct; Q9BX66; 34.
MINT; MINT-2792261; -.
STRING; 9606.ENSP00000355136; -.
iPTMnet; Q9BX66; -.
PhosphoSitePlus; Q9BX66; -.
BioMuta; SORBS1; -.
DMDM; 317373504; -.
EPD; Q9BX66; -.
MaxQB; Q9BX66; -.
PaxDb; Q9BX66; -.
PeptideAtlas; Q9BX66; -.
PRIDE; Q9BX66; -.
DNASU; 10580; -.
Ensembl; ENST00000277982; ENSP00000277982; ENSG00000095637. [Q9BX66-2]
Ensembl; ENST00000306402; ENSP00000302556; ENSG00000095637. [Q9BX66-9]
Ensembl; ENST00000354106; ENSP00000277984; ENSG00000095637. [Q9BX66-5]
Ensembl; ENST00000361941; ENSP00000355136; ENSG00000095637. [Q9BX66-1]
Ensembl; ENST00000371227; ENSP00000360271; ENSG00000095637. [Q9BX66-11]
Ensembl; ENST00000371239; ENSP00000360283; ENSG00000095637. [Q9BX66-8]
Ensembl; ENST00000371241; ENSP00000360285; ENSG00000095637. [Q9BX66-4]
Ensembl; ENST00000371245; ENSP00000360291; ENSG00000095637. [Q9BX66-3]
Ensembl; ENST00000371246; ENSP00000360292; ENSG00000095637. [Q9BX66-2]
Ensembl; ENST00000371247; ENSP00000360293; ENSG00000095637. [Q9BX66-1]
Ensembl; ENST00000371249; ENSP00000360295; ENSG00000095637. [Q9BX66-10]
Ensembl; ENST00000607232; ENSP00000475901; ENSG00000095637. [Q9BX66-12]
GeneID; 10580; -.
KEGG; hsa:10580; -.
UCSC; uc001kko.4; human. [Q9BX66-1]
CTD; 10580; -.
DisGeNET; 10580; -.
GeneCards; SORBS1; -.
HGNC; HGNC:14565; SORBS1.
HPA; HPA027559; -.
HPA; HPA043084; -.
MIM; 605264; gene.
neXtProt; NX_Q9BX66; -.
OpenTargets; ENSG00000095637; -.
PharmGKB; PA37899; -.
eggNOG; KOG4225; Eukaryota.
eggNOG; ENOG410XNVJ; LUCA.
GeneTree; ENSGT00760000119190; -.
HOVERGEN; HBG053053; -.
InParanoid; Q9BX66; -.
KO; K06086; -.
OMA; DYIDLPF; -.
OrthoDB; EOG091G0172; -.
PhylomeDB; Q9BX66; -.
TreeFam; TF320680; -.
Reactome; R-HSA-445355; Smooth Muscle Contraction.
SignaLink; Q9BX66; -.
SIGNOR; Q9BX66; -.
ChiTaRS; SORBS1; human.
EvolutionaryTrace; Q9BX66; -.
GeneWiki; SORBS1; -.
GenomeRNAi; 10580; -.
PRO; PR:Q9BX66; -.
Proteomes; UP000005640; Chromosome 10.
Bgee; ENSG00000095637; -.
ExpressionAtlas; Q9BX66; baseline and differential.
Genevisible; Q9BX66; HS.
GO; GO:0005913; C:cell-cell adherens junction; ISS:UniProtKB.
GO; GO:0005924; C:cell-substrate adherens junction; ISS:UniProtKB.
GO; GO:0005813; C:centrosome; IDA:HPA.
GO; GO:0005829; C:cytosol; ISS:BHF-UCL.
GO; GO:0005925; C:focal adhesion; IDA:HPA.
GO; GO:0045121; C:membrane raft; ISS:UniProtKB.
GO; GO:0016363; C:nuclear matrix; IEA:UniProtKB-SubCell.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; IDA:HPA.
GO; GO:0001725; C:stress fiber; ISS:UniProtKB.
GO; GO:0005915; C:zonula adherens; TAS:ProtInc.
GO; GO:0003779; F:actin binding; TAS:ProtInc.
GO; GO:0008092; F:cytoskeletal protein binding; TAS:ProtInc.
GO; GO:0005158; F:insulin receptor binding; IDA:UniProtKB.
GO; GO:0005070; F:SH3/SH2 adaptor activity; ISS:BHF-UCL.
GO; GO:0007160; P:cell-matrix adhesion; TAS:ProtInc.
GO; GO:0032869; P:cellular response to insulin stimulus; ISS:BHF-UCL.
GO; GO:0048041; P:focal adhesion assembly; ISS:UniProtKB.
GO; GO:0015758; P:glucose transport; ISS:UniProtKB.
GO; GO:0008286; P:insulin receptor signaling pathway; ISS:UniProtKB.
GO; GO:0006936; P:muscle contraction; TAS:Reactome.
GO; GO:0090004; P:positive regulation of establishment of protein localization to plasma membrane; ISS:BHF-UCL.
GO; GO:0046326; P:positive regulation of glucose import; ISS:BHF-UCL.
GO; GO:0045725; P:positive regulation of glycogen biosynthetic process; ISS:BHF-UCL.
GO; GO:0046889; P:positive regulation of lipid biosynthetic process; ISS:BHF-UCL.
GO; GO:0043149; P:stress fiber assembly; ISS:UniProtKB.
CDD; cd11919; SH3_Sorbs1_1; 1.
CDD; cd11922; SH3_Sorbs1_2; 1.
CDD; cd11916; SH3_Sorbs1_3; 1.
InterPro; IPR028506; CAP/ponsin.
InterPro; IPR011511; SH3_2.
InterPro; IPR001452; SH3_domain.
InterPro; IPR003127; SoHo_dom.
InterPro; IPR035606; SORBS1_SH3.
InterPro; IPR035610; SORBS1_SH3_1.
InterPro; IPR035611; SORBS1_SH3_2.
PANTHER; PTHR10663:SF292; PTHR10663:SF292; 1.
Pfam; PF00018; SH3_1; 1.
Pfam; PF07653; SH3_2; 1.
Pfam; PF14604; SH3_9; 1.
Pfam; PF02208; Sorb; 1.
SMART; SM00326; SH3; 3.
SMART; SM00459; Sorb; 1.
SUPFAM; SSF50044; SSF50044; 3.
PROSITE; PS50002; SH3; 3.
PROSITE; PS50831; SOHO; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Cell junction; Cell membrane;
Complete proteome; Cytoplasm; Cytoskeleton; Glycoprotein; Membrane;
Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Repeat;
SH3 domain; Transport.
CHAIN 1 1292 Sorbin and SH3 domain-containing protein
1.
/FTId=PRO_0000072185.
DOMAIN 366 469 SoHo. {ECO:0000255|PROSITE-
ProRule:PRU00195}.
DOMAIN 793 852 SH3 1. {ECO:0000255|PROSITE-
ProRule:PRU00192}.
DOMAIN 867 928 SH3 2. {ECO:0000255|PROSITE-
ProRule:PRU00192}.
DOMAIN 1231 1292 SH3 3. {ECO:0000255|PROSITE-
ProRule:PRU00192}.
MOD_RES 82 82 Phosphothreonine.
{ECO:0000250|UniProtKB:Q62417}.
MOD_RES 86 86 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 89 89 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 242 242 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 259 259 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 341 341 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 344 344 Phosphothreonine.
{ECO:0000250|UniProtKB:Q62417}.
MOD_RES 350 350 Phosphoserine.
{ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 369 369 Phosphoserine.
{ECO:0000250|UniProtKB:Q62417}.
MOD_RES 374 374 Phosphoserine.
{ECO:0000250|UniProtKB:Q62417}.
MOD_RES 465 465 Phosphoserine.
{ECO:0000250|UniProtKB:P84109}.
MOD_RES 472 472 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 481 481 Phosphoserine.
{ECO:0000244|PubMed:21406692}.
MOD_RES 536 536 Phosphotyrosine; by ABL1.
{ECO:0000250|UniProtKB:Q62417}.
MOD_RES 556 556 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 609 609 Phosphoserine.
{ECO:0000250|UniProtKB:Q62417}.
MOD_RES 640 640 Phosphoserine.
{ECO:0000250|UniProtKB:Q62417}.
MOD_RES 654 654 Phosphotyrosine; by ABL1.
{ECO:0000250|UniProtKB:Q62417}.
MOD_RES 665 665 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 708 708 Phosphothreonine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 713 713 Phosphoserine.
{ECO:0000250|UniProtKB:Q62417}.
MOD_RES 862 862 Phosphothreonine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:24275569}.
MOD_RES 937 937 Phosphotyrosine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 945 945 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 953 953 Phosphoserine.
{ECO:0000250|UniProtKB:Q62417}.
MOD_RES 1240 1240 Phosphotyrosine; by ABL1.
{ECO:0000250|UniProtKB:Q62417}.
VAR_SEQ 26 57 Missing (in isoform 4, isoform 7, isoform
8, isoform 10 and isoform 12).
{ECO:0000303|PubMed:11230166,
ECO:0000303|PubMed:11371513,
ECO:0000303|PubMed:11374898,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_050895.
VAR_SEQ 101 109 Missing (in isoform 4, isoform 5, isoform
6 and isoform 7).
{ECO:0000303|PubMed:11374898,
ECO:0000303|PubMed:11532984,
ECO:0000303|PubMed:12504111,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_050896.
VAR_SEQ 147 215 Missing (in isoform 3).
{ECO:0000303|PubMed:11374898}.
/FTId=VSP_050898.
VAR_SEQ 148 270 Missing (in isoform 4, isoform 6, isoform
8, isoform 9 and isoform 12).
{ECO:0000303|PubMed:10718198,
ECO:0000303|PubMed:11371513,
ECO:0000303|PubMed:11374898,
ECO:0000303|PubMed:12504111,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_050899.
VAR_SEQ 319 328 Missing (in isoform 12). {ECO:0000305}.
/FTId=VSP_041193.
VAR_SEQ 408 453 Missing (in isoform 3, isoform 4, isoform
7, isoform 8, isoform 9, isoform 10,
isoform 11 and isoform 12).
{ECO:0000303|PubMed:10718198,
ECO:0000303|PubMed:11230166,
ECO:0000303|PubMed:11371513,
ECO:0000303|PubMed:11374898,
ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:17462669}.
/FTId=VSP_050900.
VAR_SEQ 431 451 Missing (in isoform 5).
{ECO:0000303|PubMed:11371513,
ECO:0000303|PubMed:11374898,
ECO:0000303|PubMed:11532984}.
/FTId=VSP_050901.
VAR_SEQ 434 453 DNPYTPTYQFPASTPSPKSE -> TKSCSVMSPRLECSGTV
IAHCSLKLLDSSNPPTSASQVAGTA (in isoform 2).
{ECO:0000303|PubMed:11374898}.
/FTId=VSP_050902.
VAR_SEQ 552 635 Missing (in isoform 4, isoform 7, isoform
9 and isoform 10).
{ECO:0000303|PubMed:10718198,
ECO:0000303|PubMed:11230166,
ECO:0000303|PubMed:11374898,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_050903.
VAR_SEQ 580 635 Missing (in isoform 6).
{ECO:0000303|PubMed:12504111}.
/FTId=VSP_050905.
VAR_SEQ 580 601 Missing (in isoform 8 and isoform 12).
{ECO:0000303|PubMed:11371513}.
/FTId=VSP_050904.
VAR_SEQ 602 635 Missing (in isoform 3).
{ECO:0000303|PubMed:11374898}.
/FTId=VSP_050906.
VAR_SEQ 709 709 K -> KVDRKGGNAHMISSSSVHSRTFNTSNALGPVCKHKK
PLSAAKACISEILPSKFKPRLSAPSALLQEQKSILLPSEKA
QSCENLCVSGSLNDSKRGLPLQVGGSIENLLMRSRRDYDSK
SSSTMSLQEYSTSGRRPCPLSRKAGMQFTMLYRDMHQINRS
GLFLGSISSSSSVRDLASHFEKSSLALSRGELGPSQEGSEH
IPKHTVSSRITAFEQLIQRSRSMPSLDLSGRLSKSPTPVLS
RGSLTSARSAESLLESTKLHPKEMDGMNSSGVYASPTCSNM
AHHALSFRGLVPSEPLSTCSDDVDRCSNISTDSREGSGGSV
HGDFPKHRLNKCKGTCPASYTRFTTIRKHEQQQTSRQPEWR
LDARGDKSTLLRNIYLMSPLPFRLKKPLHHHPRQPSPGDSS
GLLVGQKPDLPSQPHQDQPPSGGKPVVPTRLSSRHTMARLS
RSSEPSQERPTALEDYPRAINNGNSVPYSDHSLDRNNNPQS
ELAPSRG (in isoform 12). {ECO:0000305}.
/FTId=VSP_041194.
VAR_SEQ 738 793 Missing (in isoform 4 and isoform 10).
{ECO:0000303|PubMed:11230166,
ECO:0000303|PubMed:11374898}.
/FTId=VSP_050907.
VAR_SEQ 795 799 MRPAR -> KYDWA (in isoform 7).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_050908.
VAR_SEQ 800 1292 Missing (in isoform 7).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_050909.
VAR_SEQ 955 1212 Missing (in isoform 4, isoform 5, isoform
6, isoform 8, isoform 9, isoform 10 and
isoform 12).
{ECO:0000303|PubMed:10718198,
ECO:0000303|PubMed:11230166,
ECO:0000303|PubMed:11371513,
ECO:0000303|PubMed:11374898,
ECO:0000303|PubMed:11532984,
ECO:0000303|PubMed:12504111,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_050911.
VAR_SEQ 955 1117 Missing (in isoform 2).
{ECO:0000303|PubMed:11374898}.
/FTId=VSP_050910.
VAR_SEQ 956 975 FSSHSKLITPAPSSLPHSRR -> LSHHSLRAGPDLTESEK
SYV (in isoform 3).
{ECO:0000303|PubMed:11374898}.
/FTId=VSP_050912.
VAR_SEQ 976 1213 Missing (in isoform 3).
{ECO:0000303|PubMed:11374898}.
/FTId=VSP_050913.
VAR_SEQ 1213 1213 Q -> QLSHHSLRAGPDLTESEKSYV (in isoform
11). {ECO:0000303|PubMed:17462669}.
/FTId=VSP_039210.
VARIANT 61 61 L -> P (in dbSNP:rs943542).
{ECO:0000269|PubMed:10718198,
ECO:0000269|PubMed:11230166,
ECO:0000269|PubMed:11371513,
ECO:0000269|PubMed:11374898,
ECO:0000269|PubMed:11532984,
ECO:0000269|PubMed:12504111,
ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:17462669}.
/FTId=VAR_047652.
VARIANT 74 74 R -> W (in dbSNP:rs757431022).
{ECO:0000269|PubMed:11532984}.
/FTId=VAR_019653.
VARIANT 175 175 G -> V (in dbSNP:rs7081076).
/FTId=VAR_047653.
VARIANT 195 195 T -> A (in a breast cancer sample;
somatic mutation).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_035661.
VARIANT 237 237 T -> A (has a protective role in both
obesity and diabetes; dbSNP:rs2281939).
{ECO:0000269|PubMed:11532984}.
/FTId=VAR_019654.
VARIANT 485 485 Y -> C (in dbSNP:rs35808802).
/FTId=VAR_047654.
CONFLICT 9 9 S -> P (in Ref. 5; CAJ97431).
{ECO:0000305}.
CONFLICT 18 18 P -> S (in Ref. 1; AAD27647 and 3;
AAF22175). {ECO:0000305}.
CONFLICT 110 110 D -> G (in Ref. 1; AAD27647 and 3;
AAF22175). {ECO:0000305}.
CONFLICT 113 113 R -> K (in Ref. 1; AAD27647 and 3;
AAF22175). {ECO:0000305}.
CONFLICT 131 131 A -> V (in Ref. 1; AAD27647 and 3;
AAF22175). {ECO:0000305}.
CONFLICT 134 134 Y -> S (in Ref. 1; AAD27647 and 3;
AAF22175). {ECO:0000305}.
CONFLICT 226 228 RAS -> SAC (in Ref. 3; AAF22175).
{ECO:0000305}.
CONFLICT 264 264 T -> P (in Ref. 3; AAF22175).
{ECO:0000305}.
CONFLICT 292 295 PSVS -> SSEC (in Ref. 1; AAD27647 and 3;
AAF22175). {ECO:0000305}.
CONFLICT 481 481 S -> R (in Ref. 3; AAF22175).
{ECO:0000305}.
CONFLICT 489 489 E -> V (in Ref. 1; AAD27647 and 3;
AAF22175). {ECO:0000305}.
CONFLICT 607 607 D -> E (in Ref. 3; AAF22175).
{ECO:0000305}.
CONFLICT 610 610 L -> F (in Ref. 3; AAF22175).
{ECO:0000305}.
CONFLICT 644 644 E -> G (in Ref. 1; AAD27647 and 3;
AAF22175). {ECO:0000305}.
CONFLICT 679 679 R -> S (in Ref. 1; AAD27647 and 3;
AAF22175). {ECO:0000305}.
CONFLICT 690 690 D -> V (in Ref. 1; AAD27647 and 3;
AAF22175). {ECO:0000305}.
CONFLICT 694 694 Q -> R (in Ref. 5; CAJ97431).
{ECO:0000305}.
CONFLICT 695 695 G -> D (in Ref. 1; AAD27647 and 3;
AAF22175). {ECO:0000305}.
CONFLICT 710 710 D -> N (in Ref. 1; AAD27647 and 3;
AAF22175). {ECO:0000305}.
CONFLICT 1156 1156 V -> G (in Ref. 1; AAK37563/AAK37564).
{ECO:0000305}.
STRAND 796 802 {ECO:0000244|PDB:4LNP}.
STRAND 808 811 {ECO:0000244|PDB:2MOX}.
STRAND 819 825 {ECO:0000244|PDB:4LNP}.
STRAND 827 835 {ECO:0000244|PDB:4LNP}.
STRAND 838 843 {ECO:0000244|PDB:4LNP}.
HELIX 844 846 {ECO:0000244|PDB:4LNP}.
STRAND 847 849 {ECO:0000244|PDB:4LNP}.
STRAND 863 865 {ECO:0000244|PDB:2MOX}.
STRAND 870 874 {ECO:0000244|PDB:2O9S}.
STRAND 882 885 {ECO:0000244|PDB:2MOX}.
STRAND 893 899 {ECO:0000244|PDB:2O9S}.
STRAND 901 908 {ECO:0000244|PDB:2O9S}.
TURN 910 912 {ECO:0000244|PDB:2ECZ}.
STRAND 915 919 {ECO:0000244|PDB:2O9S}.
HELIX 920 922 {ECO:0000244|PDB:2O9S}.
STRAND 923 927 {ECO:0000244|PDB:2O9S}.
STRAND 1230 1233 {ECO:0000244|PDB:2LJ0}.
STRAND 1235 1240 {ECO:0000244|PDB:2LJ0}.
STRAND 1257 1263 {ECO:0000244|PDB:2LJ0}.
STRAND 1267 1273 {ECO:0000244|PDB:2LJ0}.
TURN 1274 1276 {ECO:0000244|PDB:2LJ0}.
STRAND 1279 1283 {ECO:0000244|PDB:2LJ0}.
STRAND 1286 1289 {ECO:0000244|PDB:2LJ0}.
SEQUENCE 1292 AA; 142513 MW; 70DA4169B6D82F06 CRC64;
MSSECDGGSK AVMNGLAPGS NGQDKATADP LRARSISAVK IIPVKTVKNA SGLVLPTDMD
LTKICTGKGA VTLRASSSYR ETPSSSPASP QETRQHESKP GLEPEPSSAD EWRLSSSADA
NGNAQPSSLA AKGYRSVHPN LPSDKSQDAT SSSAAQPEVI VVPLYLVNTD RGQEGTARPP
TPLGPLGCVP TIPATASAAS PLTFPTLDDF IPPHLQRWPH HSQPARASGS FAPISQTPPS
FSPPPPLVPP APEDLRRVSE PDLTGAVSST DSSPLLNEVS SSLIGTDSQA FPSVSKPSSA
YPSTTIVNPT IVLLQHNREQ QKRLSSLSDP VSERRVGEQD SAPTQEKPTS PGKAIEKRAK
DDSRRVVKST QDLSDVSMDE VGIPLRNTER SKDWYKTMFK QIHKLNRDTP EENPYFPTYK
FPELPEIQQT SEEDNPYTPT YQFPASTPSP KSEDDDSDLY SPRYSFSEDT KSPLSVPRSK
SEMSYIDGEK VVKRSATLPL PARSSSLKSS SERNDWEPPD KKVDTRKYRA EPKSIYEYQP
GKSSVLTNEK MSRDISPEEI DLKNEPWYKF FSELEFGKPP PKKIWDYTPG DCSILPREDR
KTNLDKDLSL CQTELEADLE KMETLNKAPS ANVPQSSAIS PTPEISSETP GYIYSSNFHA
VKRESDGAPG DLTSLENERQ IYKSVLEGGD IPLQGLSGLK RPSSSASTKD SESPRHFIPA
DYLESTEEFI RRRHDDKEKL LADQRRLKRE QEEADIAARR HTGVIPTHHQ FITNERFGDL
LNIDDTAKRK SGSEMRPARA KFDFKAQTLK ELPLQKGDIV YIYKQIDQNW YEGEHHGRVG
IFPRTYIELL PPAEKAQPKK LTPVQVLEYG EAIAKFNFNG DTQVEMSFRK GERITLLRQV
DENWYEGRIP GTSRQGIFPI TYVDVIKRPL VKNPVDYMDL PFSSSPSRSA TASPQFSSHS
KLITPAPSSL PHSRRALSPE MHAVTSEWIS LTVGVPGRRS LALTPPLPPL PEASIYNTDH
LALSPRASPS LSLSLPHLSW SDRPTPRSVA SPLALPSPHK TYSLAPTSQA SLHMNGDGGV
HTPSSGIHQD SFLQLPLGSS DSVISQLSDA FSSQSKRQPW REESGQYERK AERGAGERGP
GGPKISKKSC LKPSDVVRCL STEQRLSDLN TPEESRPGKP LGSAFPGSEA EQTERHRGGE
QAGRKAARRG GSQQPQAQQR RVTPDRSQTS QDLFSYQALY SYIPQNDDEL ELRDGDIVDV
MEKCDDGWFV GTSRRTKQFG TFPGNYVKPL YL


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