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Sorbin and SH3 domain-containing protein 2 (Arg-binding protein 2) (ArgBP2) (Arg/Abl-interacting protein 2) (Sorbin)

 SRBS2_HUMAN             Reviewed;        1100 AA.
O94875; A6NEK9; B3KPQ7; B7Z1G5; B7Z3X6; C9JKV9; D3DP62; D3DP63;
E9PAS5; E9PAW4; G3XAI0; H7BXR4; J3KNZ5; O60592; O60593; Q96EX0;
22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
22-JUL-2008, sequence version 3.
25-OCT-2017, entry version 154.
RecName: Full=Sorbin and SH3 domain-containing protein 2;
AltName: Full=Arg-binding protein 2;
Short=ArgBP2;
AltName: Full=Arg/Abl-interacting protein 2;
AltName: Full=Sorbin;
Name=SORBS2; Synonyms=ARGBP2, KIAA0777;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 5), NUCLEOTIDE SEQUENCE
[MRNA] OF 1-1049 (ISOFORM 4), PHOSPHORYLATION, TISSUE SPECIFICITY,
SUBCELLULAR LOCATION, INTERACTION WITH ABL1 AND ABL2, AND FUNCTION.
TISSUE=Brain;
PubMed=9211900; DOI=10.1074/jbc.272.28.17542;
Wang B., Golemis E.A., Kruh G.D.;
"ArgBP2, a multiple Src homology 3 domain-containing, Arg/Abl-
interacting protein, is phosphorylated in v-Abl-transformed cells and
localized in stress fibers and cardiocyte Z-disks.";
J. Biol. Chem. 272:17542-17550(1997).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 6), AMIDATION AT ALA-153 (ISOFORM
6), AND TISSUE SPECIFICITY.
PubMed=11786189; DOI=10.1016/S0196-9781(01)00558-7;
Wahbi K., Magaud J.-P., Pansu D., Descroix-Vagne M.;
"Coding region of the sorbin gene in different species.";
Peptides 22:2045-2053(2001).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain;
PubMed=9872452; DOI=10.1093/dnares/5.5.277;
Nagase T., Ishikawa K., Suyama M., Kikuno R., Miyajima N., Tanaka A.,
Kotani H., Nomura N., Ohara O.;
"Prediction of the coding sequences of unidentified human genes. XI.
The complete sequences of 100 new cDNA clones from brain which code
for large proteins in vitro.";
DNA Res. 5:277-286(1998).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 7; 8 AND 11).
TISSUE=Embryonic brain, Thalamus, and Urinary bladder;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 9 AND 10).
TISSUE=Heart, and Hepatoma;
Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
Tanaka A., Yokoyama S.;
Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15815621; DOI=10.1038/nature03466;
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
Waterston R.H., Wilson R.K.;
"Generation and annotation of the DNA sequences of human chromosomes 2
and 4.";
Nature 434:724-731(2005).
[7]
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.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
TISSUE=Lymph;
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).
[9]
INTERACTION WITH CBL, UBIQUITINATION BY CBL, AND FUNCTION.
PubMed=12475393; DOI=10.1042/BJ20021539;
Soubeyran P., Barac A., Szymkiewicz I., Dikic I.;
"Cbl-ArgBP2 complex mediates ubiquitination and degradation of c-
Abl.";
Biochem. J. 370:29-34(2003).
[10]
INTERACTION WITH PALLD AND ACTN, AND SUBCELLULAR LOCATION.
PubMed=16125169; DOI=10.1016/j.yexcr.2005.06.026;
Roenty M., Taivainen A., Moza M., Kruh G.D., Ehler E., Carpen O.;
"Involvement of palladin and alpha-actinin in targeting of the Abl/Arg
kinase adaptor ArgBP2 to the actin cytoskeleton.";
Exp. Cell Res. 310:88-98(2005).
[11]
INTERACTION WITH AKT1 AND PAK1, UBIQUITINATION BY CBL, AND
PHOSPHORYLATION.
PubMed=15784622; DOI=10.1074/jbc.M500097200;
Yuan Z.-Q., Kim D., Kaneko S., Sussman M., Bokoch G.M., Kruh G.D.,
Nicosia S.V., Testa J.R., Cheng J.Q.;
"ArgBP2gamma interacts with Akt and p21-activated kinase-1 and
promotes cell survival.";
J. Biol. Chem. 280:21483-21490(2005).
[12]
FUNCTION, INTERACTION WITH PTPN12 AND WASF1, SUBCELLULAR LOCATION,
TISSUE SPECIFICITY, DEPHOSPHORYLATION BY PTPN12, AND DOMAIN.
PubMed=18559503; DOI=10.1158/0008-5472.CAN-08-0958;
Taieb D., Roignot J., Andre F., Garcia S., Masson B., Pierres A.,
Iovanna J.L., Soubeyran P.;
"ArgBP2-dependent signaling regulates pancreatic cell migration,
adhesion, and tumorigenicity.";
Cancer Res. 68:4588-4596(2008).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-157; THR-277; SER-301
AND SER-302, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-437 AND
SER-439 (ISOFORM 10), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT
SER-344 AND SER-346 (ISOFORM 12), PHOSPHORYLATION [LARGE SCALE
ANALYSIS] AT SER-258 AND SER-260 (ISOFORM 3), PHOSPHORYLATION [LARGE
SCALE ANALYSIS] AT SER-304 AND SER-306 (ISOFORMS 4 AND 5), 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).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-157; SER-298; SER-299
AND SER-302, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-437 AND
SER-439 (ISOFORM 10), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-28
(ISOFORM 11), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-344 AND
SER-346 (ISOFORM 12), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14
(ISOFORMS 12 AND 9), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-258
AND SER-260 (ISOFORM 3), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT
SER-304 AND SER-306 (ISOFORMS 4 AND 5), AND 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-154; SER-157; SER-239;
SER-259; SER-287; THR-292; SER-302; SER-304; SER-843 AND SER-1023,
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-413; THR-415; SER-439;
THR-459 AND SER-474 (ISOFORM 10), PHOSPHORYLATION [LARGE SCALE
ANALYSIS] AT SER-27 AND SER-28 (ISOFORM 11), PHOSPHORYLATION [LARGE
SCALE ANALYSIS] AT THR-320; THR-322; SER-346; THR-366 AND SER-381
(ISOFORM 12), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13 AND
SER-14 (ISOFORMS 12 AND 9), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT
SER-316 (ISOFORM 2), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT
THR-234; THR-236; SER-260 AND SER-295 (ISOFORM 3), PHOSPHORYLATION
[LARGE SCALE ANALYSIS] AT THR-280 (ISOFORMS 3; 4 AND 5),
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-282; SER-306; THR-326
AND SER-341 (ISOFORMS 4 AND 5), PHOSPHORYLATION [LARGE SCALE ANALYSIS]
AT SER-311 (ISOFORM 8), 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).
-!- FUNCTION: Adapter protein that plays a role in the assembling of
signaling complexes, being a link between ABL kinases and actin
cytoskeleton. Can form complex with ABL1 and CBL, thus promoting
ubiquitination and degradation of ABL1 or with AKT1 and PAK1, thus
mediating AKT1-mediated activation of PAK1. May play a role in the
regulation of pancreatic cell adhesion, possibly by acting on
WASF1 phosphorylation, enhancing phosphorylation by ABL1, as well
as dephosphorylation by PTPN12 (PubMed:18559503). Isoform 6
increases water and sodium absorption in the intestine and gall-
bladder. {ECO:0000269|PubMed:12475393,
ECO:0000269|PubMed:18559503, ECO:0000269|PubMed:9211900}.
-!- SUBUNIT: Interacts with ABL, CBL, DNM1, DNM2, FLOT1, AFDN,
PTK2B/PYK2, SAPAP, SPTAN1, SYNJ1, SYNJ2, VCL/vinculin, and WASF
(By similarity). Interacts with ABL1/c-Abl, ABL2/v-Abl/Arg, ACTN,
AKT1, CBL, PALLD and PAK1. Interacts with PTPN12 and WASF1 via its
SH3 domains; this interaction may mediate the partial PTPN12 and
WASF1 translocation to focal adhesion sites. {ECO:0000250,
ECO:0000269|PubMed:12475393, ECO:0000269|PubMed:15784622,
ECO:0000269|PubMed:16125169, ECO:0000269|PubMed:18559503,
ECO:0000269|PubMed:9211900}.
-!- INTERACTION:
Q9WMX2:- (xeno); NbExp=2; IntAct=EBI-311323, EBI-6863748;
O43707:ACTN4; NbExp=4; IntAct=EBI-12037893, EBI-351526;
Q8N5M1:ATPAF2; NbExp=3; IntAct=EBI-311323, EBI-1166928;
O43281:EFS; NbExp=3; IntAct=EBI-311323, EBI-718488;
V9HW98:HEL2; NbExp=3; IntAct=EBI-311323, EBI-10190883;
O43639:NCK2; NbExp=3; IntAct=EBI-311323, EBI-713635;
Q13177:PAK2; NbExp=2; IntAct=EBI-311323, EBI-1045887;
Q8WX93:PALLD; NbExp=2; IntAct=EBI-311323, EBI-2803991;
Q9H788-2:SH2D4A; NbExp=3; IntAct=EBI-311323, EBI-10308083;
A5D8V6:VPS37C; NbExp=3; IntAct=EBI-311323, EBI-2559305;
P42768:WAS; NbExp=3; IntAct=EBI-311323, EBI-346375;
P63104:YWHAZ; NbExp=2; IntAct=EBI-311323, EBI-347088;
-!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region
{ECO:0000269|PubMed:16125169, ECO:0000269|PubMed:9211900}. Apical
cell membrane {ECO:0000269|PubMed:18559503}. Cell junction, focal
adhesion {ECO:0000269|PubMed:18559503}. Cell projection,
lamellipodium {ECO:0000269|PubMed:18559503}. Note=Found at the Z-
disk sarcomeres, stress fibers, dense bodies and focal adhesion.
In pancreatic acinar cells, localized preferentially to the apical
membrane. Colocalized with vinculin and filamentous actin at focal
adhesions and lamellipodia of pancreatic cells.
{ECO:0000269|PubMed:18559503}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=12;
Name=1;
IsoId=O94875-1; Sequence=Displayed;
Name=2; Synonyms=ArgBP2a;
IsoId=O94875-2; Sequence=VSP_034792, VSP_034794, VSP_034798;
Note=Ref.1 (AAC05509) sequence is in conflict in position:
13:A->P. Contains a phosphoserine at position 316.
{ECO:0000244|PubMed:24275569, ECO:0000305};
Name=3;
IsoId=O94875-3; Sequence=VSP_034795, VSP_034798;
Note=Contains a phosphothreonine at position 234. Contains a
phosphothreonine at position 236. Contains a phosphoserine at
position 258. Contains a phosphoserine at position 260. Contains
a phosphothreonine at position 280. Contains a phosphoserine at
position 295. {ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231, ECO:0000244|PubMed:24275569};
Name=4;
IsoId=O94875-4; Sequence=VSP_034792, VSP_034795, VSP_034798;
Note=Contains a phosphothreonine at position 280. Contains a
phosphothreonine at position 282. Contains a phosphoserine at
position 304. Contains a phosphoserine at position 306. Contains
a phosphothreonine at position 326. Contains a phosphoserine at
position 341. {ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231, ECO:0000244|PubMed:24275569};
Name=5; Synonyms=ArgBP2b;
IsoId=O94875-5; Sequence=VSP_034792, VSP_034795, VSP_034798,
VSP_034799;
Note=Ref.1 (AAC05508) sequence is in conflict in position:
13:A->P. Contains a phosphothreonine at position 280. Contains a
phosphothreonine at position 282. Contains a phosphoserine at
position 304. Contains a phosphoserine at position 306. Contains
a phosphothreonine at position 326. Contains a phosphoserine at
position 341. {ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231, ECO:0000244|PubMed:24275569,
ECO:0000305};
Name=6; Synonyms=Sorbin;
IsoId=O94875-6; Sequence=VSP_034791, VSP_034793, VSP_034796,
VSP_034797;
Note=Contains a alanine amide at position 153.
{ECO:0000269|PubMed:11786189};
Name=7;
IsoId=O94875-7; Sequence=VSP_043665, VSP_043666;
Note=No experimental confirmation available.;
Name=8;
IsoId=O94875-8; Sequence=VSP_045640, VSP_045641, VSP_034798;
Note=No experimental confirmation available. Contains a
phosphoserine at position 311. {ECO:0000244|PubMed:24275569};
Name=9;
IsoId=O94875-9; Sequence=VSP_046219, VSP_043666, VSP_034798;
Note=No experimental confirmation available. Contains a
phosphoserine at position 14. Contains a phosphoserine at
position 13. {ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:24275569};
Name=10;
IsoId=O94875-10; Sequence=VSP_046220, VSP_034795, VSP_034798;
Note=No experimental confirmation available. Ref.5 (AK225812)
sequence is in conflict in position: 424:K->E. Contains a
phosphothreonine at position 413. Contains a phosphothreonine at
position 415. Contains a phosphoserine at position 437. Contains
a phosphoserine at position 439. Contains a phosphothreonine at
position 459. Contains a phosphoserine at position 474.
{ECO:0000244|PubMed:18669648, ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:24275569, ECO:0000305};
Name=11;
IsoId=O94875-11; Sequence=VSP_047056;
Note=Contains a phosphoserine at position 28. Contains a
phosphoserine at position 27. {ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:24275569};
Name=12;
IsoId=O94875-12; Sequence=VSP_046219, VSP_034795, VSP_034798;
Note=Contains a phosphoserine at position 14. Contains a
phosphoserine at position 13. Contains a phosphothreonine at
position 320. Contains a phosphothreonine at position 322.
Contains a phosphoserine at position 344. Contains a
phosphoserine at position 346. Contains a phosphothreonine at
position 366. Contains a phosphoserine at position 381.
{ECO:0000244|PubMed:18669648, ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:24275569};
-!- TISSUE SPECIFICITY: Abundantly expressed in heart. In cardiac
muscle cells, located in the Z-disks of sarcomere. Also found, but
to a lower extent, in small and large intestine, pancreas, thymus,
colon, spleen, prostate, testis, brain, ovary and epithelial
cells. In the pancreas, mainly expressed in acinar cells, duct
cells and all cell types in islets (at protein level). Tends to be
down-regulated in pancreatic adenocarcinomas ans metastases.
{ECO:0000269|PubMed:11786189, ECO:0000269|PubMed:18559503,
ECO:0000269|PubMed:9211900}.
-!- DOMAIN: The first 2 SH3 domains are required for WASF1-binding.
All 3 SH3 domains can bind independently to PTPN12.
{ECO:0000269|PubMed:18559503}.
-!- PTM: Ubiquitinated by CBL. {ECO:0000269|PubMed:12475393,
ECO:0000269|PubMed:15784622}.
-!- PTM: Dephosphorylated by PTPN12. {ECO:0000269|PubMed:18559503}.
-!- SEQUENCE CAUTION:
Sequence=BAA34497.2; Type=Erroneous initiation; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/SORBS2ID693ch4q35.html";
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EMBL; AF049884; AAC05508.1; -; mRNA.
EMBL; AF049885; AAC05509.1; -; mRNA.
EMBL; AB018320; BAA34497.2; ALT_INIT; mRNA.
EMBL; AK056628; BAG51769.1; -; mRNA.
EMBL; AK293400; BAH11501.1; -; mRNA.
EMBL; AK296461; BAH12362.1; -; mRNA.
EMBL; AK225327; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; AK225812; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; AC093797; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC096659; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC104805; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC108472; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471056; EAX04630.1; -; Genomic_DNA.
EMBL; CH471056; EAX04631.1; -; Genomic_DNA.
EMBL; CH471056; EAX04632.1; -; Genomic_DNA.
EMBL; CH471056; EAX04635.1; -; Genomic_DNA.
EMBL; CH471056; EAX04636.1; -; Genomic_DNA.
EMBL; BC011883; AAH11883.1; -; mRNA.
CCDS; CCDS3845.1; -. [O94875-1]
CCDS; CCDS43289.2; -. [O94875-2]
CCDS; CCDS47173.1; -. [O94875-9]
CCDS; CCDS47174.1; -. [O94875-12]
CCDS; CCDS47175.1; -. [O94875-10]
CCDS; CCDS47176.1; -. [O94875-7]
CCDS; CCDS54825.1; -. [O94875-8]
CCDS; CCDS59482.1; -. [O94875-11]
RefSeq; NP_001139142.1; NM_001145670.1. [O94875-9]
RefSeq; NP_001139143.1; NM_001145671.2. [O94875-12]
RefSeq; NP_001139144.1; NM_001145672.1. [O94875-8]
RefSeq; NP_001139145.1; NM_001145673.1. [O94875-10]
RefSeq; NP_001139146.1; NM_001145674.1. [O94875-7]
RefSeq; NP_001257700.1; NM_001270771.1. [O94875-11]
RefSeq; NP_003594.3; NM_003603.6. [O94875-2]
RefSeq; NP_066547.1; NM_021069.4. [O94875-1]
RefSeq; XP_005263369.1; XM_005263312.1. [O94875-4]
RefSeq; XP_006714453.1; XM_006714390.1. [O94875-8]
RefSeq; XP_016864260.1; XM_017008771.1. [O94875-3]
UniGene; Hs.481342; -.
UniGene; Hs.619806; -.
UniGene; Hs.655143; -.
PDB; 5VEI; X-ray; 1.33 A; A=866-921.
PDBsum; 5VEI; -.
ProteinModelPortal; O94875; -.
SMR; O94875; -.
BioGrid; 114047; 58.
CORUM; O94875; -.
DIP; DIP-31634N; -.
IntAct; O94875; 57.
MINT; MINT-196404; -.
STRING; 9606.ENSP00000284776; -.
iPTMnet; O94875; -.
PhosphoSitePlus; O94875; -.
BioMuta; SORBS2; -.
MaxQB; O94875; -.
PaxDb; O94875; -.
PeptideAtlas; O94875; -.
PRIDE; O94875; -.
DNASU; 8470; -.
Ensembl; ENST00000284776; ENSP00000284776; ENSG00000154556. [O94875-1]
Ensembl; ENST00000319471; ENSP00000322182; ENSG00000154556. [O94875-12]
Ensembl; ENST00000355634; ENSP00000347852; ENSG00000154556. [O94875-11]
Ensembl; ENST00000393528; ENSP00000377162; ENSG00000154556. [O94875-2]
Ensembl; ENST00000418609; ENSP00000397482; ENSG00000154556. [O94875-7]
Ensembl; ENST00000437304; ENSP00000396008; ENSG00000154556. [O94875-10]
Ensembl; ENST00000448662; ENSP00000409158; ENSG00000154556. [O94875-8]
Ensembl; ENST00000449407; ENSP00000397262; ENSG00000154556. [O94875-9]
GeneID; 8470; -.
KEGG; hsa:8470; -.
UCSC; uc003iyh.4; human. [O94875-1]
CTD; 8470; -.
DisGeNET; 8470; -.
EuPathDB; HostDB:ENSG00000154556.17; -.
GeneCards; SORBS2; -.
HGNC; HGNC:24098; SORBS2.
HPA; HPA036754; -.
HPA; HPA036755; -.
MIM; 616349; gene.
neXtProt; NX_O94875; -.
OpenTargets; ENSG00000154556; -.
PharmGKB; PA142670890; -.
eggNOG; ENOG410IPNR; Eukaryota.
eggNOG; ENOG410XNVJ; LUCA.
GeneTree; ENSGT00760000119190; -.
HOGENOM; HOG000294090; -.
HOVERGEN; HBG108509; -.
InParanoid; O94875; -.
OMA; XEDELEL; -.
OrthoDB; EOG091G01CW; -.
PhylomeDB; O94875; -.
TreeFam; TF320680; -.
SignaLink; O94875; -.
SIGNOR; O94875; -.
ChiTaRS; SORBS2; human.
GeneWiki; SORBS2; -.
GenomeRNAi; 8470; -.
PRO; PR:O94875; -.
Proteomes; UP000005640; Chromosome 4.
Bgee; ENSG00000154556; -.
CleanEx; HS_SORBS2; -.
ExpressionAtlas; O94875; baseline and differential.
Genevisible; O94875; HS.
GO; GO:0015629; C:actin cytoskeleton; TAS:ProtInc.
GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0005925; C:focal adhesion; IEA:UniProtKB-SubCell.
GO; GO:0030027; C:lamellipodium; IEA:UniProtKB-SubCell.
GO; GO:0005634; C:nucleus; TAS:ProtInc.
GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0030018; C:Z disc; NAS:UniProtKB.
GO; GO:0008093; F:cytoskeletal adaptor activity; TAS:ProtInc.
GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
GO; GO:0005200; F:structural constituent of cytoskeleton; TAS:ProtInc.
GO; GO:0008307; F:structural constituent of muscle; TAS:ProtInc.
GO; GO:0007015; P:actin filament organization; IEA:InterPro.
GO; GO:0061049; P:cell growth involved in cardiac muscle cell development; ISS:BHF-UCL.
InterPro; IPR036028; SH3-like_dom.
InterPro; IPR001452; SH3_domain.
InterPro; IPR003127; SoHo_dom.
InterPro; IPR028506; Sorbin_SH3.
InterPro; IPR013087; Znf_C2H2_type.
PANTHER; PTHR45043; PTHR45043; 1.
Pfam; PF00018; SH3_1; 2.
Pfam; PF14604; SH3_9; 1.
Pfam; PF02208; Sorb; 1.
PRINTS; PR00452; SH3DOMAIN.
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; Amidation; Cell junction;
Cell membrane; Cell projection; Complete proteome; Cytoplasm;
Membrane; Phosphoprotein; Polymorphism; Reference proteome; Repeat;
SH3 domain; Ubl conjugation.
CHAIN 1 1100 Sorbin and SH3 domain-containing protein
2.
/FTId=PRO_0000344477.
DOMAIN 66 127 SoHo. {ECO:0000255|PROSITE-
ProRule:PRU00195}.
DOMAIN 863 922 SH3 1. {ECO:0000255|PROSITE-
ProRule:PRU00192}.
DOMAIN 938 999 SH3 2. {ECO:0000255|PROSITE-
ProRule:PRU00192}.
DOMAIN 1041 1100 SH3 3. {ECO:0000255|PROSITE-
ProRule:PRU00192}.
COMPBIAS 167 182 Pro-rich.
COMPBIAS 640 652 His-rich.
COMPBIAS 931 934 Poly-Pro.
MOD_RES 30 30 Phosphoserine.
{ECO:0000250|UniProtKB:Q3UTJ2}.
MOD_RES 43 43 Phosphoserine.
{ECO:0000250|UniProtKB:Q3UTJ2}.
MOD_RES 154 154 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 157 157 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:24275569}.
MOD_RES 239 239 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 245 245 Phosphoserine.
{ECO:0000250|UniProtKB:Q3UTJ2}.
MOD_RES 248 248 Phosphoserine.
{ECO:0000250|UniProtKB:Q3UTJ2}.
MOD_RES 259 259 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 277 277 Phosphothreonine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 287 287 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 292 292 Phosphothreonine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 297 297 Phosphoserine.
{ECO:0000250|UniProtKB:Q3UTJ2}.
MOD_RES 298 298 Phosphoserine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 299 299 Phosphoserine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 301 301 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 302 302 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:24275569}.
MOD_RES 304 304 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 383 383 Phosphoserine.
{ECO:0000250|UniProtKB:Q3UTJ2}.
MOD_RES 494 494 Phosphoserine.
{ECO:0000250|UniProtKB:O35413}.
MOD_RES 497 497 Phosphoserine.
{ECO:0000250|UniProtKB:Q3UTJ2}.
MOD_RES 550 550 Phosphoserine.
{ECO:0000250|UniProtKB:Q3UTJ2}.
MOD_RES 750 750 Phosphoserine.
{ECO:0000250|UniProtKB:Q3UTJ2}.
MOD_RES 843 843 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 1017 1017 Phosphoserine.
{ECO:0000250|UniProtKB:Q3UTJ2}.
MOD_RES 1023 1023 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
VAR_SEQ 1 89 MSYYQRPFSPSAYSLPASLNSSIVMQHGTSLDSTDTYPQHA
QSLDGTTSSSIPLYRSSEEEKRVTVIKAPHYPGIGPVDESG
IPTAIRT -> MKATTPLQ (in isoform 7).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_043665.
VAR_SEQ 1 81 Missing (in isoform 6).
{ECO:0000303|PubMed:11786189}.
/FTId=VSP_034791.
VAR_SEQ 1 1 M -> MYSNEDSRQTIVYSEESNTTMSYTQKITNPLPAASS
TDPAPFANINTPVLQEDYRQDSQTRRISTLKLTHNQDLGSS
SPISTPQFSKSVEVPSFLKRPRSLTPNPVPETHTASLSIQI
APLSGQDLESHKQLPELSPETAKIPLQQERQKSAVAAASQS
SDCRVSQITVNGNSGGAVSPM (in isoform 10).
{ECO:0000303|Ref.5}.
/FTId=VSP_046220.
VAR_SEQ 1 1 M -> MNTDSGGCARKRAAMSVTLTSVKRVQSSPNLLAAGR
DSQSPDSAWRSYNDGNQETLNGDATYSSLAAKGFRSVRPNL
QDKRSPTQSQITVNGNSGGAVSPM (in isoform 11).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_047056.
VAR_SEQ 1 1 M -> MNTGRDSQSPDSAKGFRSVRPNLQDKRSPTQSQITV
NGNSGGAVSPM (in isoform 2, isoform 4 and
isoform 5). {ECO:0000303|PubMed:9211900}.
/FTId=VSP_034792.
VAR_SEQ 1 1 M -> MNTGRDSQSPDSAWRSYNDGNQETLNGDATYSSLAA
KGFRSVRPNLQDKRSPTQSQITVNGNSGGAVSPM (in
isoform 8).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_045640.
VAR_SEQ 1 1 M -> MSVTLTSVKRVQSSPNLLAAGRDSQSPDSAWRSYND
GNQETLNGDATYSSLAAKGFRSVRPNLQDKRSPTQSQITVN
GNSGGAVSPM (in isoform 9 and isoform 12).
{ECO:0000303|Ref.5}.
/FTId=VSP_046219.
VAR_SEQ 82 89 GIPTAIRT -> MKATTPLQ (in isoform 6).
{ECO:0000303|PubMed:11786189}.
/FTId=VSP_034793.
VAR_SEQ 112 126 Missing (in isoform 7 and isoform 9).
{ECO:0000303|PubMed:14702039,
ECO:0000303|Ref.5}.
/FTId=VSP_043666.
VAR_SEQ 228 228 P -> PTDRINPDDIDLENEPWYKFFSELEFGRPPPKKPLD
YVQDHSSGVFNE (in isoform 2).
{ECO:0000303|PubMed:9211900}.
/FTId=VSP_034794.
VAR_SEQ 228 228 P -> PPPLPTTPTPVPREPGRKPLSSSRLGEVTGSPSPPP
RSGAPTPSSRAPALSPTRPPKKPLDYVQDHSSGVFNE (in
isoform 3, isoform 4, isoform 5, isoform
10 and isoform 12).
{ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:9211900,
ECO:0000303|Ref.5}.
/FTId=VSP_034795.
VAR_SEQ 228 228 P -> PPPKKPLDYVQDHSSGVFNE (in isoform 8).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_045641.
VAR_SEQ 229 237 ASLYQSSID -> VSKPQAGRR (in isoform 6).
{ECO:0000303|PubMed:11786189}.
/FTId=VSP_034796.
VAR_SEQ 238 1100 Missing (in isoform 6).
{ECO:0000303|PubMed:11786189}.
/FTId=VSP_034797.
VAR_SEQ 308 834 Missing (in isoform 2, isoform 3, isoform
4, isoform 5, isoform 8, isoform 9,
isoform 10 and isoform 12).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:9211900,
ECO:0000303|Ref.5}.
/FTId=VSP_034798.
VAR_SEQ 1050 1100 YNYTPRNEDELELRESDVIDVMEKCDDGWFVGTSRRTKFFG
TFPGNYVKRL -> GYTLT (in isoform 5).
{ECO:0000303|PubMed:9211900}.
/FTId=VSP_034799.
VARIANT 1048 1048 A -> V (in dbSNP:rs725185).
/FTId=VAR_045624.
CONFLICT 73 73 P -> L (in Ref. 5; AK225327).
{ECO:0000305}.
CONFLICT 206 206 R -> Q (in Ref. 5; AK225327).
{ECO:0000305}.
CONFLICT 231 231 L -> S (in Ref. 4; BAG51769).
{ECO:0000305}.
CONFLICT 536 536 L -> P (in Ref. 4; BAG51769).
{ECO:0000305}.
CONFLICT 891 891 Y -> N (in Ref. 4; BAG51769).
{ECO:0000305}.
CONFLICT 1034 1034 F -> L (in Ref. 4; BAH11501).
{ECO:0000305}.
STRAND 866 872 {ECO:0000244|PDB:5VEI}.
STRAND 889 905 {ECO:0000244|PDB:5VEI}.
STRAND 908 913 {ECO:0000244|PDB:5VEI}.
HELIX 914 916 {ECO:0000244|PDB:5VEI}.
STRAND 917 919 {ECO:0000244|PDB:5VEI}.
SEQUENCE 1100 AA; 124108 MW; 7E98B196D4DB38E6 CRC64;
MSYYQRPFSP SAYSLPASLN SSIVMQHGTS LDSTDTYPQH AQSLDGTTSS SIPLYRSSEE
EKRVTVIKAP HYPGIGPVDE SGIPTAIRTT VDRPKDWYKT MFKQIHMVHK PDDDTDMYNT
PYTYNAGLYN PPYSAQSHPA AKTQTYRPLS KSHSDNSPNA FKDASSPVPP PHVPPPVPPL
RPRDRSSTEK HDWDPPDRKV DTRKFRSEPR SIFEYEPGKS SILQHERPAS LYQSSIDRSL
ERPMSSASMA SDFRKRRKSE PAVGPPRGLG DQSASRTSPG RVDLPGSSTT LTKSFTSSSP
SSPSRAKGGD DSKICPSLCS YSGLNGNPSS ELDYCSTYRQ HLDVPRDSPR AISFKNGWQM
ARQNAEIWSS TEETVSPKIK SRSCDDLLND DCDSFPDPKV KSESMGSLLC EEDSKESCPM
AWGSPYVPEV RSNGRSRIRH RSARNAPGFL KMYKKMHRIN RKDLMNSEVI CSVKSRILQY
ESEQQHKDLL RAWSQCSTEE VPRDMVPTRI SEFEKLIQKS KSMPNLGDDM LSPVTLEPPQ
NGLCPKRRFS IEYLLEEENQ SGPPARGRRG CQSNALVPIH IEVTSDEQPR AHVEFSDSDQ
DGVVSDHSDY IHLEGSSFCS ESDFDHFSFT SSESFYGSSH HHHHHHHHHH RHLISSCKGR
CPASYTRFTT MLKHERARHE NTEEPRRQEM DPGLSKLAFL VSPVPFRRKK NSAPKKQTEK
AKCKASVFEA LDSALKDICD QIKAEKKRGS LPDNSILHRL ISELLPDVPE RNSSLRALRR
SPLHQPLHPL PPDGAIHCPP YQNDCGRMPR SASFQDVDTA NSSCHHQDRG GALQDRESPR
SYSSTLTDMG RSAPRERRGT PEKEKLPAKA VYDFKAQTSK ELSFKKGDTV YILRKIDQNW
YEGEHHGRVG IFPISYVEKL TPPEKAQPAR PPPPAQPGEI GEAIAKYNFN ADTNVELSLR
KGDRVILLKR VDQNWYEGKI PGTNRQGIFP VSYVEVVKKN TKGAEDYPDP PIPHSYSSDR
IHSLSSNKPQ RPVFTHENIQ GGGEPFQALY NYTPRNEDEL ELRESDVIDV MEKCDDGWFV
GTSRRTKFFG TFPGNYVKRL


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