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Src kinase-associated phosphoprotein 1 (Src family-associated phosphoprotein 1) (Src kinase-associated phosphoprotein of 55 kDa) (SKAP-55) (pp55)

 SKAP1_HUMAN             Reviewed;         359 AA.
Q86WV1; D3DTV1; O15268;
09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
24-NOV-2009, sequence version 3.
10-OCT-2018, entry version 135.
RecName: Full=Src kinase-associated phosphoprotein 1;
AltName: Full=Src family-associated phosphoprotein 1;
AltName: Full=Src kinase-associated phosphoprotein of 55 kDa;
Short=SKAP-55;
Short=pp55;
Name=SKAP1; Synonyms=SCAP1, SKAP55;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 101-110;
120-130 AND 153-158, PHOSPHORYLATION, INTERACTION WITH FYN, TISSUE
SPECIFICITY, AND VARIANT SER-161.
TISSUE=Blood;
PubMed=9195899; DOI=10.1074/jbc.272.26.16077;
Marie-Cardine A., Bruyns E., Eckerskorn C., Kirchgessner H., Meuer S.,
Schraven B.;
"Molecular cloning of SKAP55, a novel protein that associates with
p59fyn in human T-lymphocytes.";
J. Biol. Chem. 272:16077-16080(1997).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16625196; DOI=10.1038/nature04689;
Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R.,
Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N.,
Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B.,
Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J.,
Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E.,
Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J.,
Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C.,
Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
"DNA sequence of human chromosome 17 and analysis of rearrangement in
the human lineage.";
Nature 440:1045-1049(2006).
[3]
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.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Pancreas;
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).
[5]
INTERACTION WITH FYB1, AND MUTAGENESIS OF TRP-333.
PubMed=9748251; DOI=10.1074/jbc.273.40.25789;
Marie-Cardine A., Hendricks-Taylor L.R., Boerth N.J., Zhao H.,
Schraven B., Koretzky G.A.;
"Molecular interaction between the Fyn-associated protein SKAP55 and
the SLP-76-associated phosphoprotein SLAP-130.";
J. Biol. Chem. 273:25789-25795(1998).
[6]
INTERACTION WITH FYB1, AND SUBCELLULAR LOCATION.
PubMed=9671755; DOI=10.1073/pnas.95.15.8779;
Liu J., Kang H., Raab M., da Silva A.J., Kraeft S.-K., Rudd C.E.;
"FYB (FYN binding protein) serves as a binding partner for lymphoid
protein and FYN kinase substrate SKAP55 and a SKAP55-related protein
in T cells.";
Proc. Natl. Acad. Sci. U.S.A. 95:8779-8784(1998).
[7]
INTERACTION WITH FYB1, MUTAGENESIS OF TYR-295 AND TYR-298, AND
FUNCTION.
PubMed=10856234; DOI=10.1093/emboj/19.12.2889;
Kang H., Freund C., Duke-Cohan J.S., Musacchio A., Wagner G.,
Rudd C.E.;
"SH3 domain recognition of a proline-independent tyrosine-based
RKxxYxxY motif in immune cell adaptor SKAP55.";
EMBO J. 19:2889-2899(2000).
[8]
HOMODIMERIZATION, MUTAGENESIS OF TYR-219; TYR-232; TYR-271 AND
TRP-333, PHOSPHORYLATION, AND INTERACTION WITH GRB2.
PubMed=12171928; DOI=10.1074/jbc.M206023200;
Wu L., Yu Z., Shen S.-H.;
"SKAP55 recruits to lipid rafts and positively mediates the MAPK
pathway upon T cell receptor activation.";
J. Biol. Chem. 277:40420-40427(2002).
[9]
PHOSPHORYLATION AT TYR-219 AND TYR-232, DEPHOSPHORYLATION BY PTPRC,
MUTAGENESIS OF TYR-219; TYR-232 AND TYR-271, SUBCELLULAR LOCATION,
FUNCTION, AND INTERACTION WITH PTPRC.
PubMed=11909961; DOI=10.1128/MCB.22.8.2673-2686.2002;
Wu L., Fu J., Shen S.-H.;
"SKAP55 coupled with CD45 positively regulates T-cell receptor-
mediated gene transcription.";
Mol. Cell. Biol. 22:2673-2686(2002).
[10]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=12652296; DOI=10.1038/ni913;
Wang H., Moon E.-Y., Azouz A., Wu X., Smith A., Schneider H., Hogg N.,
Rudd C.E.;
"SKAP-55 regulates integrin adhesion and formation of T cell-APC
conjugates.";
Nat. Immunol. 4:366-374(2003).
[11]
INTERACTION WITH FYB1, AND MUTAGENESIS OF TRP-333.
PubMed=15849195; DOI=10.1074/jbc.M413201200;
Huang Y., Norton D.D., Precht P., Martindale J.L., Burkhardt J.K.,
Wange R.L.;
"Deficiency of ADAP/Fyb/SLAP-130 destabilizes SKAP55 in Jurkat T
cells.";
J. Biol. Chem. 280:23576-23583(2005).
[12]
FUNCTION.
PubMed=15939789; DOI=10.1084/jem.20042577;
Jo E.-K., Wang H., Rudd C.E.;
"An essential role for SKAP-55 in LFA-1 clustering on T cells that
cannot be substituted by SKAP-55R.";
J. Exp. Med. 201:1733-1739(2005).
[13]
PHOSPHORYLATION, AND INTERACTION WITH FYB1.
PubMed=16461356; DOI=10.1074/jbc.M508774200;
Duke-Cohan J.S., Kang H., Liu H., Rudd C.E.;
"Regulation and function of SKAP-55 non-canonical motif binding to the
SH3c domain of adhesion and degranulation-promoting adaptor protein.";
J. Biol. Chem. 281:13743-13750(2006).
[14]
FUNCTION.
PubMed=16980616; DOI=10.1128/MCB.00331-06;
Kliche S., Breitling D., Togni M., Pusch R., Heuer K., Wang X.,
Freund C., Kasirer-Friede A., Menasche G., Koretzky G.A., Schraven B.;
"The ADAP/SKAP55 signaling module regulates T-cell receptor-mediated
integrin activation through plasma membrane targeting of Rap1.";
Mol. Cell. Biol. 26:7130-7144(2006).
[15]
INTERACTION WITH RASGRP1.
PubMed=17658605; DOI=10.1016/j.molimm.2007.05.024;
Kosco K.A., Cerignoli F., Williams S., Abraham R.T., Mustelin T.;
"SKAP55 modulates T cell antigen receptor-induced activation of the
Ras-Erk-AP1 pathway by binding RasGRP1.";
Mol. Immunol. 45:510-522(2008).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-271, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[17]
INTERACTION WITH FYB2 AND FYB1.
PubMed=27335501; DOI=10.4049/jimmunol.1501913;
Jung S.H., Yoo E.H., Yu M.J., Song H.M., Kang H.Y., Cho J.Y.,
Lee J.R.;
"ARAP, a novel adaptor protein, is required for TCR signaling and
integrin-mediated adhesion.";
J. Immunol. 197:942-952(2016).
[18]
X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 108-213.
Tang Y., Swanson K.D., Neel B.G., Eck M.J.;
"Structural basis for the dimerization and phosphoinositide
specificity of the Src kinase-associated phosphoproteins SKAP55 and
SKAP-HOM.";
Submitted (JUL-2005) to the PDB data bank.
-!- FUNCTION: Positively regulates T-cell receptor signaling by
enhancing the MAP kinase pathway. Required for optimal conjugation
between T-cells and antigen-presenting cells by promoting the
clustering of integrin ITGAL on the surface of T-cells. May be
involved in high affinity immunoglobulin epsilon receptor
signaling in mast cells. {ECO:0000269|PubMed:10856234,
ECO:0000269|PubMed:11909961, ECO:0000269|PubMed:12652296,
ECO:0000269|PubMed:15939789, ECO:0000269|PubMed:16980616}.
-!- SUBUNIT: Homodimer. Interacts with FYN (PubMed:9195899). Interacts
with PTPRC (PubMed:11909961). Interacts with GRB2 when
phosphorylated on Tyr-271 (PubMed:12171928). Interacts with FYB1,
which is required for SKAP2 protein stability (PubMed:10856234,
PubMed:27335501, PubMed:9671755, PubMed:10856234, PubMed:15849195,
PubMed:16461356). Part of a complex consisting of SKAP1, FYB1 and
CLNK (By similarity). Interacts with RASGRP1 (PubMed:17658605).
Interacts with FYB2 (PubMed:27335501).
{ECO:0000250|UniProtKB:Q4V7G1, ECO:0000269|PubMed:10856234,
ECO:0000269|PubMed:12171928, ECO:0000269|PubMed:15849195,
ECO:0000269|PubMed:16461356, ECO:0000269|PubMed:17658605,
ECO:0000269|PubMed:27335501, ECO:0000269|PubMed:9195899,
ECO:0000269|PubMed:9671755, ECO:0000269|PubMed:9748251}.
-!- INTERACTION:
P62952:BLCAP; NbExp=3; IntAct=EBI-2477305, EBI-3895726;
Q5T9C2:FAM102A; NbExp=3; IntAct=EBI-2477305, EBI-10246318;
O15117:FYB1; NbExp=6; IntAct=EBI-2477305, EBI-1753267;
Q96QH2:PRAM1; NbExp=3; IntAct=EBI-2477305, EBI-2860740;
Q9H788:SH2D4A; NbExp=3; IntAct=EBI-2477305, EBI-747035;
Q9H788-2:SH2D4A; NbExp=3; IntAct=EBI-2477305, EBI-10308083;
-!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Note=Upon
T-cell stimulation, translocates to lipid rafts at the cell
membrane.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q86WV1-1; Sequence=Displayed;
Name=2;
IsoId=Q86WV1-2; Sequence=VSP_022179;
-!- TISSUE SPECIFICITY: Highly expressed in thymocytes and peripheral
blood lymphocytes. Also expressed in spleen cells and testis.
Present in T-cells (at protein level).
{ECO:0000269|PubMed:9195899}.
-!- DOMAIN: The SH3 domain interacts with FYB1.
-!- PTM: Phosphorylated on tyrosines. Phosphorylation by FYN on Tyr-
271 is required for GRB2 interaction. Phosphorylation by FYN on
Tyr-295 abolishes interaction with FYB1. Tyr-232 is
dephosphorylated by PTPRC (Probable).
{ECO:0000305|PubMed:11909961, ECO:0000305|PubMed:12171928,
ECO:0000305|PubMed:16461356, ECO:0000305|PubMed:9195899}.
-!- SIMILARITY: Belongs to the SKAP family. {ECO:0000305}.
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EMBL; Y11215; CAA72101.1; -; mRNA.
EMBL; AC006468; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC027152; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC036222; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC090627; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471109; EAW94749.1; -; Genomic_DNA.
EMBL; CH471109; EAW94750.1; -; Genomic_DNA.
EMBL; BC047870; AAH47870.1; -; mRNA.
CCDS; CCDS32674.1; -. [Q86WV1-1]
RefSeq; NP_001068567.1; NM_001075099.1. [Q86WV1-2]
RefSeq; NP_003717.3; NM_003726.3. [Q86WV1-1]
UniGene; Hs.316931; -.
PDB; 1U5D; X-ray; 1.70 A; A/B/C/D=108-213.
PDBsum; 1U5D; -.
ProteinModelPortal; Q86WV1; -.
SMR; Q86WV1; -.
BioGrid; 114184; 101.
IntAct; Q86WV1; 7.
MINT; Q86WV1; -.
STRING; 9606.ENSP00000338171; -.
iPTMnet; Q86WV1; -.
PhosphoSitePlus; Q86WV1; -.
BioMuta; SKAP1; -.
DMDM; 269849660; -.
MaxQB; Q86WV1; -.
PaxDb; Q86WV1; -.
PeptideAtlas; Q86WV1; -.
PRIDE; Q86WV1; -.
ProteomicsDB; 70207; -.
ProteomicsDB; 70208; -. [Q86WV1-2]
DNASU; 8631; -.
Ensembl; ENST00000336915; ENSP00000338171; ENSG00000141293. [Q86WV1-1]
Ensembl; ENST00000584924; ENSP00000464311; ENSG00000141293. [Q86WV1-1]
GeneID; 8631; -.
KEGG; hsa:8631; -.
UCSC; uc002ini.2; human. [Q86WV1-1]
CTD; 8631; -.
DisGeNET; 8631; -.
EuPathDB; HostDB:ENSG00000141293.15; -.
GeneCards; SKAP1; -.
HGNC; HGNC:15605; SKAP1.
HPA; CAB025882; -.
HPA; CAB055513; -.
HPA; HPA002969; -.
MIM; 604969; gene.
neXtProt; NX_Q86WV1; -.
OpenTargets; ENSG00000141293; -.
PharmGKB; PA162403362; -.
eggNOG; ENOG410IENN; Eukaryota.
eggNOG; ENOG410YF8P; LUCA.
GeneTree; ENSGT00390000017856; -.
HOGENOM; HOG000231109; -.
HOVERGEN; HBG052827; -.
InParanoid; Q86WV1; -.
KO; K17699; -.
OMA; HLRRDSK; -.
OrthoDB; EOG091G0HBY; -.
PhylomeDB; Q86WV1; -.
TreeFam; TF331055; -.
SignaLink; Q86WV1; -.
SIGNOR; Q86WV1; -.
ChiTaRS; SKAP1; human.
EvolutionaryTrace; Q86WV1; -.
GeneWiki; SKAP1; -.
GenomeRNAi; 8631; -.
PRO; PR:Q86WV1; -.
Proteomes; UP000005640; Chromosome 17.
Bgee; ENSG00000141293; Expressed in 134 organ(s), highest expression level in leukocyte.
CleanEx; HS_SKAP1; -.
ExpressionAtlas; Q86WV1; baseline and differential.
Genevisible; Q86WV1; HS.
GO; GO:0005911; C:cell-cell junction; IEA:Ensembl.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0001772; C:immunological synapse; IDA:BHF-UCL.
GO; GO:0005634; C:nucleus; IDA:HPA.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0044853; C:plasma membrane raft; IDA:BHF-UCL.
GO; GO:0042101; C:T cell receptor complex; IEA:Ensembl.
GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
GO; GO:0019903; F:protein phosphatase binding; IPI:UniProtKB.
GO; GO:0044877; F:protein-containing complex binding; IEA:Ensembl.
GO; GO:0042169; F:SH2 domain binding; IDA:UniProtKB.
GO; GO:0017124; F:SH3 domain binding; TAS:BHF-UCL.
GO; GO:0005070; F:SH3/SH2 adaptor activity; IBA:GO_Central.
GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
GO; GO:0002821; P:positive regulation of adaptive immune response; IDA:BHF-UCL.
GO; GO:0033634; P:positive regulation of cell-cell adhesion mediated by integrin; IGI:BHF-UCL.
GO; GO:0001954; P:positive regulation of cell-matrix adhesion; IGI:BHF-UCL.
GO; GO:0034116; P:positive regulation of heterotypic cell-cell adhesion; IDA:BHF-UCL.
GO; GO:0033625; P:positive regulation of integrin activation; IDA:BHF-UCL.
GO; GO:1903039; P:positive regulation of leukocyte cell-cell adhesion; IDA:BHF-UCL.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:BHF-UCL.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IMP:UniProtKB.
GO; GO:0072659; P:protein localization to plasma membrane; IEA:Ensembl.
GO; GO:0050852; P:T cell receptor signaling pathway; IMP:UniProtKB.
CDD; cd12044; SH3_SKAP1; 1.
Gene3D; 2.30.29.30; -; 1.
InterPro; IPR011993; PH-like_dom_sf.
InterPro; IPR001849; PH_domain.
InterPro; IPR036028; SH3-like_dom_sf.
InterPro; IPR001452; SH3_domain.
InterPro; IPR035765; SKAP1_SH3.
InterPro; IPR037781; SKAP_fam.
PANTHER; PTHR15129; PTHR15129; 1.
Pfam; PF00169; PH; 1.
Pfam; PF00018; SH3_1; 1.
PRINTS; PR00452; SH3DOMAIN.
SMART; SM00233; PH; 1.
SMART; SM00326; SH3; 1.
SUPFAM; SSF50044; SSF50044; 1.
PROSITE; PS50003; PH_DOMAIN; 1.
PROSITE; PS50002; SH3; 1.
1: Evidence at protein level;
3D-structure; Adaptive immunity; Alternative splicing; Cell membrane;
Complete proteome; Cytoplasm; Direct protein sequencing; Immunity;
Membrane; Nucleus; Phosphoprotein; Polymorphism; Reference proteome;
SH3 domain.
CHAIN 1 359 Src kinase-associated phosphoprotein 1.
/FTId=PRO_0000270173.
DOMAIN 107 210 PH. {ECO:0000255|PROSITE-
ProRule:PRU00145}.
DOMAIN 294 355 SH3. {ECO:0000255|PROSITE-
ProRule:PRU00192}.
REGION 290 295 Interaction with FYB1.
COMPBIAS 220 230 Poly-Glu.
MOD_RES 142 142 Phosphotyrosine.
{ECO:0000250|UniProtKB:Q3UUV5}.
MOD_RES 219 219 Phosphotyrosine.
{ECO:0000305|PubMed:11909961}.
MOD_RES 232 232 Phosphotyrosine.
{ECO:0000305|PubMed:11909961}.
MOD_RES 271 271 Phosphotyrosine; by FYN.
{ECO:0000244|PubMed:19690332}.
MOD_RES 295 295 Phosphotyrosine; by FYN. {ECO:0000305}.
VAR_SEQ 293 293 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_022179.
VARIANT 161 161 G -> S (in dbSNP:rs2278868).
{ECO:0000269|PubMed:9195899}.
/FTId=VAR_029811.
VARIANT 242 242 S -> G (in dbSNP:rs35288886).
/FTId=VAR_035343.
MUTAGEN 219 219 Y->F: Impairs interaction with PTPRC. No
effect on interaction with FYN or GRB2.
{ECO:0000269|PubMed:11909961,
ECO:0000269|PubMed:12171928}.
MUTAGEN 232 232 Y->F: Abolishes interaction with PTPRC,
translocation to cell membrane upon T-
cell stimulation and activation of the
MAP kinase pathway. No effect on
interaction with FYN or GRB2.
{ECO:0000269|PubMed:11909961,
ECO:0000269|PubMed:12171928}.
MUTAGEN 271 271 Y->F: No effect on interaction with PTPRC
and translocation to cell membrane upon
T-cell stimulation. Abolishes interaction
with FYN and GRB2 and activation of the
MAP kinase pathway.
{ECO:0000269|PubMed:11909961,
ECO:0000269|PubMed:12171928}.
MUTAGEN 295 295 Y->F: Abolishes FYB1-dependent activation
of ITGAL clustering.
{ECO:0000269|PubMed:10856234}.
MUTAGEN 298 298 Y->F: Impairs interaction with FYB1.
{ECO:0000269|PubMed:10856234}.
MUTAGEN 333 333 W->R: Abolishes homodimerization,
interaction with FYB1 and activation of
the MAP kinase pathway.
{ECO:0000269|PubMed:12171928,
ECO:0000269|PubMed:15849195,
ECO:0000269|PubMed:9748251}.
CONFLICT 187 187 S -> T (in Ref. 1; CAA72101).
{ECO:0000305}.
STRAND 108 119 {ECO:0000244|PDB:1U5D}.
STRAND 121 124 {ECO:0000244|PDB:1U5D}.
STRAND 126 136 {ECO:0000244|PDB:1U5D}.
STRAND 139 145 {ECO:0000244|PDB:1U5D}.
STRAND 152 156 {ECO:0000244|PDB:1U5D}.
STRAND 161 164 {ECO:0000244|PDB:1U5D}.
HELIX 166 168 {ECO:0000244|PDB:1U5D}.
HELIX 172 176 {ECO:0000244|PDB:1U5D}.
STRAND 177 181 {ECO:0000244|PDB:1U5D}.
STRAND 183 185 {ECO:0000244|PDB:1U5D}.
STRAND 188 191 {ECO:0000244|PDB:1U5D}.
HELIX 195 212 {ECO:0000244|PDB:1U5D}.
SEQUENCE 359 AA; 41432 MW; 630FE4C17295BD6D CRC64;
MQAAALPEEI RWLLEDAEEF LAEGLRNENL SAVARDHRDH ILRGFQQIKA RYYWDFQPQG
GDIGQDSSDD NHSGTLGLSL TSDAPFLSDY QDEGMEDIVK GAQELDNVIK QGYLEKKSKD
HSFFGSEWQK RWCVVSRGLF YYYANEKSKQ PKGTFLIKGY GVRMAPHLRR DSKKESCFEL
TSQDRRSYEF TATSPAEARD WVDQISFLLK DLSSLTIPYE EDEEEEEKEE TYDDIDGFDS
PSCGSQCRPT ILPGSVGIKE PTEEKEEEDI YEVLPDEEHD LEEDESGTRR KGVDYASYYQ
GLWDCHGDQP DELSFQRGDL IRILSKEYNM YGWWVGELNS LVGIVPKEYL TTAFEVEER


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EIAAB38555 Mouse,Mus musculus,Scap1,Skap1,Src family-associated phosphoprotein 1,Src kinase-associated phosphoprotein 1
EIAAB38557 Bos taurus,Bovine,SCAP2,SKAP2,Src family-associated phosphoprotein 2,Src kinase-associated phosphoprotein 2
EIAAB38556 Homo sapiens,Human,PRAP,Pyk2_RAFTK-associated protein,RA70,Retinoic acid-induced protein 70,SAPS,SCAP2,SKAP2,SKAP55 homolog,SKAP-55HOM,SKAP55R,SKAP-HOM,Src family-associated phosphoprotein 2,Src kinas
10-663-45069 Cytomegalo Virus phosphoprotein 150 (pp150) - pp150; 150 kDa matrix phosphoprotein; Basic phosphoprotein; BPP; Tegument protein UL32 N_A 0.1 mg
10-663-45069 Cytomegalo Virus phosphoprotein 150 (pp150) - pp150; 150 kDa matrix phosphoprotein; Basic phosphoprotein; BPP; Tegument protein UL32 N_A 1 mg
10-663-45069 Cytomegalo Virus phosphoprotein 150 (pp150) - pp150; 150 kDa matrix phosphoprotein; Basic phosphoprotein; BPP; Tegument protein UL32 N_A 0.5 mg
EIAAB30502 15 kDa phosphoprotein enriched in astrocytes,Astrocytic phosphoprotein PEA-15,Homo sapiens,Human,PEA15,PED,Phosphoprotein enriched in diabetes
EIAAB27510 140 kDa nucleolar phosphoprotein,Nolc1,Nopp140,Nucleolar 130 kDa protein,Nucleolar and coiled-body phosphoprotein 1,Nucleolar phosphoprotein p130,Rat,Rattus norvegicus
EIAAB30501 15 kDa phosphoprotein enriched in astrocytes,Astrocytic phosphoprotein PEA-15,Pea15,Rat,Rattus norvegicus
10-663-45065 Cytomegalo Virus phosphoprotein-28 (pp28_UL99) - 28 kDa structural phosphoprotein; PP28 N_A 1 mg
10-663-45065 Cytomegalo Virus phosphoprotein-28 (pp28_UL99) - 28 kDa structural phosphoprotein; PP28 N_A 0.1 mg
10-663-45065 Cytomegalo Virus phosphoprotein-28 (pp28_UL99) - 28 kDa structural phosphoprotein; PP28 N_A 0.5 mg
EIAAB30500 15 kDa phosphoprotein enriched in astrocytes,Astrocytic phosphoprotein PEA-15,Mouse,Mus musculus,Pea15,Pea15a
EIAAB29727 Cbp,Csk-binding protein,Pag,Pag1,Phosphoprotein associated with glycosphingolipid-enriched microdomains 1,Rat,Rattus norvegicus,Transmembrane phosphoprotein Cbp
EIAAB29729 Cbp,Csk-binding protein,Mouse,Mus musculus,Pag,Pag1,Phosphoprotein associated with glycosphingolipid-enriched microdomains 1,Transmembrane phosphoprotein Cbp
18-785-210444 Stathmin 1 (Ab-37) - Phosphoprotein p19; pp19; Oncoprotein 18; Op18; Leukemia-associated phosphoprotein p18; pp17; Prosolin; Metablastin; Protein Pr22 Polyclonal 0.1 mg
18-785-210443 Stathmin 1 (Ab-24) - Phosphoprotein p19; pp19; Oncoprotein 18; Op18; Leukemia-associated phosphoprotein p18; pp17; Prosolin; Metablastin; Protein Pr22 Polyclonal 0.05 mg
18-785-210445 Stathmin 1 (Ab-15) - Phosphoprotein p19; pp19; Oncoprotein 18; Op18; Leukemia-associated phosphoprotein p18; pp17; Prosolin; Metablastin; Protein Pr22 Polyclonal 0.1 mg
18-785-210444 Stathmin 1 (Ab-37) - Phosphoprotein p19; pp19; Oncoprotein 18; Op18; Leukemia-associated phosphoprotein p18; pp17; Prosolin; Metablastin; Protein Pr22 Polyclonal 0.05 mg
18-785-210443 Stathmin 1 (Ab-24) - Phosphoprotein p19; pp19; Oncoprotein 18; Op18; Leukemia-associated phosphoprotein p18; pp17; Prosolin; Metablastin; Protein Pr22 Polyclonal 0.1 mg
18-785-210445 Stathmin 1 (Ab-15) - Phosphoprotein p19; pp19; Oncoprotein 18; Op18; Leukemia-associated phosphoprotein p18; pp17; Prosolin; Metablastin; Protein Pr22 Polyclonal 0.05 mg


 

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