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O75563

- SKAP2_HUMAN

UniProt

O75563 - SKAP2_HUMAN

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Protein

Src kinase-associated phosphoprotein 2

Gene
SKAP2, PRAP, RA70, SAPS, SCAP2, SKAP55R
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

May be involved in B-cell and macrophage adhesion processes. In B-cells, may act by coupling the B-cell receptor (BCR) to integrin activation. May play a role in src signaling pathway.2 Publications

GO - Molecular functioni

  1. SH3/SH2 adaptor activity Source: ProtInc

GO - Biological processi

  1. B cell activation Source: UniProtKB-KW
  2. negative regulation of cell proliferation Source: Ensembl
  3. positive regulation of signal transduction Source: GOC
  4. protein complex assembly Source: ProtInc
  5. signal transduction Source: ProtInc
Complete GO annotation...

Keywords - Biological processi

B-cell activation

Enzyme and pathway databases

ReactomeiREACT_23916. Signal regulatory protein (SIRP) family interactions.
SignaLinkiO75563.

Names & Taxonomyi

Protein namesi
Recommended name:
Src kinase-associated phosphoprotein 2
Alternative name(s):
Pyk2/RAFTK-associated protein
Retinoic acid-induced protein 70
SKAP55 homolog
Short name:
SKAP-55HOM
Short name:
SKAP-HOM
Src family-associated phosphoprotein 2
Src kinase-associated phosphoprotein 55-related protein
Src-associated adapter protein with PH and SH3 domains
Gene namesi
Name:SKAP2
Synonyms:PRAP, RA70, SAPS, SCAP2, SKAP55R
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 7

Organism-specific databases

HGNCiHGNC:15687. SKAP2.

Subcellular locationi

Cytoplasm 1 Publication

GO - Cellular componenti

  1. cytoplasm Source: HPA
  2. cytosol Source: Reactome
  3. nucleus Source: HPA
  4. plasma membrane Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA162403393.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 359359Src kinase-associated phosphoprotein 2PRO_0000270179Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei75 – 751Phosphotyrosine1 Publication
Modified residuei151 – 1511Phosphotyrosine By similarity
Modified residuei261 – 2611Phosphotyrosine By similarity

Post-translational modificationi

Phosphorylated in resting platelets. Phosphorylated by FYN on Tyr-261 upon T-cell activation Inferred. Dephosphorylated on Tyr-75 by PTPN22.5 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiO75563.
PRIDEiO75563.

2D gel databases

OGPiO75563.

PTM databases

PhosphoSiteiO75563.

Expressioni

Tissue specificityi

Ubiquitously expressed. Present in platelets (at protein level).3 Publications

Inductioni

By retinoic acid.2 Publications

Gene expression databases

ArrayExpressiO75563.
BgeeiO75563.
CleanExiHS_SKAP2.
GenevestigatoriO75563.

Organism-specific databases

HPAiHPA005560.
HPA024045.

Interactioni

Subunit structurei

Homodimer By similarity. Interacts with PTPNS1. Part of a complex consisting of SKAP2, FYB and PTPNS1. Part of a complex consisting of SKAP2, FYB and LILRB3. May interact with actin By similarity. Interacts with FYB, which is required for SKAP2 protein stability. Interacts with LAT, GRB2, PTK2B and PRAM1. May interact with FYN, HCK and LYN. Interacts with FASLG.7 Publications

Protein-protein interaction databases

BioGridi114448. 11 interactions.
IntActiO75563. 3 interactions.
STRINGi9606.ENSP00000005587.

Structurei

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3OMHX-ray2.90E/F/G/H71-79[»]
ProteinModelPortaliO75563.
SMRiO75563. Positions 14-221, 304-359.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini116 – 219104PHAdd
BLAST
Domaini297 – 35862SH3Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni14 – 6451Homodimerization By similarityAdd
BLAST

Domaini

The SH3 domain interacts with FYB and PTK2B.

Sequence similaritiesi

Belongs to the SKAP family.
Contains 1 PH domain.
Contains 1 SH3 domain.

Keywords - Domaini

SH3 domain

Phylogenomic databases

eggNOGiNOG46742.
HOGENOMiHOG000231109.
HOVERGENiHBG052827.
InParanoidiO75563.
OMAiWDCTGAL.
OrthoDBiEOG7K6PVB.
PhylomeDBiO75563.
TreeFamiTF331055.

Family and domain databases

Gene3Di2.30.29.30. 1 hit.
InterProiIPR001849. PH_domain.
IPR011993. PH_like_dom.
IPR001452. SH3_domain.
[Graphical view]
PfamiPF00169. PH. 1 hit.
PF14604. SH3_9. 1 hit.
[Graphical view]
PRINTSiPR00452. SH3DOMAIN.
SMARTiSM00233. PH. 1 hit.
SM00326. SH3. 1 hit.
[Graphical view]
SUPFAMiSSF50044. SSF50044. 1 hit.
PROSITEiPS50003. PH_DOMAIN. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O75563-1 [UniParc]FASTAAdd to Basket

« Hide

MPNPSSTSSP YPLPEEIRNL LADVETFVAD ILKGENLSKK AKEKRESLIK    50
KIKDVKSIYL QEFQDKGDAE DGEEYDDPFA GPPDTISLAS ERYDKDDEAP 100
SDGAQFPPIA AQDLPFVLKA GYLEKRRKDH SFLGFEWQKR WCALSKTVFY 150
YYGSDKDKQQ KGEFAIDGYS VRMNNTLRKD GKKDCCFEIS APDKRIYQFT 200
AASPKDAEEW VQQLKFVLQD MESDIIPEDY DERGELYDDV DHPLPISNPL 250
TSSQPIDDEI YEELPEEEED SAPVKVEEQR KMSQDSVHHT SGDKSTDYAN 300
FYQGLWDCTG AFSDELSFKR GDVIYILSKE YNRYGWWVGE MKGAIGLVPK 350
AYIMEMYDI 359
Length:359
Mass (Da):41,217
Last modified:November 1, 1998 - v1
Checksum:i65F266535A89281E
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti202 – 2021A → S.3 Publications
Corresponds to variant rs1129771 [ dbSNP | Ensembl ].
VAR_029812
Natural varianti253 – 2531S → T.
Corresponds to variant rs17154402 [ dbSNP | Ensembl ].
VAR_029813

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti6 – 61S → C in BAA36194. 1 Publication
Sequence conflicti352 – 3521Y → H in BAD96605. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB014486 mRNA. Translation: BAA36194.1.
AJ004886 mRNA. Translation: CAA06193.1.
AF072166 mRNA. Translation: AAC39924.1.
AF051323 mRNA. Translation: AAC99296.1.
AK313209 mRNA. Translation: BAG36025.1.
AK222885 mRNA. Translation: BAD96605.1.
AC003999 Genomic DNA. Translation: AAS02033.1.
AC011299 Genomic DNA. Translation: AAS07536.1.
CH236948 Genomic DNA. Translation: EAL24231.1.
CH471073 Genomic DNA. Translation: EAW93859.1.
BC002893 mRNA. Translation: AAH02893.1.
BC036044 mRNA. Translation: AAH36044.1.
CCDSiCCDS5400.1.
RefSeqiNP_003921.2. NM_003930.3.
XP_005249958.1. XM_005249901.1.
UniGeneiHs.200770.
Hs.610137.

Genome annotation databases

EnsembliENST00000345317; ENSP00000005587; ENSG00000005020.
GeneIDi8935.
KEGGihsa:8935.
UCSCiuc003syc.3. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB014486 mRNA. Translation: BAA36194.1 .
AJ004886 mRNA. Translation: CAA06193.1 .
AF072166 mRNA. Translation: AAC39924.1 .
AF051323 mRNA. Translation: AAC99296.1 .
AK313209 mRNA. Translation: BAG36025.1 .
AK222885 mRNA. Translation: BAD96605.1 .
AC003999 Genomic DNA. Translation: AAS02033.1 .
AC011299 Genomic DNA. Translation: AAS07536.1 .
CH236948 Genomic DNA. Translation: EAL24231.1 .
CH471073 Genomic DNA. Translation: EAW93859.1 .
BC002893 mRNA. Translation: AAH02893.1 .
BC036044 mRNA. Translation: AAH36044.1 .
CCDSi CCDS5400.1.
RefSeqi NP_003921.2. NM_003930.3.
XP_005249958.1. XM_005249901.1.
UniGenei Hs.200770.
Hs.610137.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3OMH X-ray 2.90 E/F/G/H 71-79 [» ]
ProteinModelPortali O75563.
SMRi O75563. Positions 14-221, 304-359.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 114448. 11 interactions.
IntActi O75563. 3 interactions.
STRINGi 9606.ENSP00000005587.

PTM databases

PhosphoSitei O75563.

2D gel databases

OGPi O75563.

Proteomic databases

PaxDbi O75563.
PRIDEi O75563.

Protocols and materials databases

DNASUi 8935.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000345317 ; ENSP00000005587 ; ENSG00000005020 .
GeneIDi 8935.
KEGGi hsa:8935.
UCSCi uc003syc.3. human.

Organism-specific databases

CTDi 8935.
GeneCardsi GC07M026706.
H-InvDB HIX0025350.
HGNCi HGNC:15687. SKAP2.
HPAi HPA005560.
HPA024045.
MIMi 605215. gene.
neXtProti NX_O75563.
PharmGKBi PA162403393.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG46742.
HOGENOMi HOG000231109.
HOVERGENi HBG052827.
InParanoidi O75563.
OMAi WDCTGAL.
OrthoDBi EOG7K6PVB.
PhylomeDBi O75563.
TreeFami TF331055.

Enzyme and pathway databases

Reactomei REACT_23916. Signal regulatory protein (SIRP) family interactions.
SignaLinki O75563.

Miscellaneous databases

ChiTaRSi SKAP2. human.
GeneWikii SKAP2.
GenomeRNAii 8935.
NextBioi 33596.
PROi O75563.
SOURCEi Search...

Gene expression databases

ArrayExpressi O75563.
Bgeei O75563.
CleanExi HS_SKAP2.
Genevestigatori O75563.

Family and domain databases

Gene3Di 2.30.29.30. 1 hit.
InterProi IPR001849. PH_domain.
IPR011993. PH_like_dom.
IPR001452. SH3_domain.
[Graphical view ]
Pfami PF00169. PH. 1 hit.
PF14604. SH3_9. 1 hit.
[Graphical view ]
PRINTSi PR00452. SH3DOMAIN.
SMARTi SM00233. PH. 1 hit.
SM00326. SH3. 1 hit.
[Graphical view ]
SUPFAMi SSF50044. SSF50044. 1 hit.
PROSITEi PS50003. PH_DOMAIN. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, INDUCTION, POSSIBLE INTERACTION WITH FYN; HCK AND LYN, FUNCTION, VARIANT SER-202.
    Tissue: Testis.
  2. "SKAP-HOM, a novel adaptor protein homologous to the FYN-associated protein SKAP55."
    Marie-Cardine A., Verhagen A.M., Eckerskorn C., Schraven B.
    FEBS Lett. 435:55-60(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, PHOSPHORYLATION, INTERACTION WITH FYB, VARIANT SER-202.
    Tissue: Leukocyte.
  3. "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."
    Liu J., Kang H., Raab M., da Silva A.J., Kraeft S.-K., Rudd C.E.
    Proc. Natl. Acad. Sci. U.S.A. 95:8779-8784(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH FYB, PHOSPHORYLATION.
    Tissue: Lymphocyte.
  4. "Identification and characterization of a novel Pyk2/related adhesion focal tyrosine kinase-associated protein that inhibits alpha-synuclein phosphorylation."
    Takahashi T., Yamashita H., Nagano Y., Nakamura T., Ohmori H., Avraham H., Avraham S., Yasuda M., Matsumoto M.
    J. Biol. Chem. 278:42225-42233(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH PTK2B, PHOSPHORYLATION, SUBCELLULAR LOCATION, FUNCTION.
    Tissue: Hippocampus.
  5. "Src-associated adaptor protein with PH and SH3 domain."
    Lee J.-S., Suh K.S., Burr J.G.
    Submitted (FEB-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT SER-202.
    Tissue: Pancreas.
  6. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    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.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  7. Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
    Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Liver.
  8. "The DNA sequence of human chromosome 7."
    Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L.
    , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
    Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  9. "Human chromosome 7: DNA sequence and biology."
    Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K., Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R., Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A., Kanematsu E., Gentles S.
    , Christopoulos C.C., Choufani S., Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H., Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J., Adams M.D., Tsui L.-C.
    Science 300:767-772(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  10. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  11. "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].
    Tissue: Lung and Testis.
  12. "Interaction of linker for activation of T cells with multiple adapter proteins in platelets activated by the glycoprotein VI-selective ligand, convulxin."
    Asazuma N., Wilde J.I., Berlanga O., Leduc M., Leo A., Schweighoffer E., Tybulewicz V., Bon C., Liu S.K., McGlade C.J., Schraven B., Watson S.P.
    J. Biol. Chem. 275:33427-33434(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION, INTERACTION WITH FYB; LAT AND GRB2, TISSUE SPECIFICITY.
  13. "PRAM-1 is a novel adaptor protein regulated by retinoic acid (RA) and promyelocytic leukemia (PML)-RA receptor alpha in acute promyelocytic leukemia cells."
    Moog-Lutz C., Peterson E.J., Lutz P.G., Eliason S., Cave-Riant F., Singer A., Di Gioia Y., Dmovski S., Kamens J., Cayre Y.E., Koretzky G.
    J. Biol. Chem. 276:22375-22381(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION, INTERACTION WITH PRAM1.
  14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  15. "Identification of SH3 domain interaction partners of human FasL (CD178) by phage display screening."
    Voss M., Lettau M., Janssen O.
    BMC Immunol. 10:53-53(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH FASLG.
  16. "Substrate specificity of lymphoid-specific tyrosine phosphatase (Lyp) and identification of Src kinase-associated protein of 55 kDa homolog (SKAP-HOM) as a Lyp substrate."
    Yu X., Chen M., Zhang S., Yu Z.H., Sun J.P., Wang L., Liu S., Imasaki T., Takagi Y., Zhang Z.Y.
    J. Biol. Chem. 286:30526-30534(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 71-79 IN COMPLEX WITH PTPN22, PHOSPHORYLATION AT TYR-75.

Entry informationi

Entry nameiSKAP2_HUMAN
AccessioniPrimary (citable) accession number: O75563
Secondary accession number(s): A4D173
, Q53GP6, Q75MK6, Q75MZ4, Q9UBZ3, Q9UED8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 9, 2007
Last sequence update: November 1, 1998
Last modified: September 3, 2014
This is version 115 of the entry and version 1 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 7
    Human chromosome 7: 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

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