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O75563 (SKAP2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 112. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:SKAP2
Synonyms:PRAP, RA70, SAPS, SCAP2, SKAP55R
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length359 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.1 Ref.4

Subunit structure

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. Ref.1 Ref.2 Ref.3 Ref.4 Ref.12 Ref.13 Ref.15

Subcellular location

Cytoplasm Ref.4.

Tissue specificity

Ubiquitously expressed. Present in platelets (at protein level). Ref.1 Ref.2 Ref.12

Induction

By retinoic acid. Ref.1 Ref.13

Domain

The SH3 domain interacts with FYB and PTK2B.

Post-translational modification

Phosphorylated in resting platelets. Phosphorylated by FYN on Tyr-261 upon T-cell activation Probable. Dephosphorylated on Tyr-75 by PTPN22. Ref.2 Ref.3 Ref.4 Ref.12 Ref.16

Sequence similarities

Belongs to the SKAP family.

Contains 1 PH domain.

Contains 1 SH3 domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 359359Src kinase-associated phosphoprotein 2
PRO_0000270179

Regions

Domain116 – 219104PH
Domain297 – 35862SH3
Region14 – 6451Homodimerization By similarity

Amino acid modifications

Modified residue751Phosphotyrosine Ref.16
Modified residue1511Phosphotyrosine By similarity
Modified residue2611Phosphotyrosine By similarity

Natural variations

Natural variant2021A → S. Ref.1 Ref.2 Ref.5
Corresponds to variant rs1129771 [ dbSNP | Ensembl ].
VAR_029812
Natural variant2531S → T.
Corresponds to variant rs17154402 [ dbSNP | Ensembl ].
VAR_029813

Experimental info

Sequence conflict61S → C in BAA36194. Ref.1
Sequence conflict3521Y → H in BAD96605. Ref.7

Sequences

Sequence LengthMass (Da)Tools
O75563 [UniParc].

Last modified November 1, 1998. Version 1.
Checksum: 65F266535A89281E

FASTA35941,217
        10         20         30         40         50         60 
MPNPSSTSSP YPLPEEIRNL LADVETFVAD ILKGENLSKK AKEKRESLIK KIKDVKSIYL 

        70         80         90        100        110        120 
QEFQDKGDAE DGEEYDDPFA GPPDTISLAS ERYDKDDEAP SDGAQFPPIA AQDLPFVLKA 

       130        140        150        160        170        180 
GYLEKRRKDH SFLGFEWQKR WCALSKTVFY YYGSDKDKQQ KGEFAIDGYS VRMNNTLRKD 

       190        200        210        220        230        240 
GKKDCCFEIS APDKRIYQFT AASPKDAEEW VQQLKFVLQD MESDIIPEDY DERGELYDDV 

       250        260        270        280        290        300 
DHPLPISNPL TSSQPIDDEI YEELPEEEED SAPVKVEEQR KMSQDSVHHT SGDKSTDYAN 

       310        320        330        340        350 
FYQGLWDCTG AFSDELSFKR GDVIYILSKE YNRYGWWVGE MKGAIGLVPK AYIMEMYDI 

« Hide

References

« Hide 'large scale' references
[1]"RA70 is a src kinase-associated protein expressed ubiquitously."
Kouroku Y., Soyama A., Fujita E., Urase K., Tsukahara T., Momoi T.
Biochem. Biophys. Res. Commun. 252:738-742(1998) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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. expand/collapse author list , 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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton 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. expand/collapse author list , 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 (JUL-2005) to the EMBL/GenBank/DDBJ databases
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]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_003921.2. NM_003930.3.
XP_005249958.1. XM_005249901.1.
UniGeneHs.200770.
Hs.610137.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3OMHX-ray2.90E/F/G/H71-79[»]
ProteinModelPortalO75563.
SMRO75563. Positions 14-221, 299-356.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114448. 11 interactions.
IntActO75563. 3 interactions.
STRING9606.ENSP00000005587.

PTM databases

PhosphoSiteO75563.

2D gel databases

OGPO75563.

Proteomic databases

PaxDbO75563.
PRIDEO75563.

Protocols and materials databases

DNASU8935.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000345317; ENSP00000005587; ENSG00000005020.
GeneID8935.
KEGGhsa:8935.
UCSCuc003syc.3. human.

Organism-specific databases

CTD8935.
GeneCardsGC07M026706.
H-InvDBHIX0025350.
HGNCHGNC:15687. SKAP2.
HPAHPA005560.
HPA024045.
MIM605215. gene.
neXtProtNX_O75563.
PharmGKBPA162403393.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG46742.
HOGENOMHOG000231109.
HOVERGENHBG052827.
InParanoidO75563.
OMAWDCTGAL.
OrthoDBEOG7K6PVB.
PhylomeDBO75563.
TreeFamTF331055.

Enzyme and pathway databases

ReactomeREACT_111155. Cell-Cell communication.
SignaLinkO75563.

Gene expression databases

ArrayExpressO75563.
BgeeO75563.
CleanExHS_SKAP2.
GenevestigatorO75563.

Family and domain databases

Gene3D2.30.29.30. 1 hit.
InterProIPR011993. PH_like_dom.
IPR001849. Pleckstrin_homology.
IPR001452. SH3_domain.
[Graphical view]
PfamPF00169. PH. 1 hit.
[Graphical view]
PRINTSPR00452. SH3DOMAIN.
SMARTSM00233. PH. 1 hit.
SM00326. SH3. 1 hit.
[Graphical view]
SUPFAMSSF50044. SSF50044. 1 hit.
PROSITEPS50003. PH_DOMAIN. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSSKAP2. human.
GeneWikiSKAP2.
GenomeRNAi8935.
NextBio33596.
PROO75563.
SOURCESearch...

Entry information

Entry nameSKAP2_HUMAN
AccessionPrimary (citable) accession number: O75563
Secondary accession number(s): A4D173 expand/collapse secondary AC list , Q53GP6, Q75MK6, Q75MZ4, Q9UBZ3, Q9UED8
Entry history
Integrated into UniProtKB/Swiss-Prot: January 9, 2007
Last sequence update: November 1, 1998
Last modified: April 16, 2014
This is version 112 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 7

Human chromosome 7: entries, gene names and cross-references to MIM