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Reviewed, UniProtKB/Swiss-Prot O75563 (SKAP2_HUMAN)

Last modified June 16, 2009. Version 65. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Src kinase-associated phosphoprotein 2
Alternative name(s):
    Src family-associated phosphoprotein 2
    Src kinase-associated phosphoprotein 55-related protein
    SKAP55 homolog
      Short name=SKAP-55HOM
      Short name=SKAP-HOM
    Src-associated adapter protein with PH and SH3 domains
    Pyk2/RAFTK-associated protein
    Retinoic acid-induced protein 70
Gene names
Name: SKAP2
Synonyms: PRAP, RA70, SAPS, SCAP2, SKAP55R
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length359 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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

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.

Subcellular location

Cytoplasm. Ref.4

Tissue specificity

Ubiquitously expressed. Present in platelets (at protein level). Ref.1 Ref.2 Ref.9

Induction

By retinoic acid. Ref.1 Ref.10

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.

Sequence similarities

Belongs to the SKAP family.

Contains 1 PH domain.

Contains 1 SH3 domain.

Ontologies

Keywords
   Biological processB-cell activation
   Cellular componentCytoplasm
   Coding sequence diversityPolymorphism
   DomainSH3 domain
   PTMPhosphoprotein
Gene Ontology (GO)
   Biological processB cell activation

Inferred from electronic annotation. Source: UniProtKB-KW

protein complex assembly Ref.3

Traceable author statement. Source: ProtInc

signal transduction Ref.1

Traceable author statement. Source: ProtInc

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

plasma membrane

Inferred from direct assay. Source: MGI

   Molecular functionSH3/SH2 adaptor activity Ref.3

Traceable author statement. Source: ProtInc

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 359359Src kinase-associated phosphoprotein 2
PRO_0000270179

Regions

Domain116 – 219104PH
Domain297 – 35862SH3

Amino acid modifications

Modified residue751Phosphotyrosine By similarity
Modified residue1511Phosphotyrosine Ref.12
Modified residue1971Phosphotyrosine Ref.12
Modified residue2611Phosphotyrosine By similarity
Modified residue3251Phosphotyrosine Ref.11

Natural variations

Natural variant2021A → S: dbSNP rs1129771. Ref.1 Ref.2 Ref.5
VAR_029812
Natural variant2531S → T: dbSNP rs17154402.
VAR_029813

Experimental info

Sequence conflict61S → C in BAA36194. Ref.1
Sequence conflict3521Y → H in BAD96605. Ref.6

Sequences

Sequence LengthMass (Da)Tools
O75563-1 [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: 9837776] [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: 9755858] [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: 9671755] [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: 12893833] [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]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.
[7]"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: 12853948] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]"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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Lung and Testis.
[9]"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: 10942756] [Abstract]
Cited for: PHOSPHORYLATION, INTERACTION WITH FYB; LAT AND GRB2, TISSUE SPECIFICITY.
[10]"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: 11301322] [Abstract]
Cited for: INDUCTION, INTERACTION WITH PRAM1.
[11]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed: 17081983] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-325, MASS SPECTROMETRY.
Tissue: Epithelium.
[12]"Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer."
Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J., Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L., Mitchell J., Wetzel R., Macneill J., Ren J.M. expand/collapse author list , Yuan J., Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X., Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.
Cell 131:1190-1203(2007) [PubMed: 18083107] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-151 AND TYR-197, MASS SPECTROMETRY.
+Additional computationally mapped references.

Cross-references

Sequence databases

AB014486 mRNA. Translation: BAA36194.1.
AJ004886 mRNA. Translation: CAA06193.1.
AF072166 mRNA. Translation: AAC39924.1.
AF051323 mRNA. Translation: AAC99296.1.
AK222885 mRNA. Translation: BAD96605.1.
AC003999 Genomic DNA. Translation: AAS02033.1.
AC011299 Genomic DNA. Translation: AAS07536.1.
BC002893 mRNA. Translation: AAH02893.1.
BC036044 mRNA. Translation: AAH36044.1.
IPIIPI00022508.
RefSeqNP_003921.2.
UniGeneHs.200770
Hs.510635

3D structure databases

HSSPHSSP built from PDB template 1K76 based on UniProtKB P29355.
SMRO75563. Positions 14-221.
ModBaseSearch...

PTM databases

PhosphoSiteO75563.

2-D gel databases

OGPO75563.

Proteomic databases

PRIDEO75563.

Genome annotation databases

EnsemblENSG00000005020. Homo sapiens. [Contig view]
GeneID8935.
KEGGhsa:8935.

Organism-specific databases

GeneCardsGC07M026674.
HGNCHGNC:15687. SKAP2.
MIM605215. gene.
GenAtlasSearch...

Phylogenomic databases

HOVERGENO75563.
OMAO75563. DGKKDCC.

Gene expression databases

ArrayExpressO75563.
BgeeO75563.
CleanExHS_SKAP2.

Family and domain databases

InterProIPR011993. PH_type.
IPR001849. Pleckstrin_homology.
IPR001452. SH3_domain.
[Graphical view]
Gene3DG3DSA:2.30.29.30. PH_type. 1 hit.
PfamPF00169. PH. 1 hit.
PF00018. SH3_1. 1 hit.
[Graphical view]
ProDomPD000066. SH3. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTSM00233. PH. 1 hit.
SM00326. SH3. 1 hit.
[Graphical view]
PROSITEPS50003. PH_DOMAIN. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio33596.
SOURCESearch...

Entry information

Entry nameSKAP2_HUMAN
AccessionPrimary (citable) accession number: O75563
Secondary accession number(s): Q53GP6 expand/collapse secondary AC list , Q75MK6, Q75MZ4, Q9UBZ3, Q9UED8
Entry history
Integrated into UniProtKB/Swiss-Prot: January 9, 2007
Last sequence update: November 1, 1998
Last modified: June 16, 2009
This is version 65 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

Human chromosome 7

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

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

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

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents