Reviewed, UniProtKB/Swiss-Prot O75563 (SKAP2_HUMAN)

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	359 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence 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 process	B-cell activation
Cellular component	Cytoplasm
Coding sequence diversity	Polymorphism
Domain	SH3 domain
PTM	Phosphoprotein
Gene Ontology (GO)
Biological process	B 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 component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell plasma membrane Inferred from direct assay. Source: MGI
Molecular function	SH3/SH2 adaptor activity Ref.3 Traceable author statement. Source: ProtInc
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 359	359	Src kinase-associated phosphoprotein 2		PRO_0000270179
Regions
	Domain	116 – 219	104	PH
	Domain	297 – 358	62	SH3
Amino acid modifications
	Modified residue	75	1	Phosphotyrosine By similarity
	Modified residue	151	1	Phosphotyrosine Ref.12
	Modified residue	197	1	Phosphotyrosine Ref.12
	Modified residue	261	1	Phosphotyrosine By similarity
	Modified residue	325	1	Phosphotyrosine Ref.11
Natural variations
	Natural variant	202	1	A → S: dbSNP rs1129771. Ref.1 Ref.2 Ref.5		VAR_029812
	Natural variant	253	1	S → T: dbSNP rs17154402.		VAR_029813
Experimental info
	Sequence conflict	6	1	S → C in BAA36194. Ref.1
	Sequence conflict	352	1	Y → H in BAD96605. Ref.6

Sequences

	Sequence		Length	Mass (Da)
	O75563-1 [UniParc]. Last modified November 1, 1998. Version 1. Checksum: 65F266535A89281E	FASTA	359	41,217
	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

References

	« Hide 'large scale' referencesShow '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. , 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. , 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
EMBLGenBankDDBJ	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.
IPI	IPI00022508.
RefSeq	NP_003921.2.
UniGene	Hs.200770 Hs.510635
3D structure databases
HSSP	HSSP built from PDB template 1K76 based on UniProtKB P29355.
SMR	O75563. Positions 14-221.
ModBase	Search...
PTM databases
PhosphoSite	O75563.
2-D gel databases
OGP	O75563.
Proteomic databases
PRIDE	O75563.
Genome annotation databases
Ensembl	ENSG00000005020. Homo sapiens. [Contig view]
GeneID	8935.
KEGG	hsa:8935.
Organism-specific databases
GeneCards	GC07M026674.
HGNC	HGNC:15687. SKAP2.
MIM	605215. gene.
GenAtlas	Search...
Phylogenomic databases
HOVERGEN	O75563.
OMA	O75563. DGKKDCC.
Gene expression databases
ArrayExpress	O75563.
Bgee	O75563.
CleanEx	HS_SKAP2.
Family and domain databases
InterPro	IPR011993. PH_type. IPR001849. Pleckstrin_homology. IPR001452. SH3_domain. [Graphical view]
Gene3D	G3DSA:2.30.29.30. PH_type. 1 hit.
Pfam	PF00169. PH. 1 hit. PF00018. SH3_1. 1 hit. [Graphical view]
ProDom	PD000066. SH3. 1 hit. [Graphical view] [Entries sharing at least one domain]
SMART	SM00233. PH. 1 hit. SM00326. SH3. 1 hit. [Graphical view]
PROSITE	PS50003. PH_DOMAIN. 1 hit. PS50002. SH3. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	33596.
SOURCE	Search...

Entry information

Entry name

SKAP2_HUMAN

Accession

Primary (citable) accession number: O75563
Secondary accession number(s): Q53GP6 , 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 status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)