Q9H792 (PEAK1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Pseudopodium-enriched atypical kinase 1
EC=2.7.10.2

Alternative name(s):
Sugen kinase 269
Tyrosine-protein kinase SgK269

Gene names

Name:	PEAK1
Synonyms:	KIAA2002

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	1746 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Tyrosine kinase that may play a role in cell spreading and migration on fibronectin. May directly or indirectly affect phosphorylation levels of cytoskeleton-associated proteins MAPK1/ERK and PXN. Ref.6
Catalytic activity	ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate. Ref.6
Subunit structure	Interacts with BCAR1 and CRK. Ref.6
Subcellular location	Cytoplasm › cytoskeleton. Cell junction › focal adhesion. Note: Colocalizes with F-actin in serum-rich medium. Actin colocalization is reduced during serum starvation. Ref.6
Post-translational modification	Phosphorylated on tyrosine in a CSK-dependent manner in response to adhesion to fibronectin and to EGF stimulation. Autophosphorylated in vitro. Ref.6
Sequence similarities	Belongs to the protein kinase superfamily. Contains 1 protein kinase domain.
Sequence caution	The sequence BAB15006.1 differs from that shown. Reason: Erroneous initiation. The sequence BAC87076.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Cellular component	Cell junction Cytoplasm Cytoskeleton
Coding sequence diversity	Polymorphism
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Transferase Tyrosine-protein kinase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cell migration Inferred from direct assay Ref.6. Source: UniProtKB protein autophosphorylation Inferred from direct assay Ref.6. Source: UniProtKB substrate adhesion-dependent cell spreading Inferred from direct assay Ref.6. Source: UniProtKB
Cellular_component	actin cytoskeleton Inferred from direct assay Ref.6. Source: UniProtKB cytoplasm Inferred from electronic annotation. Source: UniProtKB-KW focal adhesion Inferred from direct assay Ref.6. Source: UniProtKB
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW non-membrane spanning protein tyrosine kinase activity Inferred from direct assay Ref.6. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1746	1746	Pseudopodium-enriched atypical kinase 1		PRO_0000250589
Regions
	Domain	1313 – 1675	363	Protein kinase
	Nucleotide binding	1319 – 1327	9	ATP By similarity
	Compositional bias	117 – 120	4	Poly-Asn
	Compositional bias	324 – 406	83	Ser-rich
	Compositional bias	500 – 503	4	Poly-Ser
	Compositional bias	776 – 873	98	Pro-rich
	Compositional bias	964 – 967	4	Poly-Pro
Sites
	Active site	1516	1	Proton acceptor By similarity
	Binding site	1359	1	ATP By similarity
Amino acid modifications
	Modified residue	281	1	Phosphoserine By similarity
	Modified residue	635	1	Phosphotyrosine By similarity
Natural variations
	Natural variant	213	1	G → R. Ref.8 Corresponds to variant rs35459975 [ dbSNP | Ensembl ].		VAR_041817
	Natural variant	240	1	V → I. Ref.8 Corresponds to variant rs56129428 [ dbSNP | Ensembl ].		VAR_041818
	Natural variant	440	1	S → P. Ref.8 Corresponds to variant rs35335169 [ dbSNP | Ensembl ].		VAR_041819
	Natural variant	611	1	H → Q in a bladder carcinoma NOS sample; somatic mutation. Ref.8		VAR_041820
	Natural variant	792	1	S → I. Ref.8 Corresponds to variant rs34885462 [ dbSNP | Ensembl ].		VAR_041821
	Natural variant	836	1	D → E. Ref.8 Corresponds to variant rs56388121 [ dbSNP | Ensembl ].		VAR_041822
	Natural variant	1035	1	S → F in a metastatic melanoma sample; somatic mutation. Ref.8		VAR_041823
	Natural variant	1071	1	R → K. Ref.8 Corresponds to variant rs12909704 [ dbSNP | Ensembl ].		VAR_041824
	Natural variant	1077	1	T → P. Ref.8 Corresponds to variant rs56133554 [ dbSNP | Ensembl ].		VAR_041825
	Natural variant	1145	1	P → L in a metastatic melanoma sample; somatic mutation. Ref.8		VAR_041826
	Natural variant	1408	1	P → Q. Ref.8 Corresponds to variant rs56079860 [ dbSNP | Ensembl ].		VAR_041827
	Natural variant	1542	1	S → T. Ref.8 Corresponds to variant rs1867780 [ dbSNP | Ensembl ].		VAR_041828
	Natural variant	1699	1	R → G. Ref.8 Corresponds to variant rs34004337 [ dbSNP | Ensembl ].		VAR_041829
Experimental info
	Sequence conflict	779	1	S → F in BAC87076. Ref.2
	Sequence conflict	1046 – 1049	4	SHMT → RYVK in AK091802. Ref.2
	Sequence conflict	1112 – 1120	9	QSRAAMIPP → KCKCPISSI in BAB84983. Ref.3
	Sequence conflict	1375 – 1378	4	LAVR → SQEF in BAC87076. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Q9H792 [UniParc]. Last modified February 10, 2009. Version 4. Checksum: 7C9A9F60BBCF6C61	FASTA	1,746	193,106
	10 20 30 40 50 60 MSACNTFTEH VWKPGECKNC FKPKSLHQLP PDPEKAPITH GNVKTNANHS NNHRIRNTGN 70 80 90 100 110 120 FRPPVAKKPT IAVKPTMIVA DGQSICGELS IQEHCENKPV IIGWNRNRAA LSQKPLNNNN 130 140 150 160 170 180 EDDEGISHVP KPYGNNDSAK KMSDNNNGLT EVLKEIAGLD TAPQIRGNET NSRETFLGRI 190 200 210 220 230 240 NDCYKRSLER KLPPSCMIGG IKETQGKHVI LSGSTEVISN EGGRFCYPEF SSGEESEEDV 250 260 270 280 290 300 LFSNMEEEHE SWDESDEELL AMEIRMRGQP RFANFRANTL SPVRFFVDKK WNTIPLRNKS 310 320 330 340 350 360 LQRICAVDYD DSYDEILNGY EENSVVSYGQ GSIQSMVSSD STSPDSSLTE ESRSETASSL 370 380 390 400 410 420 SQKICNGGLS PGNPGDSKDM KEIEPNYESP SSNNQDKDSS QASKSSIKVP ETHKAVLALR 430 440 450 460 470 480 LEEKDGKIAV QTEKEESKAS TDVAGQAVTI NLVPTEEQAK PYRVVNLEQP LCKPYTVVDV 490 500 510 520 530 540 SAAMASEHLE GPVNSPKTKS SSSTPNSPVT SSSLTPGQIS AHFQKSSAIR YQEVWTSSTS 550 560 570 580 590 600 PRQKIPKVEL ITSGTGPNVP PRKNCHKSAP TSPTATNISS KTIPVKSPNL SEIKFNSYNN 610 620 630 640 650 660 AGMPPFPIII HDEPTYARSS KNAIKVPIVI NPNAYDNLAI YKSFLGTSGE LSVKEKTTSV 670 680 690 700 710 720 ISHTYEEIET ESKVPDNTTS KTTDCLQTKG FSNSTEHKRG SVAQKVQEFN NCLNRGQSSP 730 740 750 760 770 780 QRSYSSSHSS PAKIQRATQE PVAKIEGTQE SQMVGSSSTR EKASTVLSQI VASIQPPQSP 790 800 810 820 830 840 PETPQSGPKA CSVEELYAIP PDADVAKSTP KSTPVRPKSL FTSQPSGEAE APQTTDSPTT 850 860 870 880 890 900 KVQKDPSIKP VTPSPSKLVT SPQSEPPAPF PPPRSTSSPY HAGNLLQRHF TNWTKPTSPT 910 920 930 940 950 960 RSTEAESVLH SEGSRRAADA KPKRWISFKS FFRRRKTDEE DDKEKEREKG KLVGLDGTVI 970 980 990 1000 1010 1020 HMLPPPPVQR HHWFTEAKGE SSEKPAIVFM YRCDPAQGQL SVDQSKARTD QAAVMEKGRA 1030 1040 1050 1060 1070 1080 ENALLQDSEK KRSHSSPSQI PKKILSHMTH EVTEDFSPRD PRTVVGKQDG RGCTSVTTAL 1090 1100 1110 1120 1130 1140 SLPELEREDG KEDISDPMDP NPCSATYSNL GQSRAAMIPP KQPRQPKGAV DDAIAFGGKT 1150 1160 1170 1180 1190 1200 DQEAPNASQP TPPPLPKKMI IRANTEPISK DLQKSMESSL CVMANPTYDI DPNWDASSAG 1210 1220 1230 1240 1250 1260 SSISYELKGL DIESYDSLER PLRKERPVPS AANSISSLTT LSIKDRFSNS MESLSSRRGP 1270 1280 1290 1300 1310 1320 SCRQGRGIQK PQRQALYRGL ENREEVVGKI RSLHTDALKK LAVKCEDLFM AGQKDQLRFG 1330 1340 1350 1360 1370 1380 VDSWSDFRLT SDKPCCEAGD AVYYTASYAK DPLNNYAVKI CKSKAKESQQ YYHSLAVRQS 1390 1400 1410 1420 1430 1440 LAVHFNIQQD CGHFLAEVPN RLLPWEDPDD PEKDEDDMEE TEEDAKGETD GKNPKPCSEA 1450 1460 1470 1480 1490 1500 ASSQKENQGV MSKKQRSHVV VITREVPCLT VADFVRDSLA QHGKSPDLYE RQVCLLLLQL 1510 1520 1530 1540 1550 1560 CSGLEHLKPY HVTHCDLRLE NLLLVHYQPG GTAQGFGPAE PSPTSSYPTR LIVSNFSQAK 1570 1580 1590 1600 1610 1620 QKSHLVDPEI LRDQSRLAPE IITATQYKKC DEFQTGILIY EMLHLPNPFD ENPELKEREY 1630 1640 1650 1660 1670 1680 TRADLPRIPF RSPYSRGLQQ LASCLLNPNP SERILISDAK GILQCLLWGP REDLFQTFTA 1690 1700 1710 1720 1730 1740 CPSLVQRNTL LQNWLDIKRT LLMIKFAEKS LDREGGISLE DWLCAQYLAF ATTDSLSCIV KILQHR

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Analysis of the DNA sequence and duplication history of human chromosome 15." Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K., Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N., Abouelleil A. , Arachchi H.M., Baradarani L., Birditt B., Bloom S., Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K., DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B., Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C. Nature 440:671-675(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[2]	"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] OF 537-1746. Tissue: Lung, Mesangial cell and Smooth muscle.
[3]	"The nucleotide sequence of a long cDNA clone isolated from human spleen." Jikuya H., Takano J., Nomura N., Kikuno R., Nagase T., Ohara O. Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 707-1120. Tissue: Spleen.
[4]	"Characterization of size-fractionated cDNA libraries generated by the in vitro recombination-assisted method." Ohara O., Nagase T., Mitsui G., Kohga H., Kikuno R., Hiraoka S., Takahashi Y., Kitajima S., Saga Y., Koseki H. DNA Res. 9:47-57(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 983-1746. Tissue: Brain.
[5]	"The protein kinase complement of the human genome." Manning G., Whyte D.B., Martinez R., Hunter T., Sudarsanam S. Science 298:1912-1934(2002) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION.
[6]	"Pseudopodium-enriched atypical kinase 1 regulates the cytoskeleton and cancer progression." Wang Y., Kelber J.A., Tran Cao H.S., Cantin G.T., Lin R., Wang W., Kaushal S., Bristow J.M., Edgington T.S., Hoffman R.M., Bouvet M., Yates J.R. III, Klemke R.L. Proc. Natl. Acad. Sci. U.S.A. 107:10920-10925(2010) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH BCAR1 AND CRK, SUBCELLULAR LOCATION, AUTOPHOSPHORYLATION, PHOSPHORYLATION BY CSK.
[7]	Erratum Wang Y., Kelber J.A., Tran Cao H.S., Cantin G.T., Lin R., Wang W., Kaushal S., Bristow J.M., Edgington T.S., Hoffman R.M., Bouvet M., Yates J.R. III, Klemke R.L. Proc. Natl. Acad. Sci. U.S.A. 107:13556-13556(2010)
[8]	"Patterns of somatic mutation in human cancer genomes." Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G. , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R. Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS [LARGE SCALE ANALYSIS] ARG-213; ILE-240; PRO-440; GLN-611; ILE-792; GLU-836; PHE-1035; LYS-1071; PRO-1077; LEU-1145; GLN-1408; THR-1542 AND GLY-1699.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AC087465 Genomic DNA. No translation available. AC107883 Genomic DNA. No translation available. AK024793 mRNA. Translation: BAB15006.1. Different initiation. AK091802 mRNA. No translation available. AK127658 mRNA. Translation: BAC87076.1. Different initiation. AK074157 mRNA. Translation: BAB84983.1. AB082533 mRNA. Translation: BAC02711.1.
IPI	IPI00737545.
RefSeq	NP_079052.2. NM_024776.3.
UniGene	Hs.731402. Hs.9587.
3D structure databases
ProteinModelPortal	Q9H792.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-56276N.
IntAct	Q9H792. 4 interactions.
STRING	9606.ENSP00000309230.
PTM databases
PhosphoSite	Q9H792.
Polymorphism databases
DMDM	223634730.
Proteomic databases
PaxDb	Q9H792.
PRIDE	Q9H792.
Protocols and materials databases
DNASU	79834.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	79834.
KEGG	hsa:79834.
UCSC	uc002bcn.2. human.
Organism-specific databases
CTD	79834.
GeneCards	GC15M077401.
H-InvDB	HIX0012463.
HPA	HPA026313. HPA026517.
MIM	614248. gene.
neXtProt	NX_Q9H792.
HUGE	Search...
Phylogenomic databases
eggNOG	NOG115841.
HOVERGEN	HBG093946.
InParanoid	Q9H792.
OMA	GNNDSAK.
OrthoDB	EOG4PVNXS.
Gene expression databases
ArrayExpress	Q9H792.
Bgee	Q9H792.
Genevestigator	Q9H792.
Family and domain databases
InterPro	IPR011009. Kinase-like_dom. IPR000719. Prot_kinase_cat_dom. IPR008266. Tyr_kinase_AS. [Graphical view]
Pfam	PF00069. Pkinase. 1 hit. [Graphical view]
SUPFAM	SSF56112. Kinase_like. 1 hit.
PROSITE	PS00107. PROTEIN_KINASE_ATP. False negative. PS50011. PROTEIN_KINASE_DOM. 1 hit. PS00109. PROTEIN_KINASE_TYR. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	PEAK1. human.
GenomeRNAi	79834.
NextBio	69485.
SOURCE	Search...

Entry information

Entry name

PEAK1_HUMAN

Accession

Primary (citable) accession number: Q9H792
Secondary accession number(s): Q6ZS78 , Q8NAZ4, Q8NCM3, Q8TEG7

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 3, 2006
Last sequence update:	February 10, 2009
Last modified:	April 3, 2013
This is version 95 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.