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Q9H792

- PEAK1_HUMAN

UniProt

Q9H792 - PEAK1_HUMAN

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Protein
Pseudopodium-enriched atypical kinase 1
Gene
PEAK1, KIAA2002
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.1 Publication

Catalytic activityi

ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei1359 – 13591ATP By similarity
Active sitei1516 – 15161Proton acceptor By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi1319 – 13279ATP By similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. non-membrane spanning protein tyrosine kinase activity Source: UniProtKB
  3. protein binding Source: UniProtKB

GO - Biological processi

  1. cell migration Source: UniProtKB
  2. peptidyl-tyrosine phosphorylation Source: GOC
  3. protein autophosphorylation Source: UniProtKB
  4. substrate adhesion-dependent cell spreading Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase, Tyrosine-protein kinase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

SignaLinkiQ9H792.

Names & Taxonomyi

Protein namesi
Recommended name:
Pseudopodium-enriched atypical kinase 1 (EC:2.7.10.2)
Alternative name(s):
Sugen kinase 269
Tyrosine-protein kinase SgK269
Gene namesi
Name:PEAK1
Synonyms:KIAA2002
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Unplaced

Organism-specific databases

HGNCiHGNC:29431. PEAK1.

Subcellular locationi

Cytoplasmcytoskeleton. Cell junctionfocal adhesion
Note: Colocalizes with F-actin in serum-rich medium. Actin colocalization is reduced during serum starvation.1 Publication

GO - Cellular componenti

  1. actin cytoskeleton Source: UniProtKB
  2. cytoplasm Source: UniProtKB-KW
  3. focal adhesion Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cytoplasm, Cytoskeleton

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 17461746Pseudopodium-enriched atypical kinase 1
PRO_0000250589Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei281 – 2811Phosphoserine1 Publication
Modified residuei540 – 5401Phosphoserine1 Publication
Modified residuei587 – 5871Phosphoserine1 Publication
Modified residuei635 – 6351Phosphotyrosine1 Publication
Modified residuei641 – 6411Phosphotyrosine By similarity

Post-translational modificationi

Phosphorylated on tyrosine in a CSK-dependent manner in response to adhesion to fibronectin and to EGF stimulation. Autophosphorylated in vitro.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9H792.
PaxDbiQ9H792.
PRIDEiQ9H792.

PTM databases

PhosphoSiteiQ9H792.

Expressioni

Gene expression databases

ArrayExpressiQ9H792.
BgeeiQ9H792.
GenevestigatoriQ9H792.

Organism-specific databases

HPAiHPA026313.
HPA026517.

Interactioni

Subunit structurei

Interacts with BCAR1 and CRK.1 Publication

Protein-protein interaction databases

BioGridi122926. 3 interactions.
DIPiDIP-56276N.
IntActiQ9H792. 5 interactions.
STRINGi9606.ENSP00000309230.

Structurei

3D structure databases

ProteinModelPortaliQ9H792.
SMRiQ9H792. Positions 1490-1658.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1313 – 1675363Protein kinase
Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi117 – 1204Poly-Asn
Compositional biasi324 – 40683Ser-rich
Add
BLAST
Compositional biasi500 – 5034Poly-Ser
Compositional biasi776 – 87398Pro-rich
Add
BLAST
Compositional biasi964 – 9674Poly-Pro

Sequence similaritiesi

Phylogenomic databases

eggNOGiNOG115841.
HOVERGENiHBG093946.
InParanoidiQ9H792.
KOiK17538.
OMAiGRFCYPE.
PhylomeDBiQ9H792.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR008266. Tyr_kinase_AS.
[Graphical view]
PfamiPF00069. Pkinase. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 2 hits.
PROSITEiPS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00109. PROTEIN_KINASE_TYR. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9H792-1 [UniParc]FASTAAdd to Basket

« Hide

MSACNTFTEH VWKPGECKNC FKPKSLHQLP PDPEKAPITH GNVKTNANHS     50
NNHRIRNTGN FRPPVAKKPT IAVKPTMIVA DGQSICGELS IQEHCENKPV 100
IIGWNRNRAA LSQKPLNNNN EDDEGISHVP KPYGNNDSAK KMSDNNNGLT 150
EVLKEIAGLD TAPQIRGNET NSRETFLGRI NDCYKRSLER KLPPSCMIGG 200
IKETQGKHVI LSGSTEVISN EGGRFCYPEF SSGEESEEDV LFSNMEEEHE 250
SWDESDEELL AMEIRMRGQP RFANFRANTL SPVRFFVDKK WNTIPLRNKS 300
LQRICAVDYD DSYDEILNGY EENSVVSYGQ GSIQSMVSSD STSPDSSLTE 350
ESRSETASSL SQKICNGGLS PGNPGDSKDM KEIEPNYESP SSNNQDKDSS 400
QASKSSIKVP ETHKAVLALR LEEKDGKIAV QTEKEESKAS TDVAGQAVTI 450
NLVPTEEQAK PYRVVNLEQP LCKPYTVVDV SAAMASEHLE GPVNSPKTKS 500
SSSTPNSPVT SSSLTPGQIS AHFQKSSAIR YQEVWTSSTS PRQKIPKVEL 550
ITSGTGPNVP PRKNCHKSAP TSPTATNISS KTIPVKSPNL SEIKFNSYNN 600
AGMPPFPIII HDEPTYARSS KNAIKVPIVI NPNAYDNLAI YKSFLGTSGE 650
LSVKEKTTSV ISHTYEEIET ESKVPDNTTS KTTDCLQTKG FSNSTEHKRG 700
SVAQKVQEFN NCLNRGQSSP QRSYSSSHSS PAKIQRATQE PVAKIEGTQE 750
SQMVGSSSTR EKASTVLSQI VASIQPPQSP PETPQSGPKA CSVEELYAIP 800
PDADVAKSTP KSTPVRPKSL FTSQPSGEAE APQTTDSPTT KVQKDPSIKP 850
VTPSPSKLVT SPQSEPPAPF PPPRSTSSPY HAGNLLQRHF TNWTKPTSPT 900
RSTEAESVLH SEGSRRAADA KPKRWISFKS FFRRRKTDEE DDKEKEREKG 950
KLVGLDGTVI HMLPPPPVQR HHWFTEAKGE SSEKPAIVFM YRCDPAQGQL 1000
SVDQSKARTD QAAVMEKGRA ENALLQDSEK KRSHSSPSQI PKKILSHMTH 1050
EVTEDFSPRD PRTVVGKQDG RGCTSVTTAL SLPELEREDG KEDISDPMDP 1100
NPCSATYSNL GQSRAAMIPP KQPRQPKGAV DDAIAFGGKT DQEAPNASQP 1150
TPPPLPKKMI IRANTEPISK DLQKSMESSL CVMANPTYDI DPNWDASSAG 1200
SSISYELKGL DIESYDSLER PLRKERPVPS AANSISSLTT LSIKDRFSNS 1250
MESLSSRRGP SCRQGRGIQK PQRQALYRGL ENREEVVGKI RSLHTDALKK 1300
LAVKCEDLFM AGQKDQLRFG VDSWSDFRLT SDKPCCEAGD AVYYTASYAK 1350
DPLNNYAVKI CKSKAKESQQ YYHSLAVRQS LAVHFNIQQD CGHFLAEVPN 1400
RLLPWEDPDD PEKDEDDMEE TEEDAKGETD GKNPKPCSEA ASSQKENQGV 1450
MSKKQRSHVV VITREVPCLT VADFVRDSLA QHGKSPDLYE RQVCLLLLQL 1500
CSGLEHLKPY HVTHCDLRLE NLLLVHYQPG GTAQGFGPAE PSPTSSYPTR 1550
LIVSNFSQAK QKSHLVDPEI LRDQSRLAPE IITATQYKKC DEFQTGILIY 1600
EMLHLPNPFD ENPELKEREY TRADLPRIPF RSPYSRGLQQ LASCLLNPNP 1650
SERILISDAK GILQCLLWGP REDLFQTFTA CPSLVQRNTL LQNWLDIKRT 1700
LLMIKFAEKS LDREGGISLE DWLCAQYLAF ATTDSLSCIV KILQHR 1746
Length:1,746
Mass (Da):193,106
Last modified:February 10, 2009 - v4
Checksum:i7C9A9F60BBCF6C61
GO

Sequence cautioni

The sequence BAB15006.1 differs from that shown. Reason: Erroneous initiation.
The sequence BAC87076.1 differs from that shown. Reason: Erroneous initiation.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti213 – 2131G → R.1 Publication
Corresponds to variant rs35459975 [ dbSNP | Ensembl ].
VAR_041817
Natural varianti240 – 2401V → I.1 Publication
Corresponds to variant rs56129428 [ dbSNP | Ensembl ].
VAR_041818
Natural varianti440 – 4401S → P.1 Publication
Corresponds to variant rs35335169 [ dbSNP | Ensembl ].
VAR_041819
Natural varianti611 – 6111H → Q in a bladder carcinoma NOS sample; somatic mutation. 1 Publication
VAR_041820
Natural varianti792 – 7921S → I.1 Publication
Corresponds to variant rs34885462 [ dbSNP | Ensembl ].
VAR_041821
Natural varianti836 – 8361D → E.1 Publication
Corresponds to variant rs56388121 [ dbSNP | Ensembl ].
VAR_041822
Natural varianti1035 – 10351S → F in a metastatic melanoma sample; somatic mutation. 1 Publication
VAR_041823
Natural varianti1071 – 10711R → K.1 Publication
Corresponds to variant rs12909704 [ dbSNP | Ensembl ].
VAR_041824
Natural varianti1077 – 10771T → P.1 Publication
Corresponds to variant rs56133554 [ dbSNP | Ensembl ].
VAR_041825
Natural varianti1145 – 11451P → L in a metastatic melanoma sample; somatic mutation. 1 Publication
VAR_041826
Natural varianti1408 – 14081P → Q.1 Publication
Corresponds to variant rs56079860 [ dbSNP | Ensembl ].
VAR_041827
Natural varianti1542 – 15421S → T.1 Publication
Corresponds to variant rs1867780 [ dbSNP | Ensembl ].
VAR_041828
Natural varianti1699 – 16991R → G.1 Publication
Corresponds to variant rs34004337 [ dbSNP | Ensembl ].
VAR_041829

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti779 – 7791S → F in BAC87076. 1 Publication
Sequence conflicti1046 – 10494SHMT → RYVK in AK091802. 1 Publication
Sequence conflicti1112 – 11209QSRAAMIPP → KCKCPISSI in BAB84983. 1 Publication
Sequence conflicti1375 – 13784LAVR → SQEF in BAC87076. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS42062.1.
RefSeqiNP_079052.2. NM_024776.3.
XP_005254727.1. XM_005254670.1.
XP_005254728.1. XM_005254671.1.
XP_005254729.1. XM_005254672.1.
XP_005254730.1. XM_005254673.1.
XP_005254731.1. XM_005254674.1.
XP_005254732.1. XM_005254675.2.
XP_006720754.1. XM_006720691.1.
UniGeneiHs.731402.
Hs.9587.

Genome annotation databases

EnsembliENST00000312493; ENSP00000309230; ENSG00000173517.
ENST00000560626; ENSP00000452796; ENSG00000173517.
GeneIDi79834.
KEGGihsa:79834.
UCSCiuc002bcn.2. human.

Polymorphism databases

DMDMi223634730.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS42062.1.
RefSeqi NP_079052.2. NM_024776.3.
XP_005254727.1. XM_005254670.1.
XP_005254728.1. XM_005254671.1.
XP_005254729.1. XM_005254672.1.
XP_005254730.1. XM_005254673.1.
XP_005254731.1. XM_005254674.1.
XP_005254732.1. XM_005254675.2.
XP_006720754.1. XM_006720691.1.
UniGenei Hs.731402.
Hs.9587.

3D structure databases

ProteinModelPortali Q9H792.
SMRi Q9H792. Positions 1490-1658.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 122926. 3 interactions.
DIPi DIP-56276N.
IntActi Q9H792. 5 interactions.
STRINGi 9606.ENSP00000309230.

PTM databases

PhosphoSitei Q9H792.

Polymorphism databases

DMDMi 223634730.

Proteomic databases

MaxQBi Q9H792.
PaxDbi Q9H792.
PRIDEi Q9H792.

Protocols and materials databases

DNASUi 79834.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000312493 ; ENSP00000309230 ; ENSG00000173517 .
ENST00000560626 ; ENSP00000452796 ; ENSG00000173517 .
GeneIDi 79834.
KEGGi hsa:79834.
UCSCi uc002bcn.2. human.

Organism-specific databases

CTDi 79834.
GeneCardsi GC15M077401.
H-InvDB HIX0012463.
HGNCi HGNC:29431. PEAK1.
HPAi HPA026313.
HPA026517.
MIMi 614248. gene.
neXtProti NX_Q9H792.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG115841.
HOVERGENi HBG093946.
InParanoidi Q9H792.
KOi K17538.
OMAi GRFCYPE.
PhylomeDBi Q9H792.

Enzyme and pathway databases

SignaLinki Q9H792.

Miscellaneous databases

ChiTaRSi PEAK1. human.
GenomeRNAii 79834.
NextBioi 69485.
PROi Q9H792.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q9H792.
Bgeei Q9H792.
Genevestigatori Q9H792.

Family and domain databases

InterProi IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR008266. Tyr_kinase_AS.
[Graphical view ]
Pfami PF00069. Pkinase. 1 hit.
[Graphical view ]
SUPFAMi SSF56112. SSF56112. 2 hits.
PROSITEi PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00109. PROTEIN_KINASE_TYR. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. Cited for: IDENTIFICATION.
  6. "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] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-540 AND SER-587, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. Cited for: FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH BCAR1 AND CRK, SUBCELLULAR LOCATION, AUTOPHOSPHORYLATION, PHOSPHORYLATION BY CSK.
  10. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-281 AND TYR-635, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. "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.

Entry informationi

Entry nameiPEAK1_HUMAN
AccessioniPrimary (citable) accession number: Q9H792
Secondary accession number(s): Q6ZS78
, Q8NAZ4, Q8NCM3, Q8TEG7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 3, 2006
Last sequence update: February 10, 2009
Last modified: July 9, 2014
This is version 108 of the entry and version 4 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 15
    Human chromosome 15: 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. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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