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Q9H792

- PEAK1_HUMAN

UniProt

Q9H792 - PEAK1_HUMAN

Protein

Pseudopodium-enriched atypical kinase 1

Gene

PEAK1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 109 (01 Oct 2014)
      Sequence version 4 (10 Feb 2009)
      Previous versions | rss
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    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 PublicationPROSITE-ProRule annotation

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei1359 – 13591ATPPROSITE-ProRule annotation
    Active sitei1516 – 15161Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi1319 – 13279ATPPROSITE-ProRule annotation

    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

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

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Cell junction, Cytoplasm, Cytoskeleton

    PTM / Processingi

    Molecule processing

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

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei281 – 2811Phosphoserine2 Publications
    Modified residuei540 – 5401Phosphoserine2 Publications
    Modified residuei587 – 5871Phosphoserine2 Publications
    Modified residuei635 – 6351Phosphotyrosine2 Publications
    Modified residuei641 – 6411PhosphotyrosineBy 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.3 Publications

    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.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1313 – 1675363Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Compositional bias

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

    Sequence similaritiesi

    Belongs to the protein kinase superfamily.Curated
    Contains 1 protein kinase domain.PROSITE-ProRule annotation

    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.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti779 – 7791S → F in BAC87076. (PubMed:14702039)Curated
    Sequence conflicti1046 – 10494SHMT → RYVK in AK091802. (PubMed:14702039)Curated
    Sequence conflicti1112 – 11209QSRAAMIPP → KCKCPISSI in BAB84983. 1 PublicationCurated
    Sequence conflicti1375 – 13784LAVR → SQEF in BAC87076. (PubMed:14702039)Curated

    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 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

    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: October 1, 2014
    This is version 109 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3