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Protein

Pseudopodium-enriched atypical kinase 1

Gene

PEAK1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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 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

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: Chromosome 15

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: HPA
  3. focal adhesion Source: UniProtKB
  4. nucleoplasm Source: HPA
  5. plasma membrane Source: HPA
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 1PRO_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 – 6411PhosphotyrosineBy similarity
Modified residuei1151 – 11511Phosphothreonine1 Publication

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

BgeeiQ9H792.
ExpressionAtlasiQ9H792. baseline and differential.
GenevestigatoriQ9H792.

Organism-specific databases

HPAiHPA026313.
HPA026517.

Interactioni

Subunit structurei

Interacts with BCAR1 and CRK.1 Publication

Protein-protein interaction databases

BioGridi122926. 9 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.
GeneTreeiENSGT00460000041554.
HOVERGENiHBG093946.
InParanoidiQ9H792.
KOiK17538.
OMAiNNNGLTE.
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

        10         20         30         40         50
MSACNTFTEH VWKPGECKNC FKPKSLHQLP PDPEKAPITH GNVKTNANHS
60 70 80 90 100
NNHRIRNTGN FRPPVAKKPT IAVKPTMIVA DGQSICGELS IQEHCENKPV
110 120 130 140 150
IIGWNRNRAA LSQKPLNNNN EDDEGISHVP KPYGNNDSAK KMSDNNNGLT
160 170 180 190 200
EVLKEIAGLD TAPQIRGNET NSRETFLGRI NDCYKRSLER KLPPSCMIGG
210 220 230 240 250
IKETQGKHVI LSGSTEVISN EGGRFCYPEF SSGEESEEDV LFSNMEEEHE
260 270 280 290 300
SWDESDEELL AMEIRMRGQP RFANFRANTL SPVRFFVDKK WNTIPLRNKS
310 320 330 340 350
LQRICAVDYD DSYDEILNGY EENSVVSYGQ GSIQSMVSSD STSPDSSLTE
360 370 380 390 400
ESRSETASSL SQKICNGGLS PGNPGDSKDM KEIEPNYESP SSNNQDKDSS
410 420 430 440 450
QASKSSIKVP ETHKAVLALR LEEKDGKIAV QTEKEESKAS TDVAGQAVTI
460 470 480 490 500
NLVPTEEQAK PYRVVNLEQP LCKPYTVVDV SAAMASEHLE GPVNSPKTKS
510 520 530 540 550
SSSTPNSPVT SSSLTPGQIS AHFQKSSAIR YQEVWTSSTS PRQKIPKVEL
560 570 580 590 600
ITSGTGPNVP PRKNCHKSAP TSPTATNISS KTIPVKSPNL SEIKFNSYNN
610 620 630 640 650
AGMPPFPIII HDEPTYARSS KNAIKVPIVI NPNAYDNLAI YKSFLGTSGE
660 670 680 690 700
LSVKEKTTSV ISHTYEEIET ESKVPDNTTS KTTDCLQTKG FSNSTEHKRG
710 720 730 740 750
SVAQKVQEFN NCLNRGQSSP QRSYSSSHSS PAKIQRATQE PVAKIEGTQE
760 770 780 790 800
SQMVGSSSTR EKASTVLSQI VASIQPPQSP PETPQSGPKA CSVEELYAIP
810 820 830 840 850
PDADVAKSTP KSTPVRPKSL FTSQPSGEAE APQTTDSPTT KVQKDPSIKP
860 870 880 890 900
VTPSPSKLVT SPQSEPPAPF PPPRSTSSPY HAGNLLQRHF TNWTKPTSPT
910 920 930 940 950
RSTEAESVLH SEGSRRAADA KPKRWISFKS FFRRRKTDEE DDKEKEREKG
960 970 980 990 1000
KLVGLDGTVI HMLPPPPVQR HHWFTEAKGE SSEKPAIVFM YRCDPAQGQL
1010 1020 1030 1040 1050
SVDQSKARTD QAAVMEKGRA ENALLQDSEK KRSHSSPSQI PKKILSHMTH
1060 1070 1080 1090 1100
EVTEDFSPRD PRTVVGKQDG RGCTSVTTAL SLPELEREDG KEDISDPMDP
1110 1120 1130 1140 1150
NPCSATYSNL GQSRAAMIPP KQPRQPKGAV DDAIAFGGKT DQEAPNASQP
1160 1170 1180 1190 1200
TPPPLPKKMI IRANTEPISK DLQKSMESSL CVMANPTYDI DPNWDASSAG
1210 1220 1230 1240 1250
SSISYELKGL DIESYDSLER PLRKERPVPS AANSISSLTT LSIKDRFSNS
1260 1270 1280 1290 1300
MESLSSRRGP SCRQGRGIQK PQRQALYRGL ENREEVVGKI RSLHTDALKK
1310 1320 1330 1340 1350
LAVKCEDLFM AGQKDQLRFG VDSWSDFRLT SDKPCCEAGD AVYYTASYAK
1360 1370 1380 1390 1400
DPLNNYAVKI CKSKAKESQQ YYHSLAVRQS LAVHFNIQQD CGHFLAEVPN
1410 1420 1430 1440 1450
RLLPWEDPDD PEKDEDDMEE TEEDAKGETD GKNPKPCSEA ASSQKENQGV
1460 1470 1480 1490 1500
MSKKQRSHVV VITREVPCLT VADFVRDSLA QHGKSPDLYE RQVCLLLLQL
1510 1520 1530 1540 1550
CSGLEHLKPY HVTHCDLRLE NLLLVHYQPG GTAQGFGPAE PSPTSSYPTR
1560 1570 1580 1590 1600
LIVSNFSQAK QKSHLVDPEI LRDQSRLAPE IITATQYKKC DEFQTGILIY
1610 1620 1630 1640 1650
EMLHLPNPFD ENPELKEREY TRADLPRIPF RSPYSRGLQQ LASCLLNPNP
1660 1670 1680 1690 1700
SERILISDAK GILQCLLWGP REDLFQTFTA CPSLVQRNTL LQNWLDIKRT
1710 1720 1730 1740
LLMIKFAEKS LDREGGISLE DWLCAQYLAF ATTDSLSCIV KILQHR
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. Curated
The sequence BAC87076.1 differs from that shown. Reason: Erroneous initiation. Curated

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 (Ref. 3) Curated
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

ProteinModelPortaliQ9H792.
SMRiQ9H792. Positions 1490-1658.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi122926. 9 interactions.
DIPiDIP-56276N.
IntActiQ9H792. 5 interactions.
STRINGi9606.ENSP00000309230.

PTM databases

PhosphoSiteiQ9H792.

Polymorphism databases

DMDMi223634730.

Proteomic databases

MaxQBiQ9H792.
PaxDbiQ9H792.
PRIDEiQ9H792.

Protocols and materials databases

DNASUi79834.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi79834.
GeneCardsiGC15M077401.
H-InvDBHIX0012463.
HGNCiHGNC:29431. PEAK1.
HPAiHPA026313.
HPA026517.
MIMi614248. gene.
neXtProtiNX_Q9H792.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG115841.
GeneTreeiENSGT00460000041554.
HOVERGENiHBG093946.
InParanoidiQ9H792.
KOiK17538.
OMAiNNNGLTE.
PhylomeDBiQ9H792.

Enzyme and pathway databases

SignaLinkiQ9H792.

Miscellaneous databases

ChiTaRSiPEAK1. human.
GenomeRNAii79834.
NextBioi69485.
PROiQ9H792.
SOURCEiSearch...

Gene expression databases

BgeeiQ9H792.
ExpressionAtlasiQ9H792. baseline and differential.
GenevestigatoriQ9H792.

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]
ProtoNetiSearch...

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. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1151, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  12. "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: March 4, 2015
This is version 113 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.