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Protein

Inactive tyrosine-protein kinase PEAK1

Gene

PEAK1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Probable catalytically inactive kinase. Scaffolding protein that regulates the cytoskeleton to control cell spreading and migration by modulating focal adhesion dynamics (PubMed:23105102, PubMed:20534451). Acts as a scaffold for mediating EGFR signaling (PubMed:23846654).3 Publications

Caution

Has been the subject of controversy surrounding its catalytic capabilities. Early characterization of PEAK1 gave a weak in vitro tyrosine kinase activity (PubMed:20534451). The crystal structure indicates that the kinase-domain contains a closed nucleotide-binding cleft that in this conformation may deleteriously affect nucleotide binding (PubMed:29212708). Furthermore PEAK1 is devoid of nucleotide binding activity, as detected by a thermal-shift assay (PubMed:24107129). So it seems probable that PEAK1 is an inactive kinase.3 Publications

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • identical protein binding Source: UniProtKB
  • non-membrane spanning protein tyrosine kinase activity Source: UniProtKB

GO - Biological processi

  • cell migration Source: UniProtKB
  • focal adhesion assembly Source: UniProtKB
  • protein autophosphorylation Source: UniProtKB
  • regulation of focal adhesion assembly Source: UniProtKB
  • substrate adhesion-dependent cell spreading Source: UniProtKB

Enzyme and pathway databases

SignaLinkiQ9H792

Names & Taxonomyi

Protein namesi
Recommended name:
Inactive tyrosine-protein kinase PEAK1Curated
Alternative name(s):
Pseudopodium-enriched atypical kinase 11 Publication
Sugen kinase 2691 Publication
Tyrosine-protein kinase SgK269
Gene namesi
Name:PEAK1
Synonyms:KIAA2002
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 15

Organism-specific databases

EuPathDBiHostDB:ENSG00000173517.10
HGNCiHGNC:29431 PEAK1
MIMi614248 gene
neXtProtiNX_Q9H792

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cell junction, Cytoplasm, Cytoskeleton

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi665Y → E: No effect on localization with actin. Decreases localization in focal adhesion. Fails to regulate focal adhesion dynamics. Decreases cell migration. 1 Publication1
Mutagenesisi665Y → F: No effect on focal adhesion subcellular localization. Does not affect colocalization with F-actin. 1 Publication1
Mutagenesisi1188Y → F: Fails to bind SHC1. 1 Publication1
Mutagenesisi1609F → A: No effect on interaction with PRAG1. 1 Publication1
Mutagenesisi1707A → D: Disrupts homodimerization. 1 Publication1

Organism-specific databases

DisGeNETi79834
OpenTargetsiENSG00000173517

Chemistry databases

ChEMBLiCHEMBL3627585

Polymorphism and mutation databases

BioMutaiPEAK1
DMDMi223634730

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002505891 – 1746Inactive tyrosine-protein kinase PEAK1Add BLAST1746

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei281PhosphoserineCombined sources1
Modified residuei540PhosphoserineCombined sources1
Modified residuei572PhosphoserineCombined sources1
Modified residuei587PhosphoserineCombined sources1
Modified residuei635PhosphotyrosineCombined sources1
Modified residuei641PhosphotyrosineBy similarity1
Modified residuei648PhosphoserineCombined sources1
Modified residuei665Phosphotyrosine1 Publication1
Modified residuei826PhosphoserineBy similarity1
Modified residuei854PhosphoserineCombined sources1
Modified residuei898PhosphoserineCombined sources1
Modified residuei1151PhosphothreonineCombined sources1
Modified residuei1188Phosphotyrosine1 Publication1
Modified residuei1374PhosphoserineCombined sources1

Post-translational modificationi

Phosphorylated on tyrosine in a CSK-dependent manner in response to adhesion to fibronectin and to EGF stimulation (PubMed:20534451). Phosphorylation at Tyr-665 by a Src family kinase controls subcellular localization to focal adhesion and focal adhesion dynamics (PubMed:20534451). Phosphorylation at Tyr-1188 is essential for binding to SHC1 (PubMed:23846654).2 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ9H792
MaxQBiQ9H792
PaxDbiQ9H792
PeptideAtlasiQ9H792
PRIDEiQ9H792
ProteomicsDBi81090

PTM databases

iPTMnetiQ9H792
PhosphoSitePlusiQ9H792

Expressioni

Gene expression databases

BgeeiENSG00000173517
ExpressionAtlasiQ9H792 baseline and differential
GenevisibleiQ9H792 HS

Organism-specific databases

HPAiHPA026313
HPA026517

Interactioni

Subunit structurei

Homodimer (PubMed:29212708). Interacts with BCAR1 and CRK (PubMed:20534451). Interacts with PRAG1 (PubMed:29079850). Interacts (when phosphorylated at Tyr-1188) with SHC1 (via PID domain) (PubMed:23846654). Found in a complex with PPP1CA, PPP1CC, SHC1 and PEAK1.4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
BCAR1P569453EBI-2609701,EBI-702093

GO - Molecular functioni

  • identical protein binding Source: UniProtKB

Protein-protein interaction databases

BioGridi122926, 33 interactors
DIPiDIP-56276N
IntActiQ9H792, 17 interactors
STRINGi9606.ENSP00000309230

Structurei

Secondary structure

11746
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi1286 – 1309Combined sources24
Helixi1323 – 1326Combined sources4
Beta strandi1327 – 1330Combined sources4
Beta strandi1335 – 1337Combined sources3
Beta strandi1339 – 1348Combined sources10
Beta strandi1351 – 1361Combined sources11
Helixi1374 – 1379Combined sources6
Beta strandi1393 – 1398Combined sources6
Helixi1400 – 1402Combined sources3
Beta strandi1456 – 1465Combined sources10
Helixi1471 – 1476Combined sources6
Helixi1479 – 1484Combined sources6
Helixi1486 – 1507Combined sources22
Helixi1508 – 1510Combined sources3
Helixi1519 – 1521Combined sources3
Beta strandi1522 – 1525Combined sources4
Beta strandi1550 – 1553Combined sources4
Helixi1574 – 1576Combined sources3
Helixi1579 – 1583Combined sources5
Helixi1590 – 1602Combined sources13
Helixi1608 – 1611Combined sources4
Turni1616 – 1619Combined sources4
Turni1622 – 1624Combined sources3
Helixi1635 – 1645Combined sources11
Turni1650 – 1652Combined sources3
Helixi1656 – 1667Combined sources12
Helixi1672 – 1680Combined sources9
Helixi1684 – 1709Combined sources26
Helixi1719 – 1730Combined sources12
Helixi1733 – 1743Combined sources11

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
6BHCX-ray2.30A1272-1743[»]
ProteinModelPortaliQ9H792
SMRiQ9H792
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini1313 – 1675Protein kinasePROSITE-ProRule annotationAdd BLAST363

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1285 – 1311Required for homodimerization1 PublicationAdd BLAST27
Regioni1670 – 1743Required for homodimerization1 PublicationAdd BLAST74

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi117 – 120Poly-Asn4
Compositional biasi324 – 406Ser-richAdd BLAST83
Compositional biasi500 – 503Poly-Ser4
Compositional biasi776 – 873Pro-richAdd BLAST98
Compositional biasi964 – 967Poly-Pro4

Domaini

The dimerization region encompasses helices both from the N- and C-terminal of the protein kinase domain.1 Publication

Sequence similaritiesi

Belongs to the protein kinase superfamily.Curated

Phylogenomic databases

eggNOGiENOG410IJMD Eukaryota
ENOG4110SRP LUCA
GeneTreeiENSGT00460000041554
HOVERGENiHBG093946
InParanoidiQ9H792
KOiK17538
OMAiNDCYKRS
OrthoDBiEOG091G03K2
PhylomeDBiQ9H792

Family and domain databases

InterProiView protein in InterPro
IPR011009 Kinase-like_dom_sf
IPR000719 Prot_kinase_dom
IPR008266 Tyr_kinase_AS
PfamiView protein in Pfam
PF00069 Pkinase, 1 hit
SMARTiView protein in SMART
SM00220 S_TKc, 1 hit
SUPFAMiSSF56112 SSF56112, 2 hits
PROSITEiView protein in PROSITE
PS50011 PROTEIN_KINASE_DOM, 1 hit
PS00109 PROTEIN_KINASE_TYR, 1 hit

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

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti779S → F in BAC87076 (PubMed:14702039).Curated1
Sequence conflicti1046 – 1049SHMT → RYVK in AK091802 (PubMed:14702039).Curated4
Sequence conflicti1112 – 1120QSRAAMIPP → KCKCPISSI in BAB84983 (Ref. 3) Curated9
Sequence conflicti1375 – 1378LAVR → SQEF in BAC87076 (PubMed:14702039).Curated4

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_041817213G → R1 PublicationCorresponds to variant dbSNP:rs35459975Ensembl.1
Natural variantiVAR_041818240V → I1 PublicationCorresponds to variant dbSNP:rs56129428Ensembl.1
Natural variantiVAR_041819440S → P1 PublicationCorresponds to variant dbSNP:rs35335169Ensembl.1
Natural variantiVAR_041820611H → Q in a bladder carcinoma NOS sample; somatic mutation. 1 Publication1
Natural variantiVAR_041821792S → I1 PublicationCorresponds to variant dbSNP:rs34885462Ensembl.1
Natural variantiVAR_041822836D → E1 PublicationCorresponds to variant dbSNP:rs56388121Ensembl.1
Natural variantiVAR_0418231035S → F in a metastatic melanoma sample; somatic mutation. 1 Publication1
Natural variantiVAR_0418241071R → K1 PublicationCorresponds to variant dbSNP:rs12909704Ensembl.1
Natural variantiVAR_0418251077T → P1 PublicationCorresponds to variant dbSNP:rs56133554Ensembl.1
Natural variantiVAR_0418261145P → L in a metastatic melanoma sample; somatic mutation. 1 Publication1
Natural variantiVAR_0418271408P → Q1 PublicationCorresponds to variant dbSNP:rs56079860Ensembl.1
Natural variantiVAR_0418281542S → T1 PublicationCorresponds to variant dbSNP:rs1867780Ensembl.1
Natural variantiVAR_0418291699R → G1 PublicationCorresponds to variant dbSNP:rs34004337Ensembl.1

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_005254670.2
XP_005254728.1, XM_005254671.2
XP_005254730.1, XM_005254673.2
XP_005254731.1, XM_005254674.2
XP_005254732.1, XM_005254675.4
XP_011520335.1, XM_011522033.2
XP_011520336.1, XM_011522034.2
XP_011520337.1, XM_011522035.2
XP_011520338.1, XM_011522036.2
XP_011520339.1, XM_011522037.2
XP_011520340.1, XM_011522038.2
XP_011520341.1, XM_011522039.2
UniGeneiHs.731402
Hs.9587

Genome annotation databases

EnsembliENST00000312493; ENSP00000309230; ENSG00000173517
ENST00000560626; ENSP00000452796; ENSG00000173517
GeneIDi79834
KEGGihsa:79834
UCSCiuc059lyw.1 human

Keywords - Coding sequence diversityi

Polymorphism

Similar proteinsi

Entry informationi

Entry nameiPEAK1_HUMAN
AccessioniPrimary (citable) accession number: Q9H792
Secondary accession number(s): Q6ZS78
, Q8NAZ4, Q8NCM3, Q8TEG7
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 3, 2006
Last sequence update: February 10, 2009
Last modified: June 20, 2018
This is version 143 of the entry and version 4 of the sequence. See 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

3D-structure, Complete proteome, Reference proteome

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