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Protein
Submitted name:

Focal adhesion kinase 1

Gene

PTK2

Organism
Homo sapiens (Human)
Status
Unreviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at protein leveli

Functioni

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Names & Taxonomyi

Protein namesi
Submitted name:
Focal adhesion kinase 1Imported
Gene namesi
Name:PTK2Imported
OrganismiHomo sapiens (Human)Imported
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 8

Organism-specific databases

HGNCiHGNC:9611. PTK2.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Proteomic databases

EPDiE7ESA6.

Expressioni

Gene expression databases

ExpressionAtlasiE7ESA6. baseline and differential.

Interactioni

Protein-protein interaction databases

STRINGi9606.ENSP00000341189.

Structurei

3D structure databases

SMRiE7ESA6. Positions 78-730, 952-1093.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini79 – 399321FERMInterPro annotationAdd
BLAST
Domaini466 – 724259Protein kinaseInterPro annotationAdd
BLAST

Sequence similaritiesi

Belongs to the protein kinase superfamily. Tyr protein kinase family.SAAS annotation

Phylogenomic databases

eggNOGiKOG4257. Eukaryota.
ENOG410ZH9Y. LUCA.
GeneTreeiENSGT00760000118799.
OMAiKSGCSPF.
PhylomeDBiE7ESA6.

Family and domain databases

InterProiIPR019749. Band_41_domain.
IPR019748. FERM_central.
IPR000299. FERM_domain.
IPR005189. Focal_adhesion_kin_target_dom.
IPR011009. Kinase-like_dom.
IPR011993. PH_dom-like.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
IPR008266. Tyr_kinase_AS.
IPR020635. Tyr_kinase_cat_dom.
IPR029071. Ubiquitin-rel_dom.
[Graphical view]
PfamiPF00373. FERM_M. 1 hit.
PF03623. Focal_AT. 1 hit.
PF07714. Pkinase_Tyr. 1 hit.
[Graphical view]
PRINTSiPR00109. TYRKINASE.
SMARTiSM00295. B41. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMiSSF47031. SSF47031. 1 hit.
SSF50729. SSF50729. 1 hit.
SSF54236. SSF54236. 1 hit.
SSF56112. SSF56112. 1 hit.
SSF68993. SSF68993. 1 hit.
PROSITEiPS50057. FERM_3. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00109. PROTEIN_KINASE_TYR. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

E7ESA6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLLELAGQEA LKPAGAIYME KSGCSPFPVC WAKEYDRYLA SSKIMAAAYL
60 70 80 90 100
DPNLNHTPNS STKTHLGTGM ERSPGAMERV LKVFHYFESN SEPTTWASII
110 120 130 140 150
RHGDATDVRG IIQKIVDSHK VKHVACYGFR LSHLRSEEVH WLHVDMGVSS
160 170 180 190 200
VREKYELAHP PEEWKYELRI RYLPKGFLNQ FTEDKPTLNF FYQQVKSDYM
210 220 230 240 250
LEIADQVDQE IALKLGCLEI RRSYWEMRGN ALEKKSNYEV LEKDVGLKRF
260 270 280 290 300
FPKSLLDSVK AKTLRKLIQQ TFRQFANLNR EESILKFFEI LSPVYRFDKE
310 320 330 340 350
CFKCALGSSW IISVELAIGP EEGISYLTDK GCNPTHLADF TQVQTIQYSN
360 370 380 390 400
SEDKDRKGML QLKIAGAPEP LTVTAPSLTI AENMADLIDG YCRLVNGTSQ
410 420 430 440 450
SFIIRPQKEG ERALPSIPKL ANSEKQGMRT HAVSVSETDD YAEIIDEEDT
460 470 480 490 500
YTMPSTRDYE IQRERIELGR CIGEGQFGDV HQGIYMSPEN PALAVAIKTC
510 520 530 540 550
KNCTSDSVRE KFLQEALTMR QFDHPHIVKL IGVITENPVW IIMELCTLGE
560 570 580 590 600
LRSFLQVRKY SLDLASLILY AYQLSTALAY LESKRFVHRD IAARNVLVSS
610 620 630 640 650
NDCVKLGDFG LSRYMEDSTY YKASKGKLPI KWMAPESINF RRFTSASDVW
660 670 680 690 700
MFGVCMWEIL MHGVKPFQGV KNNDVIGRIE NGERLPMPPN CPPTLYSLMT
710 720 730 740 750
KCWAYDPSRR PRFTELKAQL STILEEEKAQ QEERMRMESR RQATVSWDSG
760 770 780 790 800
GSDEAPPKPS RPGYPSPRSS EGFYPSPQHM VQTNHYQVSG YPGSHGITAM
810 820 830 840 850
AGSIYPGQAS LLDQTDSWNH RPQEIAMWQP NVEDSTVLDL RGIGQVLPTH
860 870 880 890 900
LMEERLIRQQ QEMEEDQRWL EKEERFLKPD VRLSRGSIDR EDGSLQGPIG
910 920 930 940 950
NQHIYQPVGK PDPAAPPKKP PRPGAPGHLG SLASLSSPAD SYNEGVKLQP
960 970 980 990 1000
QEISPPPTAN LDRSNDKVYE NVTGLVKAVI EMSSKIQPAP PEEYVPMVKE
1010 1020 1030 1040 1050
VGLALRTLLA TVDETIPLLP ASTHREIEMA QKLLNSDLGE LINKMKLAQQ
1060 1070 1080 1090
YVMTSLQQEY KKQMLTAAHA LAVDAKNLLD VIDQARLKML GQTRPH
Length:1,096
Mass (Da):124,082
Last modified:March 8, 2011 - v1
Checksum:iCF501C4E502A14DF
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC067931 Genomic DNA. No translation available.
AC100860 Genomic DNA. No translation available.
AC105009 Genomic DNA. No translation available.
AC105235 Genomic DNA. No translation available.
KF458878 Genomic DNA. No translation available.
KF458882 Genomic DNA. No translation available.

Genome annotation databases

EnsembliENST00000517887; ENSP00000429082; ENSG00000169398.
ENST00000519419; ENSP00000429129; ENSG00000169398.
UCSCiuc064qqo.1. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC067931 Genomic DNA. No translation available.
AC100860 Genomic DNA. No translation available.
AC105009 Genomic DNA. No translation available.
AC105235 Genomic DNA. No translation available.
KF458878 Genomic DNA. No translation available.
KF458882 Genomic DNA. No translation available.

3D structure databases

SMRiE7ESA6. Positions 78-730, 952-1093.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9606.ENSP00000341189.

Proteomic databases

EPDiE7ESA6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000517887; ENSP00000429082; ENSG00000169398.
ENST00000519419; ENSP00000429129; ENSG00000169398.
UCSCiuc064qqo.1. human.

Organism-specific databases

HGNCiHGNC:9611. PTK2.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG4257. Eukaryota.
ENOG410ZH9Y. LUCA.
GeneTreeiENSGT00760000118799.
OMAiKSGCSPF.
PhylomeDBiE7ESA6.

Miscellaneous databases

ChiTaRSiPTK2. human.

Gene expression databases

ExpressionAtlasiE7ESA6. baseline and differential.

Family and domain databases

InterProiIPR019749. Band_41_domain.
IPR019748. FERM_central.
IPR000299. FERM_domain.
IPR005189. Focal_adhesion_kin_target_dom.
IPR011009. Kinase-like_dom.
IPR011993. PH_dom-like.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
IPR008266. Tyr_kinase_AS.
IPR020635. Tyr_kinase_cat_dom.
IPR029071. Ubiquitin-rel_dom.
[Graphical view]
PfamiPF00373. FERM_M. 1 hit.
PF03623. Focal_AT. 1 hit.
PF07714. Pkinase_Tyr. 1 hit.
[Graphical view]
PRINTSiPR00109. TYRKINASE.
SMARTiSM00295. B41. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMiSSF47031. SSF47031. 1 hit.
SSF50729. SSF50729. 1 hit.
SSF54236. SSF54236. 1 hit.
SSF56112. SSF56112. 1 hit.
SSF68993. SSF68993. 1 hit.
PROSITEiPS50057. FERM_3. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00109. PROTEIN_KINASE_TYR. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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].
  2. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
    Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
    Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  3. "DNA sequence and analysis of human chromosome 8."
    Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S., Asakawa T.
    , Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Glockner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P., Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H., Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B., O'Neill K., Parker S.C., Polley A., Raymond C.K., Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N., Lander E.S.
    Nature 439:331-335(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
    Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
    Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  5. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  6. "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].
  7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. Ensembl
    Submitted (JUL-2011) to UniProtKB
    Cited for: IDENTIFICATION.
  11. Ensembl
    Submitted (FEB-2012) to UniProtKB
    Cited for: IDENTIFICATION.
  12. "Toward a comprehensive characterization of a human cancer cell phosphoproteome."
    Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., Mohammed S.
    J. Proteome Res. 12:260-271(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiE7ESA6_HUMAN
AccessioniPrimary (citable) accession number: E7ESA6
Entry historyi
Integrated into UniProtKB/TrEMBL: March 8, 2011
Last sequence update: March 8, 2011
Last modified: June 8, 2016
This is version 58 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)
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

Caution

The sequence shown here is derived from an Ensembl automatic analysis pipeline and should be considered as preliminary data.Imported

Keywords - Technical termi

Complete proteome, Proteomics identificationCombined sources, Reference proteomeImported

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 one 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.