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Protein
Submitted name:

3-phosphoinositide-dependent protein kinase 1

Gene

PDPK1

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

Functioni

GO - Molecular functioni

  1. 3-phosphoinositide-dependent protein kinase activity Source: Ensembl
  2. ATP binding Source: UniProtKB-KW

GO - Biological processi

  1. focal adhesion assembly Source: Ensembl
  2. hyperosmotic response Source: Ensembl
  3. negative regulation of cardiac muscle cell apoptotic process Source: Ensembl
  4. negative regulation of toll-like receptor signaling pathway Source: Ensembl
  5. regulation of endothelial cell migration Source: Ensembl
  6. regulation of mast cell degranulation Source: Ensembl
  7. type B pancreatic cell development Source: Ensembl
Complete GO annotation...

Keywords - Ligandi

ATP-bindingUniRule annotation, Nucleotide-binding

Enzyme and pathway databases

SignaLinkiE9PER6.

Names & Taxonomyi

Protein namesi
Submitted name:
3-phosphoinositide-dependent protein kinase 1Imported
Gene namesi
Name:PDPK1Imported
OrganismiHomo sapiens (Human)Imported
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 16

Organism-specific databases

HGNCiHGNC:8816. PDPK1.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: HPA
  2. cytoplasmic membrane-bounded vesicle Source: Ensembl
  3. cytosol Source: Ensembl
  4. plasma membrane Source: Ensembl
Complete GO annotation...

PTM / Processingi

Proteomic databases

PRIDEiE9PER6.

Expressioni

Gene expression databases

BgeeiE9PER6.
ExpressionAtlasiE9PER6. baseline and differential.

Interactioni

Structurei

3D structure databases

ProteinModelPortaliE9PER6.
SMRiE9PER6. Positions 44-529.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Phylogenomic databases

GeneTreeiENSGT00550000074819.
KOiK06276.

Family and domain databases

Gene3Di2.30.29.30. 2 hits.
InterProiIPR011009. Kinase-like_dom.
IPR011993. PH_like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00069. Pkinase. 1 hit.
[Graphical view]
SMARTiSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

E9PER6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVRTQTESST PPGIPGGSRQ GPAMDGTAAE PRPGAGSLQH AQPPPQPRKK
60 70 80 90 100
RPEDFKFGKI LGEGSFSTVV LARELATSRE YAIKILEKRH IIKENKVPYV
110 120 130 140 150
TRERDVMSRL DHPFFVKLYF TFQDDEKLYF GLSYAKNGEL LKYIRKIGSF
160 170 180 190 200
DETCTRFYTA EIVSALEYLH GKGIIHRDLK PENILLNEDM HIQITDFGTA
210 220 230 240 250
KVLSPESKQA RANSFVGTAQ YVSPELLTEK SACKSSDLWA LGCIIYQLVA
260 270 280 290 300
GLPPFRAGNE YLIFQKIIKL EYDFPEKFFP KARDLVEKLL VLDATKRLGC
310 320 330 340 350
EEMEGYGPLK AHPFFESVTW ENLHQQTPPK LTAYLPAMSE DDEDCYGNYD
360 370 380 390 400
NLLSQFGCMQ VSSSSSSHSL SASDTGLPQR SGSNIEQYIH DLDSNSFELD
410 420 430 440 450
LQFSEDEKRL LLEKQAGGNP WHQFVENNLI LKMGPVDKRK GLFARRRQLL
460 470 480 490 500
LTEGPHLYYV DPVNKVLKGE IPWSQELRPE AKNFKTFFVH TPNRTYYLMD
510 520
PSGNAHKWCR KIQEVWRQRY QSHPDAAVQ
Length:529
Mass (Da):60,329
Last modified:April 5, 2011 - v1
Checksum:iD2E118E969E45DF7
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC093525 Genomic DNA. No translation available.
AC141586 Genomic DNA. No translation available.
RefSeqiXP_005255413.1. XM_005255356.1.
UniGeneiHs.459691.

Genome annotation databases

EnsembliENST00000389224; ENSP00000373876; ENSG00000140992.
GeneIDi5170.
KEGGihsa:5170.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC093525 Genomic DNA. No translation available.
AC141586 Genomic DNA. No translation available.
RefSeqiXP_005255413.1. XM_005255356.1.
UniGeneiHs.459691.

3D structure databases

ProteinModelPortaliE9PER6.
SMRiE9PER6. Positions 44-529.
ModBaseiSearch...
MobiDBiSearch...

Chemistry

BindingDBiE9PER6.

Proteomic databases

PRIDEiE9PER6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000389224; ENSP00000373876; ENSG00000140992.
GeneIDi5170.
KEGGihsa:5170.

Organism-specific databases

CTDi5170.
HGNCiHGNC:8816. PDPK1.
GenAtlasiSearch...

Phylogenomic databases

GeneTreeiENSGT00550000074819.
KOiK06276.

Enzyme and pathway databases

SignaLinkiE9PER6.

Miscellaneous databases

ChiTaRSiPDPK1. human.
GenomeRNAii5170.
NextBioi35501766.

Gene expression databases

BgeeiE9PER6.
ExpressionAtlasiE9PER6. baseline and differential.

Family and domain databases

Gene3Di2.30.29.30. 2 hits.
InterProiIPR011009. Kinase-like_dom.
IPR011993. PH_like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00069. Pkinase. 1 hit.
[Graphical view]
SMARTiSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The sequence and analysis of duplication-rich human chromosome 16."
    Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.
    , Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A.
    Nature 432:988-994(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  2. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  3. Ensembl
    Submitted (JUL-2011) to UniProtKB
    Cited for: IDENTIFICATION.
  4. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiE9PER6_HUMAN
AccessioniPrimary (citable) accession number: E9PER6
Entry historyi
Integrated into UniProtKB/TrEMBL: April 5, 2011
Last sequence update: April 5, 2011
Last modified: April 29, 2015
This is version 34 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

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.