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Protein

Serine/threonine-protein kinase D2

Gene

PRKD2

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

Functioni

Serine/threonine-protein kinase that converts transient diacylglycerol (DAG) signals into prolonged physiological effects downstream of PKC, and is involved in the regulation of cell proliferation via MAPK1/3 (ERK1/2) signaling, oxidative stress-induced NF-kappa-B activation, inhibition of HDAC7 transcriptional repression, signaling downstream of T-cell antigen receptor (TCR) and cytokine production, and plays a role in Golgi membrane trafficking, angiogenesis, secretory granule release and cell adhesion (PubMed:15604256, PubMed:14743217, PubMed:17077180, PubMed:16928771, PubMed:17962809, PubMed:17951978, PubMed:18262756, PubMed:19192391, PubMed:19001381, PubMed:23503467, PubMed:28428613). May potentiate mitogenesis induced by the neuropeptide bombesin by mediating an increase in the duration of MAPK1/3 (ERK1/2) signaling, which leads to accumulation of immediate-early gene products including FOS that stimulate cell cycle progression (By similarity). In response to oxidative stress, is phosphorylated at Tyr-438 and Tyr-717 by ABL1, which leads to the activation of PRKD2 without increasing its catalytic activity, and mediates activation of NF-kappa-B (PubMed:15604256, PubMed:28428613). In response to the activation of the gastrin receptor CCKBR, is phosphorylated at Ser-244 by CSNK1D and CSNK1E, translocates to the nucleus, phosphorylates HDAC7, leading to nuclear export of HDAC7 and inhibition of HDAC7 transcriptional repression of NR4A1/NUR77 (PubMed:17962809). Upon TCR stimulation, is activated independently of ZAP70, translocates from the cytoplasm to the nucleus and is required for interleukin-2 (IL2) promoter up-regulation (PubMed:17077180). During adaptive immune responses, is required in peripheral T-lymphocytes for the production of the effector cytokines IL2 and IFNG after TCR engagement and for optimal induction of antibody responses to antigens (By similarity). In epithelial cells stimulated with lysophosphatidic acid (LPA), is activated through a PKC-dependent pathway and mediates LPA-stimulated interleukin-8 (IL8) secretion via a NF-kappa-B-dependent pathway (PubMed:16928771). During TCR-induced T-cell activation, interacts with and is activated by the tyrosine kinase LCK, which results in the activation of the NFAT transcription factors (PubMed:19192391). In the trans-Golgi network (TGN), regulates the fission of transport vesicles that are on their way to the plasma membrane and in polarized cells is involved in the transport of proteins from the TGN to the basolateral membrane (PubMed:14743217). Plays an important role in endothelial cell proliferation and migration prior to angiogenesis, partly through modulation of the expression of KDR/VEGFR2 and FGFR1, two key growth factor receptors involved in angiogenesis (PubMed:19001381). In secretory pathway, is required for the release of chromogranin-A (CHGA)-containing secretory granules from the TGN (PubMed:18262756). Downstream of PRKCA, plays important roles in angiotensin-2-induced monocyte adhesion to endothelial cells (PubMed:17951978). Plays a regulatory role in angiogenesis and tumor growth by phosphorylating a downstream mediator CIB1 isoform 2, resulting in vascular endothelial growth factor A (VEGFA) secretion (PubMed:23503467).By similarity11 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.4 Publications

Cofactori

Mg2+3 Publications

Enzyme regulationi

Activated by DAG and phorbol esters (PubMed:12058027, PubMed:17962809, PubMed:28428613). Phorbol-ester/DAG-type domains bind DAG, mediating translocation to membranes (PubMed:17962809). Autophosphorylation of Ser-710 and phosphorylation of Ser-706 by PKC relieves auto-inhibition by the PH domain (PubMed:17962809). Catalytic activity is further increased by phosphorylation at Tyr-717 in response to oxidative stress (PubMed:28428613).3 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei580ATPPROSITE-ProRule annotation1
Active sitei674Proton acceptorPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri138 – 188Phorbol-ester/DAG-type 1PROSITE-ProRule annotationAdd BLAST51
Zinc fingeri264 – 314Phorbol-ester/DAG-type 2PROSITE-ProRule annotationAdd BLAST51
Nucleotide bindingi557 – 565ATPPROSITE-ProRule annotation9

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • metal ion binding Source: UniProtKB-KW
  • protein kinase activity Source: BHF-UCL
  • protein kinase C activity Source: UniProtKB-EC
  • protein kinase C binding Source: UniProtKB
  • protein serine/threonine kinase activity Source: BHF-UCL

GO - Biological processi

  • adaptive immune response Source: UniProtKB-KW
  • angiogenesis Source: UniProtKB-KW
  • cell adhesion Source: UniProtKB-KW
  • cell death Source: BHF-UCL
  • cellular response to vascular endothelial growth factor stimulus Source: BHF-UCL
  • endothelial tube morphogenesis Source: BHF-UCL
  • intracellular signal transduction Source: BHF-UCL
  • peptidyl-serine phosphorylation Source: BHF-UCL
  • peptidyl-threonine phosphorylation Source: UniProtKB
  • positive regulation of angiogenesis Source: UniProtKB
  • positive regulation of blood vessel endothelial cell migration Source: BHF-UCL
  • positive regulation of cell adhesion Source: UniProtKB
  • positive regulation of CREB transcription factor activity Source: BHF-UCL
  • positive regulation of DNA binding transcription factor activity Source: UniProtKB
  • positive regulation of DNA biosynthetic process Source: UniProtKB
  • positive regulation of endothelial cell chemotaxis Source: BHF-UCL
  • positive regulation of endothelial cell chemotaxis by VEGF-activated vascular endothelial growth factor receptor signaling pathway Source: BHF-UCL
  • positive regulation of endothelial cell migration Source: UniProtKB
  • positive regulation of endothelial cell proliferation Source: UniProtKB
  • positive regulation of ERK1 and ERK2 cascade Source: UniProtKB
  • positive regulation of fibroblast growth factor receptor signaling pathway Source: UniProtKB
  • positive regulation of histone deacetylase activity Source: BHF-UCL
  • positive regulation of interleukin-2 production Source: UniProtKB
  • positive regulation of interleukin-8 production Source: UniProtKB
  • positive regulation of intracellular signal transduction Source: BHF-UCL
  • positive regulation of NF-kappaB transcription factor activity Source: UniProtKB
  • positive regulation of peptidyl-serine phosphorylation Source: BHF-UCL
  • positive regulation of T cell receptor signaling pathway Source: UniProtKB
  • positive regulation of transcription by RNA polymerase II Source: BHF-UCL
  • positive regulation of vascular endothelial growth factor receptor signaling pathway Source: UniProtKB
  • protein autophosphorylation Source: BHF-UCL
  • protein kinase D signaling Source: BHF-UCL
  • protein phosphorylation Source: CACAO
  • sphingolipid biosynthetic process Source: Reactome
  • T cell receptor signaling pathway Source: BHF-UCL
  • vascular endothelial growth factor receptor signaling pathway Source: BHF-UCL

Keywordsi

Molecular functionKinase, Serine/threonine-protein kinase, Transferase
Biological processAdaptive immunity, Angiogenesis, Cell adhesion, Immunity
LigandATP-binding, Magnesium, Metal-binding, Nucleotide-binding, Zinc

Enzyme and pathway databases

BRENDAi2.7.11.13 2681
ReactomeiR-HSA-1660661 Sphingolipid de novo biosynthesis
SignaLinkiQ9BZL6
SIGNORiQ9BZL6

Names & Taxonomyi

Protein namesi
Recommended name:
Serine/threonine-protein kinase D2 (EC:2.7.11.134 Publications)
Alternative name(s):
nPKC-D2
Gene namesi
Name:PRKD2
Synonyms:PKD2
ORF Names:HSPC187
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 19

Organism-specific databases

EuPathDBiHostDB:ENSG00000105287.12
HGNCiHGNC:17293 PRKD2
MIMi607074 gene
neXtProtiNX_Q9BZL6

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 membrane, Cytoplasm, Golgi apparatus, Membrane, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi87Y → F: Loss of phosphorylation. No effect on the interaction with PRKCD. No effect on Ser-706 or/and Ser-710 phosphorylation. 1 Publication1
Mutagenesisi244S → E: Constitutive kinase activity; when associated with E-706 and E-710. 1 Publication1
Mutagenesisi275P → G: Increase in ability to bind phorbol ester, slight increase in ability to bind DAG. 1 Publication1
Mutagenesisi438Y → D: Slight increase in Tyr-717 phosphorylation. No effect on Ser-706 or/and Ser-710 phosphorylation. Increase in Tyr-717 phosphorylation; when associated with E-706 and E-710. 1 Publication1
Mutagenesisi438Y → F: Loss of phosphorylation. No effect on phosphorylation of Tyr-717 and on Ser-706 or/and Ser-710 phosphorylation. 2 Publications1
Mutagenesisi695D → A: Loss of kinase activity. 1 Publication1
Mutagenesisi706S → A: Abolishes phosphorylation. Loss of Tyr-717 phosphorylation and any other tyrosine phosphorylation, and increases NF-kappa-B activation in response to oxidative stress; when associated with A-710. 1 Publication1
Mutagenesisi706S → E: Constitutive kinase activity; when associated with E-710 or with E-244 and E-710. Increases Tyr-717 phosphorylation; when associated with E-710 or with E-710 and D-438. 2 Publications1
Mutagenesisi710S → A: Abolishes phosphorylation. Loss of Tyr-717 phosphorylation and any other tyrosine phosphorylation, and increases NF-kappa-B activation in response to oxidative stress; when associated with A-706. 1 Publication1
Mutagenesisi710S → E: Constitutive kinase activity; when associated with E-706 or with E-244 and E-706. when associated with E-710 or with E-244 and E-710. Increases Tyr-717 phosphorylation; when associated with E-710 or with E-710 and D-438. 2 Publications1
Mutagenesisi717Y → F: Abolishes phosphorylation. Decreases substrate affinity and increases catalytic efficiency. Increases Ser-706 or/and Ser-710 phosphorylation. Increases NF-kappa-B activation in response to oxidative stress. 1 Publication1
Mutagenesisi724 – 726LNQ → RNK: Reduced catalytic activity. Severe reduction in Tyr-717 phosphorylation by ABL1 in response to oxidative stress. No effect on Ser-706 or/and Ser-710 phosphorylation and on NF-kappa-B activation in response to oxidative stress. 1 Publication3

Organism-specific databases

DisGeNETi25865
OpenTargetsiENSG00000105287
PharmGKBiPA134903505

Chemistry databases

ChEMBLiCHEMBL4900
GuidetoPHARMACOLOGYi2173

Polymorphism and mutation databases

BioMutaiPRKD2
DMDMi296434570

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000557161 – 878Serine/threonine-protein kinase D2Add BLAST878

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei30PhosphoserineBy similarity1
Modified residuei87PhosphotyrosineBy similarity1
Modified residuei197PhosphoserineCombined sources1
Modified residuei198PhosphoserineCombined sources1
Modified residuei200PhosphoserineCombined sources1
Modified residuei203PhosphoserineCombined sources1
Modified residuei206PhosphoserineCombined sources1
Modified residuei212PhosphoserineBy similarity1
Modified residuei214PhosphoserineCombined sources1
Modified residuei244Phosphoserine; by CSNK1D and CSNK1E1 Publication1
Modified residuei407PhosphotyrosineBy similarity1
Modified residuei438Phosphotyrosine; by ABL11 Publication1 Publication1
Modified residuei518PhosphoserineCombined sources1
Modified residuei706Phosphoserine; by PKC2 Publications1
Modified residuei710PhosphoserineCombined sources2 Publications1
Modified residuei717Phosphotyrosine; by ABL1Combined sources1 Publication1
Modified residuei876Phosphoserine; by autocatalysisCombined sources2 Publications1

Post-translational modificationi

Phosphorylation of Ser-876 correlates with the activation status of the kinase (PubMed:11062248). Ser-706 or/and Ser-710 are probably phosphorylated by PKC (PubMed:12058027, PubMed:28428613). Phosphorylation at Ser-244 by CSNK1D and CSNK1E promotes nuclear localization and substrate targeting (PubMed:17962809). Phosphorylation at Ser-244, Ser-706 and Ser-710 is required for nuclear localization (PubMed:17962809). Phosphorylated at Tyr-438 by ABL1 in response to oxidative stress (PubMed:15604256). Phosphorylated at Tyr-717 by ABL1 specifically in response to oxidative stress; requires prior phosphorylation at Ser-706 or/and Ser-710 (PubMed:28428613).5 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ9BZL6
MaxQBiQ9BZL6
PaxDbiQ9BZL6
PeptideAtlasiQ9BZL6
PRIDEiQ9BZL6
ProteomicsDBi79872

PTM databases

iPTMnetiQ9BZL6
PhosphoSitePlusiQ9BZL6

Expressioni

Tissue specificityi

Widely expressed.1 Publication

Gene expression databases

BgeeiENSG00000105287
CleanExiHS_PKD2
HS_PRKD2
ExpressionAtlasiQ9BZL6 baseline and differential
GenevisibleiQ9BZL6 HS

Organism-specific databases

HPAiHPA021490
HPA056727

Interactioni

Subunit structurei

Interacts (via C-terminus) with LCK (PubMed:19192391). Interacts (via N-terminal AP-rich region) with CIB1 isoform 2 (PubMed:23503467). Interacts (via N-terminus and zing-finger domain 1 and 2) with PRKCD in response to oxidative stress; the interaction is independent of PRKD2 tyrosine phosphorylation (PubMed:28428613).3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
HDAC7Q8WUI46EBI-1384325,EBI-1048378

GO - Molecular functioni

  • protein kinase C binding Source: UniProtKB

Protein-protein interaction databases

BioGridi117384, 43 interactors
IntActiQ9BZL6, 35 interactors
MINTiQ9BZL6
STRINGi9606.ENSP00000291281

Chemistry databases

BindingDBiQ9BZL6

Structurei

Secondary structure

1878
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi399 – 406Combined sources8
Beta strandi409 – 411Combined sources3
Beta strandi415 – 421Combined sources7
Beta strandi423 – 433Combined sources11
Beta strandi438 – 442Combined sources5
Turni443 – 445Combined sources3
Beta strandi448 – 452Combined sources5
Beta strandi456 – 458Combined sources3
Beta strandi465 – 470Combined sources6
Beta strandi486 – 488Combined sources3
Helixi495 – 507Combined sources13

3D structure databases

ProteinModelPortaliQ9BZL6
SMRiQ9BZL6
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9BZL6

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini397 – 509PHPROSITE-ProRule annotationAdd BLAST113
Domaini551 – 807Protein kinasePROSITE-ProRule annotationAdd BLAST257

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi724 – 726Important for ABL1-mediated Tyr-717 phosphorylation1 Publication3

Sequence similaritiesi

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri138 – 188Phorbol-ester/DAG-type 1PROSITE-ProRule annotationAdd BLAST51
Zinc fingeri264 – 314Phorbol-ester/DAG-type 2PROSITE-ProRule annotationAdd BLAST51

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiKOG4236 Eukaryota
ENOG410XQZ3 LUCA
GeneTreeiENSGT00910000144054
HOGENOMiHOG000015135
HOVERGENiHBG003564
InParanoidiQ9BZL6
KOiK06070
OMAiCIILFQN
OrthoDBiEOG091G02RG
PhylomeDBiQ9BZL6
TreeFamiTF314320

Family and domain databases

CDDicd00029 C1, 2 hits
Gene3Di2.30.29.30, 1 hit
InterProiView protein in InterPro
IPR020454 DAG/PE-bd
IPR011009 Kinase-like_dom_sf
IPR002219 PE/DAG-bd
IPR011993 PH-like_dom_sf
IPR001849 PH_domain
IPR000719 Prot_kinase_dom
IPR017441 Protein_kinase_ATP_BS
IPR015727 Protein_Kinase_C_mu-related
IPR008271 Ser/Thr_kinase_AS
PANTHERiPTHR22968 PTHR22968, 1 hit
PfamiView protein in Pfam
PF00130 C1_1, 2 hits
PF00069 Pkinase, 1 hit
PIRSFiPIRSF000552 PKC_mu_nu_D2, 1 hit
PRINTSiPR00008 DAGPEDOMAIN
SMARTiView protein in SMART
SM00109 C1, 2 hits
SM00233 PH, 1 hit
SM00220 S_TKc, 1 hit
SUPFAMiSSF56112 SSF56112, 1 hit
PROSITEiView protein in PROSITE
PS50003 PH_DOMAIN, 1 hit
PS00107 PROTEIN_KINASE_ATP, 1 hit
PS50011 PROTEIN_KINASE_DOM, 1 hit
PS00108 PROTEIN_KINASE_ST, 1 hit
PS00479 ZF_DAG_PE_1, 2 hits
PS50081 ZF_DAG_PE_2, 2 hits

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9BZL6-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MATAPSYPAG LPGSPGPGSP PPPGGLELQS PPPLLPQIPA PGSGVSFHIQ
60 70 80 90 100
IGLTREFVLL PAASELAHVK QLACSIVDQK FPECGFYGLY DKILLFKHDP
110 120 130 140 150
TSANLLQLVR SSGDIQEGDL VEVVLSASAT FEDFQIRPHA LTVHSYRAPA
160 170 180 190 200
FCDHCGEMLF GLVRQGLKCD GCGLNYHKRC AFSIPNNCSG ARKRRLSSTS
210 220 230 240 250
LASGHSVRLG TSESLPCTAE ELSRSTTELL PRRPPSSSSS SSASSYTGRP
260 270 280 290 300
IELDKMLLSK VKVPHTFLIH SYTRPTVCQA CKKLLKGLFR QGLQCKDCKF
310 320 330 340 350
NCHKRCATRV PNDCLGEALI NGDVPMEEAT DFSEADKSAL MDESEDSGVI
360 370 380 390 400
PGSHSENALH ASEEEEGEGG KAQSSLGYIP LMRVVQSVRH TTRKSSTTLR
410 420 430 440 450
EGWVVHYSNK DTLRKRHYWR LDCKCITLFQ NNTTNRYYKE IPLSEILTVE
460 470 480 490 500
SAQNFSLVPP GTNPHCFEIV TANATYFVGE MPGGTPGGPS GQGAEAARGW
510 520 530 540 550
ETAIRQALMP VILQDAPSAP GHAPHRQASL SISVSNSQIQ ENVDIATVYQ
560 570 580 590 600
IFPDEVLGSG QFGVVYGGKH RKTGRDVAVK VIDKLRFPTK QESQLRNEVA
610 620 630 640 650
ILQSLRHPGI VNLECMFETP EKVFVVMEKL HGDMLEMILS SEKGRLPERL
660 670 680 690 700
TKFLITQILV ALRHLHFKNI VHCDLKPENV LLASADPFPQ VKLCDFGFAR
710 720 730 740 750
IIGEKSFRRS VVGTPAYLAP EVLLNQGYNR SLDMWSVGVI MYVSLSGTFP
760 770 780 790 800
FNEDEDINDQ IQNAAFMYPA SPWSHISAGA IDLINNLLQV KMRKRYSVDK
810 820 830 840 850
SLSHPWLQEY QTWLDLRELE GKMGERYITH ESDDARWEQF AAEHPLPGSG
860 870
LPTDRDLGGA CPPQDHDMQG LAERISVL
Length:878
Mass (Da):96,722
Last modified:March 28, 2018 - v3
Checksum:i8BAB45E8F99D23E7
GO
Isoform 2 (identifier: Q9BZL6-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-157: Missing.

Note: No experimental confirmation available.
Show »
Length:721
Mass (Da):80,115
Checksum:i8A97CE31824C078D
GO
Isoform 3 (identifier: Q9BZL6-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     779-779: G → GGAWGPPTPWA

Show »
Length:888
Mass (Da):97,743
Checksum:i6AF04D6B9FC444FC
GO

Sequence cautioni

The sequence AAF36107 differs from that shown. Reason: Frameshift at positions 604, 606, 738, 744, 755, 758, 833 and 854.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti790V → L in AAF36107 (PubMed:11042152).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_042330324V → M1 PublicationCorresponds to variant dbSNP:rs45455991Ensembl.1
Natural variantiVAR_042331496A → V1 PublicationCorresponds to variant dbSNP:rs55716765Ensembl.1
Natural variantiVAR_042332604S → G1 PublicationCorresponds to variant dbSNP:rs34325043Ensembl.1
Natural variantiVAR_042333773W → R1 PublicationCorresponds to variant dbSNP:rs55933311Ensembl.1
Natural variantiVAR_061531835A → V. Corresponds to variant dbSNP:rs314665Ensembl.1
Natural variantiVAR_042334848G → E in a lung adenocarcinoma sample; somatic mutation. 1 Publication1
Natural variantiVAR_042335870G → E in a gastric adenocarcinoma sample; somatic mutation. 1 Publication1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0572791 – 157Missing in isoform 2. 1 PublicationAdd BLAST157
Alternative sequenceiVSP_059398779G → GGAWGPPTPWA in isoform 3. 1 Publication1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF309082 mRNA Translation: AAK01149.1
AK074673 mRNA Translation: BAC11127.1
AK095884 mRNA Translation: BAG53158.1
AK300339 mRNA Translation: BAG62084.1
AC008635 Genomic DNA No translation available.
AC093503 Genomic DNA No translation available.
KC877745 Genomic DNA No translation available.
AL050147 mRNA Translation: CAB43292.1
AF151021 mRNA Translation: AAF36107.1 Frameshift.
CCDSiCCDS12689.1 [Q9BZL6-1]
CCDS59401.1 [Q9BZL6-2]
PIRiT08777
RefSeqiNP_001073349.1, NM_001079880.1 [Q9BZL6-1]
NP_001073350.1, NM_001079881.1 [Q9BZL6-1]
NP_001073351.1, NM_001079882.1 [Q9BZL6-2]
NP_057541.2, NM_016457.4 [Q9BZL6-1]
XP_005258773.2, XM_005258716.2 [Q9BZL6-2]
UniGeneiHs.466987

Genome annotation databases

EnsembliENST00000291281; ENSP00000291281; ENSG00000105287 [Q9BZL6-1]
ENST00000433867; ENSP00000393978; ENSG00000105287 [Q9BZL6-1]
ENST00000595515; ENSP00000470804; ENSG00000105287 [Q9BZL6-3]
ENST00000600194; ENSP00000472744; ENSG00000105287 [Q9BZL6-2]
ENST00000601806; ENSP00000469106; ENSG00000105287 [Q9BZL6-2]
GeneIDi25865
KEGGihsa:25865
UCSCiuc002pfi.4 human [Q9BZL6-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Similar proteinsi

Entry informationi

Entry nameiKPCD2_HUMAN
AccessioniPrimary (citable) accession number: Q9BZL6
Secondary accession number(s): B4DTS2
, M0QZW1, M0R2R2, Q8NCK8, Q8TB08, Q9P0T6, Q9Y3X8
Entry historyiIntegrated into UniProtKB/Swiss-Prot: March 27, 2002
Last sequence update: March 28, 2018
Last modified: June 20, 2018
This is version 187 of the entry and version 3 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

Documents

  1. Human chromosome 19
    Human chromosome 19: 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  7. SIMILARITY comments
    Index of protein domains and families

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