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Q9WTQ1 (KPCD1_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 87. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Serine/threonine-protein kinase D1

EC=2.7.11.13
Alternative name(s):
Protein kinase C mu type
Protein kinase D
nPKC-D1
nPKC-mu
Gene names
Name:Prkd1
Synonyms:Pkcm, Pkd, Prkcm
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length918 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Serine/threonine-protein kinase that converts transient diacylglycerol (DAG) signals into prolonged physiological effects downstream of PKC, and is involved in the regulation of MAPK8/JNK1 and Ras signaling, Golgi membrane integrity and trafficking, cell survival through NF-kappa-B activation, cell migration, cell differentiation by mediating HDAC7 nuclear export, cell proliferation via MAPK1/3 (ERK1/2) signaling, and plays a role in cardiac hypertrophy, VEGFA-induced angiogenesis, genotoxic-induced apoptosis and flagellin-stimulated inflammatory response. Phosphorylates the epidermal growth factor receptor (EGFR) on dual threonine residues, which leads to the suppression of epidermal growth factor (EGF)-induced MAPK8/JNK1 activation and subsequent JUN phosphorylation. Phosphorylates RIN1, inducing RIN1 binding to 14-3-3 proteins YWHAB, YWHAE and YWHAZ and increased competition with RAF1 for binding to GTP-bound form of Ras proteins (NRAS, HRAS and KRAS). Acts downstream of the heterotrimeric G-protein beta/gamma-subunit complex to maintain the structural integrity of the Golgi membranes, and is required for protein transport along the secretory pathway. In the trans-Golgi network (TGN), regulates the fission of transport vesicles that are on their way to the plasma membrane. May act by activating the lipid kinase phosphatidylinositol 4-kinase beta (PI4KB) at the TGN for the local synthesis of phosphorylated inositol lipids, which induces a sequential production of DAG, phosphatidic acid (PA) and lyso-PA (LPA) that are necessary for membrane fission and generation of specific transport carriers to the cell surface. Under oxidative stress, is phosphorylated at Tyr-469 via SRC-ABL1 and contributes to cell survival by activating IKK complex and subsequent nuclear translocation and activation of NFKB1. Involved in cell migration by regulating integrin alpha-5/beta-3 recycling and promoting its recruitment in newly forming focal adhesion. In osteoblast differentiation, mediates the bone morphogenic protein 2 (BMP2)-induced nuclear export of HDAC7, which results in the inhibition of HDAC7 transcriptional repression of RUNX2. In neurons, plays an important role in neuronal polarity by regulating the biogenesis of TGN-derived dendritic vesicles, and is involved in the maintenance of dendritic arborization and Golgi structure in hippocampal cells. May potentiate mitogenesis induced by the neuropeptide bombesin or vasopressin 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. Plays an important role in the proliferative response induced by low calcium in keratinocytes, through sustained activation of MAPK1/3 (ERK1/2) pathway. Downstream of novel PKC signaling, plays a role in cardiac hypertrophy by phosphorylating HDAC5, which in turn triggers XPO1/CRM1-dependent nuclear export of HDAC5, MEF2A transcriptional activation and induction of downstream target genes that promote myocyte hypertrophy and pathological cardiac remodeling. Mediates cardiac troponin I (TNNI3) phosphorylation at the PKA sites, which results in reduced myofilament calcium sensitivity, and accelerated crossbridge cycling kinetics. The PRKD1-HDAC5 pathway is also involved in angiogenesis by mediating VEGFA-induced specific subset of gene expression, cell migration, and tube formation. In response to VEGFA, is necessary and required for HDAC7 phosphorylation which induces HDAC7 nuclear export and endothelial cell proliferation and migration. During apoptosis induced by cytarabine and other genotoxic agents, PRKD1 is cleaved by caspase-3 at Asp-378, resulting in activation of its kinase function and increased sensitivity of cells to the cytotoxic effects of genotoxic agents. In epithelial cells, is required for transducing flagellin-stimulated inflammatory responses by binding and phosphorylating TLR5, which contributes to MAPK14/p38 activation and production of inflammatory cytokines. May play a role in inflammatory response by mediating activation of NF-kappa-B. May be involved in pain transmission by directly modulating TRPV1 receptor. Ref.3 Ref.4 Ref.6 Ref.7

Catalytic activity

ATP + a protein = ADP + a phosphoprotein.

Cofactor

Magnesium By similarity.

Enzyme regulation

Activated by DAG and phorbol esters. Phorbol-ester/DAG-type domain 1 binds DAG with high affinity and appears to play the dominant role in mediating translocation to the cell membrane and trans-Golgi network. Phorbol-ester/DAG-type domain 2 binds phorbol ester with higher affinity. Autophosphorylation of Ser-748 and phosphorylation of Ser-744 by PKC relieves auto-inhibition by the PH domain. Phosphorylation on Tyr-469 by the SRC-ABL1 pathway in response to oxidative stress, is also required for activation. Activated by DAPK1 under oxidative stress By similarity.

Subunit structure

Interacts (via N-terminus) with ADAP1/CENTA1. Interacts with MAPK13 and SRC By similarity. Interacts with DAPK1 in an oxidative stress-regulated manner By similarity.

Subcellular location

Cytoplasm By similarity. Cell membrane By similarity. Golgi apparatustrans-Golgi network By similarity. Note: Translocation to the cell membrane is required for kinase activation By similarity.

Post-translational modification

Phosphorylated at Ser-403 and Ser-407 by MAPK13 during regulation of insulin secretion in pancreatic beta cells. Phosphorylated by DAPK1. Phosphorylated by ABL at Tyr-469, which primes the kinase in response to oxidative stress, and promotes a second step activating phosphorylation at Ser-744/Ser-748 by PKRD By similarity. Ref.5

Sequence similarities

Belongs to the protein kinase superfamily. CAMK Ser/Thr protein kinase family. PKD subfamily.

Contains 1 PH domain.

Contains 2 phorbol-ester/DAG-type zinc fingers.

Contains 1 protein kinase domain.

Ontologies

Keywords
   Biological processAngiogenesis
Apoptosis
Differentiation
Immunity
Inflammatory response
Innate immunity
Neurogenesis
   Cellular componentCell membrane
Cytoplasm
Golgi apparatus
Membrane
   DomainRepeat
Zinc-finger
   LigandATP-binding
Magnesium
Metal-binding
Nucleotide-binding
Zinc
   Molecular functionKinase
Serine/threonine-protein kinase
Transferase
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processGolgi organization

Inferred from sequence or structural similarity. Source: UniProtKB

Golgi vesicle transport

Inferred from sequence or structural similarity. Source: UniProtKB

angiogenesis

Inferred from electronic annotation. Source: UniProtKB-KW

apoptotic process

Inferred from electronic annotation. Source: UniProtKB-KW

cellular response to oxidative stress

Inferred from sequence or structural similarity. Source: UniProtKB

cellular response to vascular endothelial growth factor stimulus

Inferred from sequence or structural similarity. Source: UniProtKB

inflammatory response

Inferred from electronic annotation. Source: UniProtKB-KW

innate immune response

Inferred from electronic annotation. Source: UniProtKB-KW

intracellular signal transduction

Inferred from direct assay PubMed 12057008. Source: RGD

negative regulation of cell death

Inferred from sequence or structural similarity. Source: UniProtKB

peptidyl-serine phosphorylation

Inferred from electronic annotation. Source: Ensembl

positive regulation of CREB transcription factor activity

Inferred from electronic annotation. Source: Ensembl

positive regulation of I-kappaB kinase/NF-kappaB signaling

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of NF-kappaB transcription factor activity

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of angiogenesis

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of blood vessel endothelial cell migration

Inferred from electronic annotation. Source: Ensembl

positive regulation of endothelial cell chemotaxis by VEGF-activated vascular endothelial growth factor receptor signaling pathway

Inferred from electronic annotation. Source: Ensembl

positive regulation of endothelial cell migration

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of endothelial cell proliferation

Inferred from electronic annotation. Source: Ensembl

positive regulation of histone deacetylase activity

Inferred from electronic annotation. Source: Ensembl

positive regulation of neuron projection development

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of osteoblast differentiation

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of peptidyl-serine phosphorylation

Inferred from electronic annotation. Source: Ensembl

positive regulation of transcription from RNA polymerase II promoter

Inferred from electronic annotation. Source: Ensembl

regulation of keratinocyte proliferation

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentcell cortex

Inferred from electronic annotation. Source: Ensembl

cell-cell junction

Inferred from electronic annotation. Source: Ensembl

cytosol

Inferred from sequence or structural similarity. Source: UniProtKB

nucleus

Inferred from electronic annotation. Source: Ensembl

plasma membrane

Inferred from sequence or structural similarity. Source: UniProtKB

trans-Golgi network

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein kinase C activity

Inferred from electronic annotation. Source: UniProtKB-EC

protein serine/threonine kinase activity

Inferred from direct assay PubMed 12057008. Source: RGD

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 918918Serine/threonine-protein kinase D1
PRO_0000333881

Regions

Domain428 – 547120PH
Domain589 – 845257Protein kinase
Zinc finger144 – 19451Phorbol-ester/DAG-type 1
Zinc finger276 – 32651Phorbol-ester/DAG-type 2
Nucleotide binding595 – 6039ATP By similarity
Compositional bias16 – 2611Poly-Ala
Compositional bias198 – 2014Poly-Arg

Sites

Active site7121Proton acceptor By similarity
Binding site6181ATP By similarity

Amino acid modifications

Modified residue931Phosphotyrosine By similarity
Modified residue2031Phosphoserine By similarity
Modified residue2061Phosphoserine By similarity
Modified residue3511Phosphoserine By similarity
Modified residue4031Phosphoserine; by MAPK13 By similarity
Modified residue4071Phosphoserine; by MAPK13 By similarity
Modified residue4381Phosphotyrosine By similarity
Modified residue4541Phosphoserine By similarity
Modified residue4691Phosphotyrosine; by ABL By similarity
Modified residue5081Phosphotyrosine By similarity
Modified residue7441Phosphoserine; by PKC/PRKCD By similarity
Modified residue7481Phosphoserine; by autocatalysis and PKC/PRKCD By similarity
Modified residue9161Phosphoserine; by autocatalysis Ref.5

Experimental info

Sequence conflict7181V → G in BAA78373. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q9WTQ1 [UniParc].

Last modified May 20, 2008. Version 2.
Checksum: 93E46AF6C0242B86

FASTA918102,043
        10         20         30         40         50         60 
MSAPPLLRPP SPLLPAAAAV AAAAAALVPG SGPAPFPAPG AAPAGGISFH LQIGLSREPV 

        70         80         90        100        110        120 
LLLQDSSGDY SLAHVREMAC SIVDQKFPEC GFYGLYDKIL LFRHDPASEN ILQLVKIASD 

       130        140        150        160        170        180 
IQEGDLIEVV LSASATFEDF QIRPHALFVH SYRAPAFCDH CGEMLWGLVR QGLKCEGCGL 

       190        200        210        220        230        240 
NYHKRCAFKI PNNCSGVRRR RLSNVSLTGL GTVRTASAEF STSAPDEPLL SPVSPGFEQK 

       250        260        270        280        290        300 
SPSESFIGRE KRSNSQSYVG RPIQLDKLLM SKVKVPHTFV IHSYTRPTVC QFCKKLLKGL 

       310        320        330        340        350        360 
FRQGLQCKDC RFNCHKRCAP KVPNNCLGEV TINGELLSPG AESDVVMEEG SDDNDSERNS 

       370        380        390        400        410        420 
GLMDDMDEAM VQDTEMALAE GQSDGAEMQD PDADQEDSNR TISPSTSNNI PLMRVVQSVK 

       430        440        450        460        470        480 
HTKRRSSTVM KEGWMVHYTS KDTLRKRHYW RLDSKSITLF QNDTGSRYYK EIPLSEILCL 

       490        500        510        520        530        540 
EPAKPSALIP TGANPHCFEI TTANVVYYVG ENVVNPSSPP PNNSVPPSGI GTDVARMWEV 

       550        560        570        580        590        600 
AIQHALMPVI PKGSSVGSGT NSHKDISVSI SVSNSQIQEN VDISTVYQIF PDEVLGSGQF 

       610        620        630        640        650        660 
GIVYGGKHRK TGRDVAIKII DKLRFPTKQE SQLRNEVAIL QNLHHPGVVN LECMFETPER 

       670        680        690        700        710        720 
VFVVMEKLHG DMLEMILSSE KGRLPEHITK FLITQILVAL RHLHFKNIVH CDLKPENVLL 

       730        740        750        760        770        780 
ASADPFPQVK LCDFGFARII GEKSFRRSVV GTPAYLAPEV LRNKGYNRSL DMWSVGVIIY 

       790        800        810        820        830        840 
VSLSGTFPFN EDEDIHDQIQ NAAFMYPPNP WKEISHEAID LINNLLQVKM RKRYSVDKTL 

       850        860        870        880        890        900 
SHPWLQDYQT WLDLRELECR IGERYITHES DDSRWEQYAG EQGLQYPAHL INLSASHGDS 

       910 
PEAEEREMKA LSERVSIL 

« Hide

References

« Hide 'large scale' references
[1]"Genome sequence of the Brown Norway rat yields insights into mammalian evolution."
Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., Morgan M. expand/collapse author list , Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., Collins F.S.
Nature 428:493-521(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Brown Norway.
[2]"Rat PKC mu mRNA partial cds."
Minami H., Owada Y., Kondo H.
Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 718-864.
Strain: Wistar.
Tissue: Brain.
[3]"Gbetagamma-mediated regulation of Golgi organization is through the direct activation of protein kinase D."
Jamora C., Yamanouye N., Van Lint J., Laudenslager J., Vandenheede J.R., Faulkner D.J., Malhotra V.
Cell 98:59-68(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN GOLGI REGULATION.
[4]"Protein kinase D is a novel mediator of cardiac troponin I phosphorylation and regulates myofilament function."
Haworth R.S., Cuello F., Herron T.J., Franzen G., Kentish J.C., Gautel M., Avkiran M.
Circ. Res. 95:1091-1099(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN CARDIOMYOCYTE.
[5]"Hepatocyte resistance to oxidative stress is dependent on protein kinase C-mediated down-regulation of c-Jun/AP-1."
Wang Y., Schattenberg J.M., Rigoli R.M., Storz P., Czaja M.J.
J. Biol. Chem. 279:31089-31097(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-744; SER-748 AND SER-916.
[6]"Protein kinases C and D mediate agonist-dependent cardiac hypertrophy through nuclear export of histone deacetylase 5."
Vega R.B., Harrison B.C., Meadows E., Roberts C.R., Papst P.J., Olson E.N., McKinsey T.A.
Mol. Cell. Biol. 24:8374-8385(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN CARDIAC HYPERTROPHY.
[7]"Protein kinase d regulates trafficking of dendritic membrane proteins in developing neurons."
Bisbal M., Conde C., Donoso M., Bollati F., Sesma J., Quiroga S., Diaz Anel A., Malhotra V., Marzolo M.P., Caceres A.
J. Neurosci. 28:9297-9308(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN NEURONAL POLARITY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AABR03048549 Genomic DNA. No translation available.
AABR03048623 Genomic DNA. No translation available.
AABR03048825 Genomic DNA. No translation available.
AABR03049215 Genomic DNA. No translation available.
AABR03049278 Genomic DNA. No translation available.
AABR03050321 Genomic DNA. No translation available.
AABR03052344 Genomic DNA. No translation available.
AB020616 mRNA. Translation: BAA78373.1.
RefSeqNP_001263644.1. NM_001276715.1.
UniGeneRn.144619.
Rn.234516.

3D structure databases

ProteinModelPortalQ9WTQ1.
SMRQ9WTQ1. Positions 425-552.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ9WTQ1. 1 interaction.
STRING10116.ENSRNOP00000005596.

PTM databases

PhosphoSiteQ9WTQ1.

Proteomic databases

PaxDbQ9WTQ1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000068077; ENSRNOP00000063159; ENSRNOG00000004165.
GeneID85421.
KEGGrno:85421.
UCSCRGD:620964. rat.

Organism-specific databases

CTD5587.
RGD620964. Prkd1.

Phylogenomic databases

eggNOGCOG0515.
GeneTreeENSGT00750000117523.
HOGENOMHOG000015135.
HOVERGENHBG003564.
InParanoidQ9WTQ1.
KOK06070.
OMAMAECQND.
OrthoDBEOG75B84N.
PhylomeDBQ9WTQ1.

Gene expression databases

GenevestigatorQ9WTQ1.

Family and domain databases

Gene3D2.30.29.30. 1 hit.
InterProIPR020454. DAG/PE-bd.
IPR011009. Kinase-like_dom.
IPR011993. PH_like_dom.
IPR001849. Pleckstrin_homology.
IPR002219. Prot_Kinase_C-like_PE/DAG-bd.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR015727. Protein_Kinase_C_mu-related.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PANTHERPTHR22968. PTHR22968. 1 hit.
PfamPF00130. C1_1. 2 hits.
PF00169. PH. 1 hit.
PF00069. Pkinase. 1 hit.
[Graphical view]
PIRSFPIRSF000552. PKC_mu_nu_D2. 1 hit.
PRINTSPR00008. DAGPEDOMAIN.
SMARTSM00109. C1. 2 hits.
SM00233. PH. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMSSF56112. SSF56112. 1 hit.
PROSITEPS50003. 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.
[Graphical view]
ProtoNetSearch...

Other

NextBio617508.

Entry information

Entry nameKPCD1_RAT
AccessionPrimary (citable) accession number: Q9WTQ1
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: May 20, 2008
Last modified: July 9, 2014
This is version 87 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families