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P63319

- KPCG_RAT

UniProt

P63319 - KPCG_RAT

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Protein

Protein kinase C gamma type

Gene

Prkcg

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Calcium-activated, phospholipid- and diacylglycerol (DAG)-dependent serine/threonine-protein kinase that plays diverse roles in neuronal cells and eye tissues, such as regulation of the neuronal receptors GRIA4/GLUR4 and GRIN1/NMDAR1, modulation of receptors and neuronal functions related to sensitivity to opiates, pain and alcohol, mediation of synaptic function and cell survival after ischemia, and inhibition of gap junction activity after oxidative stress. Binds and phosphorylates GRIA4/GLUR4 glutamate receptor and regulates its function by increasing plasma membrane-associated GRIA4 expression. In primary cerebellar neurons treated with the agonist 3,5-dihyidroxyphenylglycine, functions downstream of the metabotropic glutamate receptor GRM5/MGLUR5 and phosphorylates GRIN1/NMDAR1 receptor which plays a key role in synaptic plasticity, synaptogenesis, excitotoxicity, memory acquisition and learning. May be involved in the regulation of hippocampal long-term potentiation (LTP), but may be not necessary for the process of synaptic plasticity. May be involved in desensitization of mu-type opioid receptor-mediated G-protein activation in the spinal cord, and may be critical for the development and/or maintenance of morphine-induced reinforcing effects in the limbic forebrain. May modulate the functionality of mu-type-opioid receptors by participating in a signaling pathway which leads to the phosphorylation and degradation of opioid receptors. May also contributes to chronic morphine-induced changes in nociceptive processing. Plays a role in neuropathic pain mechanisms and contributes to the maintenance of the allodynia pain produced by peripheral inflammation. Plays an important role in initial sensitivity and tolerance to ethanol, by mediating the behavioral effects of ethanol as well as the effects of this drug on the GABA(A) receptors. During and after cerebral ischemia modulate neurotransmission and cell survival in synaptic membranes, and is involved in insulin-induced inhibition of necrosis, an important mechanism for minimizing ischemic injury. Required for the elimination of multiple climbing fibers during innervation of Purkinje cells in developing cerebellum. Is activated in lens epithelial cells upon hydrogen peroxide treatment, and phosphorylates connexin-43 (GJA1/CX43), resulting in disassembly of GJA1 gap junction plaques and inhibition of gap junction activity which could provide a protective effect against oxidative stress. Phosphorylates p53/TP53 and promotes p53/TP53-dependent apoptosis in response to DNA damage (By similarity).By similarity

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Cofactori

Binds 3 calcium ions per subunit. The ions are bound to the C2 domain (By similarity).By similarity

Enzyme regulationi

Classical (or conventional) PKCs (PRKCA, PRKCB and PRKCG) are activated by calcium and diacylglycerol (DAG) in the presence of phosphatidylserine. Three specific sites; Thr-514 (activation loop of the kinase domain), Thr-655 (turn motif) and Thr-674 (hydrophobic region), need to be phosphorylated for its full activation.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi186 – 1861Calcium 1; via carbonyl oxygenBy similarity
Metal bindingi187 – 1871Calcium 1By similarity
Metal bindingi187 – 1871Calcium 2By similarity
Metal bindingi193 – 1931Calcium 2By similarity
Metal bindingi246 – 2461Calcium 1By similarity
Metal bindingi246 – 2461Calcium 2By similarity
Metal bindingi247 – 2471Calcium 2; via carbonyl oxygenBy similarity
Metal bindingi248 – 2481Calcium 1By similarity
Metal bindingi248 – 2481Calcium 2By similarity
Metal bindingi248 – 2481Calcium 3By similarity
Metal bindingi251 – 2511Calcium 3By similarity
Metal bindingi252 – 2521Calcium 3; via carbonyl oxygenBy similarity
Metal bindingi254 – 2541Calcium 1By similarity
Metal bindingi254 – 2541Calcium 3By similarity
Binding sitei380 – 3801ATPPROSITE-ProRule annotation
Active sitei480 – 4801Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri35 – 8551Phorbol-ester/DAG-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri100 – 15051Phorbol-ester/DAG-type 2PROSITE-ProRule annotationAdd
BLAST
Nucleotide bindingi357 – 3659ATPPROSITE-ProRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. calcium-dependent protein kinase C activity Source: RGD
  3. protein kinase C activity Source: RGD
  4. protein serine/threonine/tyrosine kinase activity Source: Ensembl
  5. zinc ion binding Source: InterPro

GO - Biological processi

  1. chemosensory behavior Source: Ensembl
  2. innervation Source: Ensembl
  3. intracellular signal transduction Source: RGD
  4. learning or memory Source: RGD
  5. negative regulation of neuron apoptotic process Source: UniProtKB
  6. negative regulation of protein catabolic process Source: Ensembl
  7. negative regulation of protein ubiquitination Source: Ensembl
  8. positive regulation of mismatch repair Source: Ensembl
  9. protein autophosphorylation Source: RGD
  10. response to morphine Source: UniProtKB
  11. response to pain Source: UniProtKB
  12. response to stress Source: UniProtKB
  13. synaptic transmission Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Ligandi

ATP-binding, Calcium, Metal-binding, Nucleotide-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_198398. WNT5A-dependent internalization of FZD4.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein kinase C gamma type (EC:2.7.11.13)
Short name:
PKC-gamma
Gene namesi
Name:Prkcg
Synonyms:Pkcc, Pkcg, Prkcc
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Chromosome 1

Organism-specific databases

RGDi3397. Prkcg.

Subcellular locationi

GO - Cellular componenti

  1. cell-cell junction Source: Ensembl
  2. cytosol Source: UniProtKB
  3. dendrite Source: UniProtKB
  4. neuron projection Source: RGD
  5. nucleus Source: Ensembl
  6. perinuclear region of cytoplasm Source: UniProtKB
  7. plasma membrane Source: UniProtKB
  8. synaptic membrane Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Cell projection, Cytoplasm, Membrane, Synapse, Synaptosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 697697Protein kinase C gamma typePRO_0000055692Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei250 – 2501Phosphothreonine; by autocatalysisBy similarity
Modified residuei514 – 5141Phosphothreonine; by PDPK1By similarity
Modified residuei648 – 6481Phosphothreonine; by autocatalysisBy similarity
Modified residuei655 – 6551Phosphothreonine; by autocatalysisSequence Analysis
Modified residuei674 – 6741Phosphothreonine; by autocatalysisBy similarity
Modified residuei675 – 6751Phosphotyrosine; by SYKBy similarity

Post-translational modificationi

Autophosphorylation on Thr-674 appears to regulate motor functions of junctophilins, JPH3 and JPH4.By similarity
Ubiquitinated.By similarity

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiP63319.
PRIDEiP63319.

PTM databases

PhosphoSiteiP63319.

Expressioni

Gene expression databases

GenevestigatoriP63319.

Interactioni

Subunit structurei

Interacts with CDCP1 (By similarity). Interacts with GRIA4. Interacts with TP53INP1 and p53/TP53 (By similarity).By similarity

Protein-protein interaction databases

BioGridi246813. 18 interactions.
STRINGi10116.ENSRNOP00000019825.

Structurei

Secondary structure

1
697
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi103 – 1053Combined sources
Beta strandi108 – 1103Combined sources
Beta strandi115 – 1173Combined sources
Beta strandi125 – 1273Combined sources
Beta strandi129 – 1313Combined sources
Turni132 – 1343Combined sources
Turni140 – 1456Combined sources

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1TBNNMR-A91-172[»]
1TBONMR-A91-172[»]
ProteinModelPortaliP63319.
SMRiP63319. Positions 36-683.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP63319.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini170 – 26091C2PROSITE-ProRule annotationAdd
BLAST
Domaini351 – 614264Protein kinasePROSITE-ProRule annotationAdd
BLAST
Domaini615 – 68571AGC-kinase C-terminalAdd
BLAST

Sequence similaritiesi

Contains 1 AGC-kinase C-terminal domain.Curated
Contains 1 C2 domain.PROSITE-ProRule annotation
Contains 2 phorbol-ester/DAG-type zinc fingers.PROSITE-ProRule annotation
Contains 1 protein kinase domain.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri35 – 8551Phorbol-ester/DAG-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri100 – 15051Phorbol-ester/DAG-type 2PROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00760000118891.
HOGENOMiHOG000233022.
HOVERGENiHBG108317.
InParanoidiP63319.
KOiK02677.
OMAiAIRAHGF.
OrthoDBiEOG77M8QM.
PhylomeDBiP63319.
TreeFamiTF351133.

Family and domain databases

Gene3Di2.60.40.150. 1 hit.
InterProiIPR000961. AGC-kinase_C.
IPR000008. C2_dom.
IPR020454. DAG/PE-bd.
IPR011009. Kinase-like_dom.
IPR002219. PE/DAG-bd.
IPR017892. Pkinase_C.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR014375. Protein_kinase_C_a/b/g.
IPR002290. Ser/Thr_dual-sp_kinase.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00130. C1_1. 2 hits.
PF00168. C2. 1 hit.
PF00069. Pkinase. 1 hit.
PF00433. Pkinase_C. 1 hit.
[Graphical view]
PIRSFiPIRSF000550. PKC_alpha. 1 hit.
PRINTSiPR00360. C2DOMAIN.
PR00008. DAGPEDOMAIN.
SMARTiSM00109. C1. 2 hits.
SM00239. C2. 1 hit.
SM00133. S_TK_X. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF49562. SSF49562. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEiPS51285. AGC_KINASE_CTER. 1 hit.
PS50004. C2. 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]

Sequencei

Sequence statusi: Complete.

P63319-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAGLGPGGGD SEGGPRPLFC RKGALRQKVV HEVKSHKFTA RFFKQPTFCS
60 70 80 90 100
HCTDFIWGIG KQGLQCQVCS FVVHRRCHEF VTFECPGAGK GPQTDDPRNK
110 120 130 140 150
HKFRLHSYSS PTFCDHCGSL LYGLVHQGMK CSCCEMNVHR RCVRSVPSLC
160 170 180 190 200
GVDHTERRGR LQLEIRAPTS DEIHITVGEA RNLIPMDPNG LSDPYVKLKL
210 220 230 240 250
IPDPRNLTKQ KTKTVKATLN PVWNETFVFN LKPGDVERRL SVEVWDWDRT
260 270 280 290 300
SRNDFMGAMS FGVSELLKAP VDGWYKLLNQ EEGEYYNVPV ADADNCSLLQ
310 320 330 340 350
KFEACNYPLE LYERVRMGPS SSPIPSPSPS PTDSKRCFFG ASPGRLHISD
360 370 380 390 400
FSFLMVLGKG SFGKVMLAER RGSDELYAIK ILKKDVIVQD DDVDCTLVEK
410 420 430 440 450
RVLALGGRGP GGRPHFLTQL HSTFQTPDRL YFVMEYVTGG DLMYHIQQLG
460 470 480 490 500
KFKEPHAAFY AAEIAIGLFF LHNQGIIYRD LKLDNVMLDA EGHIKITDFG
510 520 530 540 550
MCKENVFPGS TTRTFCGTPD YIAPEIIAYQ PYGKSVDWWS FGVLLYEMLA
560 570 580 590 600
GQPPFDGEDE EELFQAIMEQ TVTYPKSLSR EAVAICKGFL TKHPGKRLGS
610 620 630 640 650
GPDGEPTIRA HGFFRWIDWE RLERLEIAPP FRPRPCGRSG ENFDKFFTRA
660 670 680 690
APALTPPDRL VLASIDQADF QGFTYVNPDF VHPDARSPTS PVPVPVM
Length:697
Mass (Da):78,358
Last modified:October 11, 2004 - v1
Checksum:iE6E2F7A3B93042FF
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X07287 mRNA. Translation: CAA30267.1.
M13707 mRNA. Translation: AAA41874.1.
BC089226 mRNA. Translation: AAH89226.1.
M55417 Genomic DNA. Translation: AAA41873.1.
PIRiA05105. KIRTGC.
RefSeqiNP_036760.1. NM_012628.1.
UniGeneiRn.9747.

Genome annotation databases

EnsembliENSRNOT00000019825; ENSRNOP00000019825; ENSRNOG00000014688.
GeneIDi24681.
KEGGirno:24681.
UCSCiRGD:3397. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X07287 mRNA. Translation: CAA30267.1 .
M13707 mRNA. Translation: AAA41874.1 .
BC089226 mRNA. Translation: AAH89226.1 .
M55417 Genomic DNA. Translation: AAA41873.1 .
PIRi A05105. KIRTGC.
RefSeqi NP_036760.1. NM_012628.1.
UniGenei Rn.9747.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1TBN NMR - A 91-172 [» ]
1TBO NMR - A 91-172 [» ]
ProteinModelPortali P63319.
SMRi P63319. Positions 36-683.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 246813. 18 interactions.
STRINGi 10116.ENSRNOP00000019825.

Chemistry

BindingDBi P63319.
ChEMBLi CHEMBL2094266.

PTM databases

PhosphoSitei P63319.

Proteomic databases

PaxDbi P63319.
PRIDEi P63319.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSRNOT00000019825 ; ENSRNOP00000019825 ; ENSRNOG00000014688 .
GeneIDi 24681.
KEGGi rno:24681.
UCSCi RGD:3397. rat.

Organism-specific databases

CTDi 5582.
RGDi 3397. Prkcg.

Phylogenomic databases

eggNOGi COG0515.
GeneTreei ENSGT00760000118891.
HOGENOMi HOG000233022.
HOVERGENi HBG108317.
InParanoidi P63319.
KOi K02677.
OMAi AIRAHGF.
OrthoDBi EOG77M8QM.
PhylomeDBi P63319.
TreeFami TF351133.

Enzyme and pathway databases

Reactomei REACT_198398. WNT5A-dependent internalization of FZD4.

Miscellaneous databases

EvolutionaryTracei P63319.
NextBioi 294925.
PROi P63319.

Gene expression databases

Genevestigatori P63319.

Family and domain databases

Gene3Di 2.60.40.150. 1 hit.
InterProi IPR000961. AGC-kinase_C.
IPR000008. C2_dom.
IPR020454. DAG/PE-bd.
IPR011009. Kinase-like_dom.
IPR002219. PE/DAG-bd.
IPR017892. Pkinase_C.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR014375. Protein_kinase_C_a/b/g.
IPR002290. Ser/Thr_dual-sp_kinase.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view ]
Pfami PF00130. C1_1. 2 hits.
PF00168. C2. 1 hit.
PF00069. Pkinase. 1 hit.
PF00433. Pkinase_C. 1 hit.
[Graphical view ]
PIRSFi PIRSF000550. PKC_alpha. 1 hit.
PRINTSi PR00360. C2DOMAIN.
PR00008. DAGPEDOMAIN.
SMARTi SM00109. C1. 2 hits.
SM00239. C2. 1 hit.
SM00133. S_TK_X. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view ]
SUPFAMi SSF49562. SSF49562. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEi PS51285. AGC_KINASE_CTER. 1 hit.
PS50004. C2. 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 ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Nucleotide sequences of cDNAs for alpha and gamma subspecies of rat brain protein kinase C."
    Ono Y., Fujii T., Igarashi K., Kikkawa U., Ogita K., Nishizuka Y.
    Nucleic Acids Res. 16:5199-5200(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Brain.
  2. "Cloning and expression of multiple protein kinase C cDNAs."
    Knopf J.L., Lee M.-H., Sultzman L.A., Kriz R.W., Loomis C.R., Hewick R.M., Bell R.M.
    Cell 46:491-502(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain.
  4. "Characterization of the 5'-flanking region of the rat protein kinase C gamma gene."
    Chen K.H., Widen S.G., Wilson S.H., Huang K.P.
    J. Biol. Chem. 265:19961-19965(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-56.
  5. "Exposure to chronic psychosocial stress and corticosterone in the rat: effects on spatial discrimination learning and hippocampal protein kinase Cgamma immunoreactivity."
    Krugers H.J., Douma B.R., Andringa G., Bohus B., Korf J., Luiten P.G.
    Hippocampus 7:427-436(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  6. "Inflammation-induced up-regulation of protein kinase Cgamma immunoreactivity in rat spinal cord correlates with enhanced nociceptive processing."
    Martin W.J., Liu H., Wang H., Malmberg A.B., Basbaum A.I.
    Neuroscience 88:1267-1274(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN INFLAMMATORY PAIN.
  7. "Protein kinase C gamma associates directly with the GluR4 alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionate receptor subunit. Effect on receptor phosphorylation."
    Correia S.S., Duarte C.B., Faro C.J., Pires E.V., Carvalho A.L.
    J. Biol. Chem. 278:6307-6313(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF GRIA4/GLUR4, INTERACTION WITH GRIA4/GLUR4, SUBCELLULAR LOCATION.
  8. "Protein kinase C-gamma and calcium/calmodulin-dependent protein kinase II-alpha are persistently translocated to cell membranes of the rat brain during and after middle cerebral artery occlusion."
    Matsumoto S., Shamloo M., Matsumoto E., Isshiki A., Wieloch T.
    J. Cereb. Blood Flow Metab. 24:54-61(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  9. "Serines 890 and 896 of the NMDA receptor subunit NR1 are differentially phosphorylated by protein kinase C isoforms."
    Sanchez-Perez A.M., Felipo V.
    Neurochem. Int. 47:84-91(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF GRIN1/NMDAR1.
  10. "Insulin receptor-protein kinase C-gamma signaling mediates inhibition of hypoxia-induced necrosis of cortical neurons."
    Hamabe W., Fujita R., Ueda H.
    J. Pharmacol. Exp. Ther. 313:1027-1034(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN CELL SURVIVAL.
  11. "NMR structure of a protein kinase C-gamma phorbol-binding domain and study of protein-lipid micelle interactions."
    Xu R.X., Pawelczyk T., Xia T.-H., Brown S.C.
    Biochemistry 36:10709-10717(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 91-172 IN COMPLEX WITH PHORBOL-12,13-DIBUTYRATE, FUNCTION, SUBCELLULAR LOCATION.

Entry informationi

Entry nameiKPCG_RAT
AccessioniPrimary (citable) accession number: P63319
Secondary accession number(s): P05697, Q5FWS3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 11, 2004
Last sequence update: October 11, 2004
Last modified: October 29, 2014
This is version 107 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3