Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

O55173

- PDPK1_RAT

UniProt

O55173 - PDPK1_RAT

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

3-phosphoinositide-dependent protein kinase 1

Gene

Pdpk1

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

Functioni

Serine/threonine kinase which acts as a master kinase, phosphorylating and activating a subgroup of the AGC family of protein kinases. Its targets include: protein kinase B (PKB/AKT1, PKB/AKT2, PKB/AKT3), p70 ribosomal protein S6 kinase (RPS6KB1), p90 ribosomal protein S6 kinase (RPS6KA1, RPS6KA2 and RPS6KA3), cyclic AMP-dependent protein kinase (PRKACA), protein kinase C (PRKCD and PRKCZ), serum and glucocorticoid-inducible kinase (SGK1, SGK2 and SGK3), p21-activated kinase-1 (PAK1), protein kinase PKN (PKN1 and PKN2). Plays a central role in the transduction of signals from insulin by providing the activating phosphorylation to PKB/AKT1, thus propagating the signal to downstream targets controlling cell proliferation and survival, as well as glucose and amino acid uptake and storage. Negatively regulates the TGF-beta-induced signaling by: modulating the association of SMAD3 and SMAD7 with TGF-beta receptor, phosphorylating SMAD2, SMAD3, SMAD4 and SMAD7, preventing the nuclear translocation of SMAD3 and SMAD4 and the translocation of SMAD7 from the nucleus to the cytoplasm in response to TGF-beta. Activates PPARG transcriptional activity and promotes adipocyte differentiation. Activates the NF-kappa-B pathway via phosphorylation of IKKB. The tyrosine phosphorylated form is crucial for the regulation of focal adhesions by angiotensin II. Controls proliferation, survival, and growth of developing pancreatic cells. Participates in the regulation of Ca2+ entry and Ca2+-activated K+ channels of mast cells. Essential for the motility of vascular endothelial cells (ECs) and is involved in the regulation of their chemotaxis. Plays a critical role in cardiac homeostasis by serving as a dual effector for cell survival and beta-adrenergic response. Plays an important role during thymocyte development by regulating the expression of key nutrient receptors on the surface of pre-T cells and mediating Notch-induced cell growth and proliferative responses. Provides negative feedback inhibition to toll-like receptor-mediated NF-kappa-B activation in macrophages (By similarity).By similarity

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Enzyme regulationi

Homodimerization regulates its activity by maintaining the kinase in an autoinhibitory conformation. NPRL2 down-regulates its activity by interfering with tyrosine phosphorylation at the Tyr-9, Tyr-376 and Tyr-379 residues. The 14-3-3 protein YWHAQ acts as a negative regulator by association with the residues surrounding the Ser-244 residue. STRAP positively regulates its activity by enhancing its autophosphorylation and by stimulating its dissociation from YWHAQ. SMAD2, SMAD3, SMAD4 and SMAD7 also positively regulate its activity by stimulating its dissociation from YWHAQ. Activated by phosphorylation on Tyr-9, Tyr-376 and Tyr-379 by INSR in response to insulin (By similarity).By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei114 – 1141ATPPROSITE-ProRule annotation
Active sitei208 – 2081Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi91 – 999ATPPROSITE-ProRule annotation

GO - Molecular functioni

  1. 3-phosphoinositide-dependent protein kinase activity Source: RGD
  2. ATP binding Source: UniProtKB-KW
  3. insulin receptor binding Source: RGD
  4. phospholipase activator activity Source: Ensembl
  5. protein kinase binding Source: RGD

GO - Biological processi

  1. activation of protein kinase B activity Source: Ensembl
  2. calcium-mediated signaling Source: Ensembl
  3. cell migration Source: Ensembl
  4. cellular response to epidermal growth factor stimulus Source: Ensembl
  5. cellular response to insulin stimulus Source: Ensembl
  6. epidermal growth factor receptor signaling pathway Source: Ensembl
  7. extrinsic apoptotic signaling pathway Source: Ensembl
  8. focal adhesion assembly Source: RGD
  9. hyperosmotic response Source: Ensembl
  10. negative regulation of cardiac muscle cell apoptotic process Source: Ensembl
  11. negative regulation of protein kinase activity Source: Ensembl
  12. negative regulation of toll-like receptor signaling pathway Source: Ensembl
  13. negative regulation of transforming growth factor beta receptor signaling pathway Source: Ensembl
  14. peptidyl-threonine phosphorylation Source: Ensembl
  15. positive regulation of establishment of protein localization to plasma membrane Source: Ensembl
  16. positive regulation of phospholipase activity Source: Ensembl
  17. positive regulation of release of sequestered calcium ion into cytosol Source: Ensembl
  18. regulation of endothelial cell migration Source: Ensembl
  19. regulation of I-kappaB kinase/NF-kappaB signaling Source: Ensembl
  20. regulation of mast cell degranulation Source: Ensembl
  21. regulation of transcription, DNA-templated Source: UniProtKB-KW
  22. transcription, DNA-templated Source: UniProtKB-KW
  23. type B pancreatic cell development Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.11.1. 5301.
ReactomeiREACT_196390. RSK activation.
REACT_197531. Role of LAT2/NTAL/LAB on calcium mobilization.
REACT_198729. Constitutive PI3K/AKT Signaling in Cancer.

Names & Taxonomyi

Protein namesi
Recommended name:
3-phosphoinositide-dependent protein kinase 1 (EC:2.7.11.1)
Alternative name(s):
Protein kinase B kinase
Short name:
PkB kinase
Gene namesi
Name:Pdpk1
Synonyms:Pdk1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Chromosome 10

Organism-specific databases

RGDi620307. Pdpk1.

Subcellular locationi

Cytoplasm By similarity. Nucleus By similarity. Cell membrane By similarity; Peripheral membrane protein By similarity. Cell junctionfocal adhesion By similarity
Note: Tyrosine phosphorylation seems to occur only at the cell membrane. Translocates to the cell membrane following insulin stimulation by a mechanism that involves binding to GRB14 and INSR. SRC and HSP90 promote its localization to the cell membrane. Its nuclear localization is dependent on its association with PTPN6 and its phosphorylation at Ser-396. Restricted to the nucleus in neuronal cells while in non-neuronal cells it is found in the cytoplasm. The Ser-244 phosphorylated form is distributed along the perinuclear region in neuronal cells while in non-neuronal cells it is found in both the nucleus and the cytoplasm. IGF1 transiently increases phosphorylation at Ser-244 of neuronal PDPK1, resulting in its translocation to other cellular compartments. The tyrosine-phosphorylated form colocalizes with PTK2B in focal adhesions after angiotensin II stimulation (By similarity).By similarity

GO - Cellular componenti

  1. cell junction Source: UniProtKB-KW
  2. cell projection Source: Ensembl
  3. cytoplasmic membrane-bounded vesicle Source: Ensembl
  4. cytosol Source: RGD
  5. nucleus Source: UniProtKB-KW
  6. plasma membrane Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Cytoplasm, Membrane, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 5595593-phosphoinositide-dependent protein kinase 1PRO_0000086502Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei9 – 91Phosphotyrosine; by SRC and INSRBy similarity
Modified residuei25 – 251PhosphoserineBy similarity
Modified residuei244 – 2441Phosphoserine; by autocatalysisBy similarity
Modified residuei307 – 3071N6-acetyllysineBy similarity
Modified residuei357 – 3571Phosphothreonine; by MELKBy similarity
Modified residuei376 – 3761Phosphotyrosine; by SRC and INSRBy similarity
Modified residuei379 – 3791Phosphotyrosine; by SRC and INSRBy similarity
Modified residuei396 – 3961PhosphoserineBy similarity
Modified residuei397 – 3971Phosphoserine; by MAP3K5By similarity
Modified residuei399 – 3991PhosphoserineBy similarity
Modified residuei401 – 4011Phosphoserine; by MAP3K5By similarity
Modified residuei413 – 4131PhosphoserineBy similarity
Modified residuei504 – 5041Phosphoserine; by PKC/PRKCQBy similarity
Modified residuei516 – 5161Phosphothreonine; by autocatalysisBy similarity
Modified residuei532 – 5321Phosphoserine; by PKC/PRKCQBy similarity

Post-translational modificationi

Phosphorylation on Ser-244 in the activation loop is required for full activity. PDPK1 itself can autophosphorylate Ser-244, leading to its own activation. Autophosphorylation is inhibited by the apoptotic C-terminus cleavage product of PKN2. Tyr-9 phosphorylation is critical for stabilization of both PDPK1 and the PDPK1/SRC complex via HSP90-mediated protection of PDPK1 degradation. Angiotensin II stimulates the tyrosine phosphorylation of PDPK1 in vascular smooth muscle in a calcium- and SRC-dependent manner. Phosphorylated on Tyr-9, Tyr-376 and Tyr-379 by INSR in response to insulin. Palmitate negatively regulates autophosphorylation at Ser-244 and palmitate-induced phosphorylation at Ser-532 and Ser-504 by PKC/PRKCQ negatively regulates its ability to phosphorylate PKB/AKT1. Phosphorylation at Thr-357 by MELK partially inhibits kinase activity, the inhibition is cooperatively enhanced by phosphorylation at Ser-397 and Ser-401 by MAP3K5 (By similarity).By similarity
Monoubiquitinated in the kinase domain, deubiquitinated by USP4.By similarity

Keywords - PTMi

Acetylation, Phosphoprotein, Ubl conjugation

Proteomic databases

PRIDEiO55173.

PTM databases

PhosphoSiteiO55173.

Expressioni

Gene expression databases

GenevestigatoriO55173.

Interactioni

Subunit structurei

Homodimer in its autoinhibited state. Active as monomer. Interacts with NPRL2, PPARG, PAK1, PTK2B, GRB14, PKN1 (via C-terminus), STRAP and IKKB. The Tyr-9 phosphorylated form interacts with SRC, RASA1 and CRK (via their SH2 domains). Interacts with SGK3 in a phosphorylation-dependent manner. The tyrosine-phosphorylated form interacts with PTPN6. The Ser-244 phosphorylated form interacts with YWHAH and YWHAQ. Binds INSR in response to insulin. Interacts (via PH domain) with SMAD3, SMAD4 and SMAD7 (By similarity). Interacts with PKN2; the interaction stimulates PDPK1 autophosphorylation, its PI(3,4,5)P3-dependent kinase activity toward 'Ser-473' of AKT1 but also activates its kinase activity toward PRKCD and PRKCZ.By similarity1 Publication

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000008434.

Structurei

3D structure databases

ProteinModelPortaliO55173.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini85 – 345261Protein kinasePROSITE-ProRule annotationAdd
BLAST
Domaini462 – 55392PHAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi392 – 3998Poly-Ser

Domaini

The PH domain plays a pivotal role in the localization and nuclear import of PDPK1 and is also essential for its homodimerization.By similarity

Sequence similaritiesi

Contains 1 PH domain.Curated
Contains 1 protein kinase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00550000074819.
HOGENOMiHOG000233026.
HOVERGENiHBG098357.
InParanoidiO55173.
KOiK06276.
OMAiSEDMHIQ.
OrthoDBiEOG7R56S4.
TreeFamiTF105423.

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.

O55173-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MARTTSQLYD AVPIQSSVVL CSCPSPSMVR SQTEPSSSPG IPSGVSRQGS
60 70 80 90 100
TMDGTTAEAR PSTNPLQQHP AQLPPQPRKK RPEDFKFGKI LGEGSFSTVV
110 120 130 140 150
LARELATSRE YAIKILEKRH IIKENKVPYV TRERDVMSRL DHPFFVKLYF
160 170 180 190 200
TFQDDEKLYF GLSYAKNGEL LKYIRKIGSF DETCTRFYTA EIVSALEYLH
210 220 230 240 250
GKGIIHRDLK PENILLNEDM HIQITDFGTA KVLSPDSKQA RANSFVGTAQ
260 270 280 290 300
YVSPELLTEK SACKSSDLWA LGCIIYQLVA GLPPFRAGNE YLIFQKIIKL
310 320 330 340 350
EYDFPEKFFP KARDLVEKLL VLDATKRLGC EEMEGYGPLK AHPFFESITW
360 370 380 390 400
ENLHQQTPPK LTAYLPAMSE DDEDCYGNYD NLLSQFGCMQ VSSSSSSHSL
410 420 430 440 450
SAVDASLPQR SGSNIEQYIH DLDTNSFELD LQFSEDEKRL LLEKQAGGNP
460 470 480 490 500
WHQFVENNLI LKMGPVDKRK GLFARRRQLL LTEGPHLYYV DPVNKVLKGE
510 520 530 540 550
IPWSQELRPE AKNFKTFFVH TPNRTYYLMD PSGNAHKWCR KIQEVWRQQY

QSSPDAAVQ
Length:559
Mass (Da):63,593
Last modified:July 11, 2012 - v2
Checksum:i4D06A17F769B800F
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti401 – 4011S → C in CAA75758. (PubMed:9445477)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Y15748 mRNA. Translation: CAA75758.1.
CH473948 Genomic DNA. Translation: EDM03805.1.
RefSeqiNP_112343.1. NM_031081.1.
UniGeneiRn.10905.

Genome annotation databases

EnsembliENSRNOT00000067660; ENSRNOP00000061683; ENSRNOG00000006136.
GeneIDi81745.
KEGGirno:81745.
UCSCiRGD:620307. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Y15748 mRNA. Translation: CAA75758.1 .
CH473948 Genomic DNA. Translation: EDM03805.1 .
RefSeqi NP_112343.1. NM_031081.1.
UniGenei Rn.10905.

3D structure databases

ProteinModelPortali O55173.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 10116.ENSRNOP00000008434.

PTM databases

PhosphoSitei O55173.

Proteomic databases

PRIDEi O55173.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSRNOT00000067660 ; ENSRNOP00000061683 ; ENSRNOG00000006136 .
GeneIDi 81745.
KEGGi rno:81745.
UCSCi RGD:620307. rat.

Organism-specific databases

CTDi 5170.
RGDi 620307. Pdpk1.

Phylogenomic databases

eggNOGi COG0515.
GeneTreei ENSGT00550000074819.
HOGENOMi HOG000233026.
HOVERGENi HBG098357.
InParanoidi O55173.
KOi K06276.
OMAi SEDMHIQ.
OrthoDBi EOG7R56S4.
TreeFami TF105423.

Enzyme and pathway databases

BRENDAi 2.7.11.1. 5301.
Reactomei REACT_196390. RSK activation.
REACT_197531. Role of LAT2/NTAL/LAB on calcium mobilization.
REACT_198729. Constitutive PI3K/AKT Signaling in Cancer.

Miscellaneous databases

NextBioi 615478.
PROi O55173.

Gene expression databases

Genevestigatori O55173.

Family and domain databases

Gene3Di 2.30.29.30. 2 hits.
InterProi IPR011009. 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 ]
Pfami PF00069. Pkinase. 1 hit.
[Graphical view ]
SMARTi SM00220. S_TKc. 1 hit.
[Graphical view ]
SUPFAMi SSF56112. SSF56112. 1 hit.
PROSITEi PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Protein kinase B kinases that mediate phosphatidylinositol 3,4,5-trisphosphate-dependent activation of protein kinase B."
    Stephens L.R., Anderson K.E., Stokoe D., Erdjument-Bromage H., Painter G.F., Holmes A.B., Gaffney P.R.J., Reese C.B., McCormick F., Tempst P., Coadwell W.J., Hawkins P.T.
    Science 279:710-714(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Brain.
  2. "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.
    , 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.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Brown Norway.
  4. "Regulation of both PDK1 and the phosphorylation of PKC-zeta and -delta by a C-terminal PRK2 fragment."
    Hodgkinson C.P., Sale G.J.
    Biochemistry 41:561-569(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF PRKCD AND PRKCZ, AUTOPHOSPHORYLATION, INTERACTION WITH PRKCD AND PRKCZ.

Entry informationi

Entry nameiPDPK1_RAT
AccessioniPrimary (citable) accession number: O55173
Secondary accession number(s): G3V9W3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 18, 2001
Last sequence update: July 11, 2012
Last modified: October 29, 2014
This is version 118 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3