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O00311

- CDC7_HUMAN

UniProt

O00311 - CDC7_HUMAN

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Protein

Cell division cycle 7-related protein kinase

Gene
CDC7, CDC7L1
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Seems to phosphorylate critical substrates that regulate the G1/S phase transition and/or DNA replication. Can phosphorylates MCM2 and MCM3.1 Publication

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Cofactori

Magnesium.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei90 – 901ATP By similarity
Active sitei177 – 1771Proton acceptor By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi64 – 729ATP By similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. kinase activity Source: HGNC
  3. metal ion binding Source: UniProtKB-KW
  4. protein binding Source: IntAct
  5. protein kinase activity Source: UniProt
  6. protein serine/threonine kinase activity Source: UniProtKB-KW

GO - Biological processi

  1. cell cycle phase transition Source: BHF-UCL
  2. cell division Source: UniProtKB-KW
  3. DNA replication Source: Reactome
  4. G1/S transition of mitotic cell cycle Source: Reactome
  5. mitotic cell cycle Source: Reactome
  6. positive regulation of cell proliferation Source: HGNC
  7. positive regulation of G2/M transition of mitotic cell cycle Source: UniProt
  8. positive regulation of nuclear cell cycle DNA replication Source: UniProt
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

Cell cycle, Cell division

Keywords - Ligandi

ATP-binding, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.11.1. 2681.
ReactomeiREACT_1095. Activation of the pre-replicative complex.
REACT_6769. Activation of ATR in response to replication stress.
SignaLinkiO00311.

Names & Taxonomyi

Protein namesi
Recommended name:
Cell division cycle 7-related protein kinase (EC:2.7.11.1)
Short name:
CDC7-related kinase
Short name:
HsCdc7
Short name:
huCdc7
Gene namesi
Name:CDC7
Synonyms:CDC7L1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:1745. CDC7.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: HGNC
  2. intercellular bridge Source: HPA
  3. microtubule cytoskeleton Source: HPA
  4. nucleoplasm Source: Reactome
  5. nucleus Source: HGNC
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA26272.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 574574Cell division cycle 7-related protein kinasePRO_0000085763Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei27 – 271Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiO00311.
PaxDbiO00311.
PRIDEiO00311.

PTM databases

PhosphoSiteiO00311.

Expressioni

Gene expression databases

ArrayExpressiO00311.
BgeeiO00311.
CleanExiHS_CDC7.
GenevestigatoriO00311.

Organism-specific databases

HPAiCAB002669.
HPA035831.

Interactioni

Subunit structurei

Forms a complex with either DBF4/DBF4A or DBF4B, leading to the activation of the kinase activity.

Binary interactionsi

WithEntry#Exp.IntActNotes
MCMBPQ9BTE32EBI-374980,EBI-749378

Protein-protein interaction databases

BioGridi113914. 35 interactions.
DIPiDIP-31728N.
IntActiO00311. 14 interactions.
MINTiMINT-1201209.
STRINGi9606.ENSP00000234626.

Structurei

Secondary structure

1
574
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi42 – 509
Helixi52 – 565
Beta strandi59 – 668
Beta strandi68 – 7912
Beta strandi84 – 929
Helixi98 – 11013
Beta strandi121 – 1266
Beta strandi129 – 1357
Helixi142 – 1465
Helixi151 – 17020
Helixi180 – 1823
Beta strandi183 – 1864
Turni187 – 1904
Beta strandi191 – 1944
Helixi209 – 2135
Turni217 – 2193
Helixi377 – 3793
Helixi382 – 3854
Helixi394 – 40916
Beta strandi412 – 4154
Helixi420 – 43112
Helixi433 – 44210
Beta strandi445 – 4517
Helixi458 – 4658
Helixi540 – 54910
Turni554 – 5563
Helixi560 – 5645
Helixi567 – 5693

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4F99X-ray2.33A37-574[»]
4F9AX-ray2.17A/C37-574[»]
4F9BX-ray2.50A/C37-574[»]
4F9CX-ray2.08A37-574[»]
ProteinModelPortaliO00311.
SMRiO00311. Positions 37-572.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini58 – 574517Protein kinaseAdd
BLAST

Sequence similaritiesi

Phylogenomic databases

eggNOGiNOG250270.
HOGENOMiHOG000193450.
HOVERGENiHBG003991.
InParanoidiO00311.
KOiK02214.
OMAiATDKVCS.
OrthoDBiEOG7VMP6J.
PhylomeDBiO00311.
TreeFamiTF101052.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00069. Pkinase. 2 hits.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 3 hits.
PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

This entry describes 1 isoform i produced by alternative splicing. Align

Note: A number of isoforms may be produced.

Isoform 1 (identifier: O00311-1) [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

MEASLGIQMD EPMAFSPQRD RFQAEGSLKK NEQNFKLAGV KKDIEKLYEA    50
VPQLSNVFKI EDKIGEGTFS SVYLATAQLQ VGPEEKIALK HLIPTSHPIR 100
IAAELQCLTV AGGQDNVMGV KYCFRKNDHV VIAMPYLEHE SFLDILNSLS 150
FQEVREYMLN LFKALKRIHQ FGIVHRDVKP SNFLYNRRLK KYALVDFGLA 200
QGTHDTKIEL LKFVQSEAQQ ERCSQNKSHI ITGNKIPLSG PVPKELDQQS 250
TTKASVKRPY TNAQIQIKQG KDGKEGSVGL SVQRSVFGER NFNIHSSISH 300
ESPAVKLMKQ SKTVDVLSRK LATKKKAIST KVMNSAVMRK TASSCPASLT 350
CDCYATDKVC SICLSRRQQV APRAGTPGFR APEVLTKCPN QTTAIDMWSA 400
GVIFLSLLSG RYPFYKASDD LTALAQIMTI RGSRETIQAA KTFGKSILCS 450
KEVPAQDLRK LCERLRGMDS STPKLTSDIQ GHASHQPAIS EKTDHKASCL 500
VQTPPGQYSG NSFKKGDSNS CEHCFDEYNT NLEGWNEVPD EAYDLLDKLL 550
DLNPASRITA EEALLHPFFK DMSL 574
Length:574
Mass (Da):63,888
Last modified:July 1, 1997 - v1
Checksum:i90D549BEE20AE583
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti23 – 231Q → P.1 Publication
Corresponds to variant rs13447459 [ dbSNP | Ensembl ].
VAR_019255
Natural varianti99 – 991I → V.1 Publication
Corresponds to variant rs13447492 [ dbSNP | Ensembl ].
VAR_019256
Natural varianti112 – 1121G → W.1 Publication
Corresponds to variant rs13447493 [ dbSNP | Ensembl ].
VAR_019257
Natural varianti162 – 1621F → L.2 Publications
Corresponds to variant rs13447503 [ dbSNP | Ensembl ].
VAR_019258
Natural varianti208 – 2081I → M.1 Publication
Corresponds to variant rs34979509 [ dbSNP | Ensembl ].
VAR_040403
Natural varianti209 – 2091E → D.1 Publication
Corresponds to variant rs56327502 [ dbSNP | Ensembl ].
VAR_040404
Natural varianti441 – 4411K → R.2 Publications
Corresponds to variant rs13447539 [ dbSNP | Ensembl ].
VAR_019259
Natural varianti472 – 4721T → I.1 Publication
Corresponds to variant rs56381770 [ dbSNP | Ensembl ].
VAR_040405
Natural varianti498 – 4981S → A.1 Publication
Corresponds to variant rs35055915 [ dbSNP | Ensembl ].
VAR_040406

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti89 – 891L → V in AAB97512. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB003698 mRNA. Translation: BAA19962.1.
AF015592 mRNA. Translation: AAC52080.1.
AF005209 mRNA. Translation: AAB97512.1.
AY585721 Genomic DNA. Translation: AAS79323.1.
AL355871 Genomic DNA. Translation: CAI14446.1.
CH471097 Genomic DNA. Translation: EAW73114.1.
CH471097 Genomic DNA. Translation: EAW73115.1.
BC110526 mRNA. Translation: AAI10527.1.
BC110527 mRNA. Translation: AAI10528.1.
BC111044 mRNA. Translation: AAI11045.1.
CCDSiCCDS734.1. [O00311-1]
RefSeqiNP_001127891.1. NM_001134419.1. [O00311-1]
NP_001127892.1. NM_001134420.1. [O00311-1]
NP_003494.1. NM_003503.3. [O00311-1]
XP_005271298.1. XM_005271241.1. [O00311-1]
UniGeneiHs.533573.

Genome annotation databases

EnsembliENST00000234626; ENSP00000234626; ENSG00000097046. [O00311-1]
ENST00000428239; ENSP00000393139; ENSG00000097046. [O00311-1]
GeneIDi8317.
KEGGihsa:8317.
UCSCiuc001doe.3. human. [O00311-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB003698 mRNA. Translation: BAA19962.1 .
AF015592 mRNA. Translation: AAC52080.1 .
AF005209 mRNA. Translation: AAB97512.1 .
AY585721 Genomic DNA. Translation: AAS79323.1 .
AL355871 Genomic DNA. Translation: CAI14446.1 .
CH471097 Genomic DNA. Translation: EAW73114.1 .
CH471097 Genomic DNA. Translation: EAW73115.1 .
BC110526 mRNA. Translation: AAI10527.1 .
BC110527 mRNA. Translation: AAI10528.1 .
BC111044 mRNA. Translation: AAI11045.1 .
CCDSi CCDS734.1. [O00311-1 ]
RefSeqi NP_001127891.1. NM_001134419.1. [O00311-1 ]
NP_001127892.1. NM_001134420.1. [O00311-1 ]
NP_003494.1. NM_003503.3. [O00311-1 ]
XP_005271298.1. XM_005271241.1. [O00311-1 ]
UniGenei Hs.533573.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
4F99 X-ray 2.33 A 37-574 [» ]
4F9A X-ray 2.17 A/C 37-574 [» ]
4F9B X-ray 2.50 A/C 37-574 [» ]
4F9C X-ray 2.08 A 37-574 [» ]
ProteinModelPortali O00311.
SMRi O00311. Positions 37-572.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 113914. 35 interactions.
DIPi DIP-31728N.
IntActi O00311. 14 interactions.
MINTi MINT-1201209.
STRINGi 9606.ENSP00000234626.

Chemistry

BindingDBi O00311.
ChEMBLi CHEMBL2111377.

PTM databases

PhosphoSitei O00311.

Proteomic databases

MaxQBi O00311.
PaxDbi O00311.
PRIDEi O00311.

Protocols and materials databases

DNASUi 8317.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000234626 ; ENSP00000234626 ; ENSG00000097046 . [O00311-1 ]
ENST00000428239 ; ENSP00000393139 ; ENSG00000097046 . [O00311-1 ]
GeneIDi 8317.
KEGGi hsa:8317.
UCSCi uc001doe.3. human. [O00311-1 ]

Organism-specific databases

CTDi 8317.
GeneCardsi GC01P091966.
HGNCi HGNC:1745. CDC7.
HPAi CAB002669.
HPA035831.
MIMi 603311. gene.
neXtProti NX_O00311.
PharmGKBi PA26272.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG250270.
HOGENOMi HOG000193450.
HOVERGENi HBG003991.
InParanoidi O00311.
KOi K02214.
OMAi ATDKVCS.
OrthoDBi EOG7VMP6J.
PhylomeDBi O00311.
TreeFami TF101052.

Enzyme and pathway databases

BRENDAi 2.7.11.1. 2681.
Reactomei REACT_1095. Activation of the pre-replicative complex.
REACT_6769. Activation of ATR in response to replication stress.
SignaLinki O00311.

Miscellaneous databases

GeneWikii Cell_division_cycle_7-related_protein_kinase.
GenomeRNAii 8317.
NextBioi 31147.
PROi O00311.
SOURCEi Search...

Gene expression databases

ArrayExpressi O00311.
Bgeei O00311.
CleanExi HS_CDC7.
Genevestigatori O00311.

Family and domain databases

InterProi IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view ]
Pfami PF00069. Pkinase. 2 hits.
[Graphical view ]
SUPFAMi SSF56112. SSF56112. 3 hits.
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. "Human and Xenopus cDNAs encoding budding yeast Cdc7-related kinases: in vitro phosphorylation of MCM subunits by a putative human homologue of Cdc7."
    Sato N., Arai K., Masai H.
    EMBO J. 16:4340-4351(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Liver and Testis.
  2. "A human homolog of the yeast CDC7 gene is overexpressed in some tumors and transformed cell lines."
    Hess G.F., Drong R.F., Weiland K.L., Slightom J.L., Sclafani R.A., Hollingsworth R.E.
    Gene 211:133-140(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "Identification and characterization of a human protein kinase related to budding yeast Cdc7p."
    Jiang W., Hunter T.
    Proc. Natl. Acad. Sci. U.S.A. 94:14320-14325(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION.
  4. NIEHS SNPs program
    Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS PRO-23; VAL-99; TRP-112; LEU-162 AND ARG-441.
  5. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "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].
  8. "A novel growth- and cell cycle-regulated protein, ASK, activates human Cdc7-related kinase and is essential for G1/S transition in mammalian cells."
    Kumagai H., Sato N., Yamada M., Mahony D., Seghezzi W., Lees E., Arai K., Masai H.
    Mol. Cell. Biol. 19:5083-5095(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH DBF4.
  9. Cited for: FUNCTION, INTERACTION WITH DBF4B.
  10. "A second human Dbf4/ASK-related protein, Drf1/ASKL1, is required for efficient progression of S and M phases."
    Yoshizawa-Sugata N., Ishii A., Taniyama C., Matsui E., Arai K., Masai H.
    J. Biol. Chem. 280:13062-13070(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH DBF4B.
  11. "Cdc7 is an active kinase in human cancer cells undergoing replication stress."
    Tenca P., Brotherton D., Montagnoli A., Rainoldi S., Albanese C., Santocanale C.
    J. Biol. Chem. 282:208-215(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH DBF4 AND DBF4B.
  12. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-27, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "Patterns of somatic mutation in human cancer genomes."
    Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.
    , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.
    Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS [LARGE SCALE ANALYSIS] LEU-162; MET-208; ASP-209; ARG-441; ILE-472 AND ALA-498.

Entry informationi

Entry nameiCDC7_HUMAN
AccessioniPrimary (citable) accession number: O00311
Secondary accession number(s): D3DT31, O00558, Q5T5U5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 11, 2001
Last sequence update: July 1, 1997
Last modified: September 3, 2014
This is version 146 of the entry and version 1 of the sequence. [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 1
    Human chromosome 1: 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

External Data

Dasty 3

Similar proteinsi