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O75909

- CCNK_HUMAN

UniProt

O75909 - CCNK_HUMAN

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Protein

Cyclin-K

Gene

CCNK

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

Functioni

Regulatory subunit of cyclin-dependent kinases that mediates activation of target kinases. Plays a role in transcriptional regulation via its role in regulating the phosphorylation of the C-terminal domain (CTD) of the large subunit of RNA polymerase II (POLR2A).3 Publications

GO - Molecular functioni

  1. cyclin-dependent protein serine/threonine kinase activity Source: MGI
  2. protein kinase binding Source: MGI
  3. RNA polymerase II carboxy-terminal domain kinase activity Source: MGI

GO - Biological processi

  1. cellular response to DNA damage stimulus Source: MGI
  2. in utero embryonic development Source: Ensembl
  3. mitotic nuclear division Source: UniProtKB-KW
  4. negative regulation of cell cycle arrest Source: MGI
  5. protein phosphorylation Source: GOC
  6. regulation of cyclin-dependent protein serine/threonine kinase activity Source: ProtInc
  7. regulation of transcription, DNA-templated Source: UniProtKB-KW
  8. transcription from RNA polymerase II promoter Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

Cyclin

Keywords - Biological processi

Cell cycle, Cell division, Mitosis, Transcription, Transcription regulation

Enzyme and pathway databases

SignaLinkiO75909.

Names & Taxonomyi

Protein namesi
Recommended name:
Cyclin-K
Gene namesi
Name:CCNK
Synonyms:CPR4
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 14

Organism-specific databases

HGNCiHGNC:1596. CCNK.

Subcellular locationi

Nucleus 1 Publication

GO - Cellular componenti

  1. cyclin K-CDK12 complex Source: MGI
  2. cyclin K-CDK13 complex Source: MGI
  3. nucleus Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA26161.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 580580Cyclin-KPRO_0000080478Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei324 – 3241Phosphoserine4 Publications
Modified residuei329 – 3291Phosphoserine1 Publication
Modified residuei340 – 3401Phosphoserine5 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiO75909.
PaxDbiO75909.
PRIDEiO75909.

PTM databases

PhosphoSiteiO75909.

Expressioni

Tissue specificityi

Ubiquitously expressed. Highest levels in testis.1 Publication

Gene expression databases

BgeeiO75909.
CleanExiHS_CCNK.
ExpressionAtlasiO75909. baseline and differential.
GenevestigatoriO75909.

Organism-specific databases

HPAiHPA000645.

Interactioni

Subunit structurei

Regulatory subunit of cyclin-dependent kinases. Identified in a complex with a kinase and the RNA polymerase II holoenzyme. Interacts with POLR2A. Interacts with CDK12 and CDK13. Interacts with CDK9 according to PubMed:10574912; does not interact with CDK9 according to PubMed:22012619.4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ATXN1P542532EBI-739806,EBI-930964

Protein-protein interaction databases

BioGridi114339. 29 interactions.
IntActiO75909. 16 interactions.
MINTiMINT-1437641.
STRINGi9606.ENSP00000374529.

Structurei

Secondary structure

1
580
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi21 – 233
Helixi28 – 336
Helixi35 – 384
Helixi43 – 6321
Helixi68 – 8114
Turni82 – 843
Turni87 – 893
Helixi92 – 10615
Helixi113 – 12311
Helixi126 – 1294
Helixi130 – 1323
Helixi136 – 15015
Turni151 – 1533
Helixi160 – 16910
Helixi175 – 19218
Turni193 – 1964
Helixi197 – 1993
Helixi203 – 21816
Helixi222 – 2254
Beta strandi226 – 2283
Helixi234 – 2374
Beta strandi239 – 2413
Helixi244 – 25512
Turni256 – 2583
Beta strandi259 – 2613

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2I53X-ray1.50A11-267[»]
4CXAX-ray3.15B/D11-267[»]
4NSTX-ray2.20B/D1-267[»]
4UN0X-ray3.15A/B11-267[»]
ProteinModelPortaliO75909.
SMRiO75909. Positions 14-267.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO75909.

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi312 – 3154Poly-Gln

Sequence similaritiesi

Belongs to the cyclin family. Cyclin C subfamily.Curated

Phylogenomic databases

eggNOGiCOG5333.
GeneTreeiENSGT00760000119191.
HOGENOMiHOG000220828.
HOVERGENiHBG050836.
InParanoidiO75909.
OMAiKIETSHP.
OrthoDBiEOG7VQJCR.
TreeFamiTF101010.

Family and domain databases

Gene3Di1.10.472.10. 1 hit.
InterProiIPR013763. Cyclin-like.
IPR015429. Cyclin_C/H/T/L.
IPR006671. Cyclin_N.
[Graphical view]
PANTHERiPTHR10026. PTHR10026. 1 hit.
PfamiPF00134. Cyclin_N. 1 hit.
[Graphical view]
SMARTiSM00385. CYCLIN. 2 hits.
[Graphical view]
SUPFAMiSSF47954. SSF47954. 2 hits.

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: O75909-3) [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
MKENKENSSP SVTSANLDHT KPCWYWDKKD LAHTPSQLEG LDPATEARYR
60 70 80 90 100
REGARFIFDV GTRLGLHYDT LATGIIYFHR FYMFHSFKQF PRYVTGACCL
110 120 130 140 150
FLAGKVEETP KKCKDIIKTA RSLLNDVQFG QFGDDPKEEV MVLERILLQT
160 170 180 190 200
IKFDLQVEHP YQFLLKYAKQ LKGDKNKIQK LVQMAWTFVN DSLCTTLSLQ
210 220 230 240 250
WEPEIIAVAV MYLAGRLCKF EIQEWTSKPM YRRWWEQFVQ DVPVDVLEDI
260 270 280 290 300
CHQILDLYSQ GKQQMPHHTP HQLQQPPSLQ PTPQVPQVQQ SQPSQSSEPS
310 320 330 340 350
QPQQKDPQQP AQQQQPAQQP KKPSPQPSSP RQVKRAVVVS PKEENKAAEP
360 370 380 390 400
PPPKIPKIET THPPLPPAHP PPDRKPPLAA ALGEAEPPGP VDATDLPKVQ
410 420 430 440 450
IPPPAHPAPV HQPPPLPHRP PPPPPSSYMT GMSTTSSYMS GEGYQSLQSM
460 470 480 490 500
MKTEGPSYGA LPPAYGPPAH LPYHPHVYPP NPPPPPVPPP PASFPPPAIP
510 520 530 540 550
PPTPGYPPPP PTYNPNFPPP PPRLPPTHAV PPHPPPGLGL PPASYPPPAV
560 570 580
PPGGQPPVPP PIPPPGMPPV GGLGRAAWMR
Length:580
Mass (Da):64,240
Last modified:December 16, 2008 - v2
Checksum:i8A945E90359AD9F8
GO
Isoform 2 (identifier: O75909-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     308-354: QQPAQQQQPA...NKAAEPPPPK → LILLQGWACR...QLGGWGGQPG
     355-580: Missing.

Show »
Length:354
Mass (Da):40,788
Checksum:i39D8F18FC9429207
GO
Isoform 3 (identifier: O75909-1) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     351-357: PPPKIPK → APSQHLW
     358-580: Missing.

Show »
Length:357
Mass (Da):41,293
Checksum:iFA7DD89035A66105
GO
Isoform 4 (identifier: O75909-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     338-338: V → VSGLKQALGRAGFPGGGNTQV

Show »
Length:600
Mass (Da):66,137
Checksum:iA79E4E8B190E7199
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti191 – 1911D → T in BAD92610. 1 PublicationCurated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei308 – 35447QQPAQ…PPPPK → LILLQGWACRQPATHLLPSP LEDSLLCPRPFPHPACLQLG GWGGQPG in isoform 2. 2 PublicationsVSP_010830Add
BLAST
Alternative sequencei338 – 3381V → VSGLKQALGRAGFPGGGNTQ V in isoform 4. 2 PublicationsVSP_035970
Alternative sequencei351 – 3577PPPKIPK → APSQHLW in isoform 3. 1 PublicationVSP_035971
Alternative sequencei355 – 580226Missing in isoform 2. 2 PublicationsVSP_035972Add
BLAST
Alternative sequencei358 – 580223Missing in isoform 3. 1 PublicationVSP_035973Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF060515 mRNA. Translation: AAD09978.1.
BT006950 mRNA. Translation: AAP35596.1.
AF542236 Genomic DNA. Translation: AAN06829.1.
AL110504 Genomic DNA. No translation available.
BC015935 mRNA. Translation: AAH15935.1.
AH009612 Genomic DNA. Translation: AAF82290.1.
BX247958 mRNA. Translation: CAD62298.1.
AB209373 Transcribed RNA. Translation: BAD92610.1.
CCDSiCCDS45160.1. [O75909-3]
RefSeqiNP_001092872.1. NM_001099402.1. [O75909-3]
XP_005268211.1. XM_005268154.2. [O75909-3]
UniGeneiHs.510409.

Genome annotation databases

EnsembliENST00000389879; ENSP00000374529; ENSG00000090061. [O75909-3]
GeneIDi8812.
KEGGihsa:8812.
UCSCiuc001ygi.4. human. [O75909-3]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Web resourcesi

NIEHS SNPs

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF060515 mRNA. Translation: AAD09978.1 .
BT006950 mRNA. Translation: AAP35596.1 .
AF542236 Genomic DNA. Translation: AAN06829.1 .
AL110504 Genomic DNA. No translation available.
BC015935 mRNA. Translation: AAH15935.1 .
AH009612 Genomic DNA. Translation: AAF82290.1 .
BX247958 mRNA. Translation: CAD62298.1 .
AB209373 Transcribed RNA. Translation: BAD92610.1 .
CCDSi CCDS45160.1. [O75909-3 ]
RefSeqi NP_001092872.1. NM_001099402.1. [O75909-3 ]
XP_005268211.1. XM_005268154.2. [O75909-3 ]
UniGenei Hs.510409.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2I53 X-ray 1.50 A 11-267 [» ]
4CXA X-ray 3.15 B/D 11-267 [» ]
4NST X-ray 2.20 B/D 1-267 [» ]
4UN0 X-ray 3.15 A/B 11-267 [» ]
ProteinModelPortali O75909.
SMRi O75909. Positions 14-267.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 114339. 29 interactions.
IntActi O75909. 16 interactions.
MINTi MINT-1437641.
STRINGi 9606.ENSP00000374529.

Chemistry

ChEMBLi CHEMBL3038475.

PTM databases

PhosphoSitei O75909.

Proteomic databases

MaxQBi O75909.
PaxDbi O75909.
PRIDEi O75909.

Protocols and materials databases

DNASUi 8812.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000389879 ; ENSP00000374529 ; ENSG00000090061 . [O75909-3 ]
GeneIDi 8812.
KEGGi hsa:8812.
UCSCi uc001ygi.4. human. [O75909-3 ]

Organism-specific databases

CTDi 8812.
GeneCardsi GC14P099947.
HGNCi HGNC:1596. CCNK.
HPAi HPA000645.
MIMi 603544. gene.
neXtProti NX_O75909.
PharmGKBi PA26161.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5333.
GeneTreei ENSGT00760000119191.
HOGENOMi HOG000220828.
HOVERGENi HBG050836.
InParanoidi O75909.
OMAi KIETSHP.
OrthoDBi EOG7VQJCR.
TreeFami TF101010.

Enzyme and pathway databases

SignaLinki O75909.

Miscellaneous databases

ChiTaRSi CCNK. human.
EvolutionaryTracei O75909.
GeneWikii Cyclin_K.
GenomeRNAii 8812.
NextBioi 33052.
PROi O75909.
SOURCEi Search...

Gene expression databases

Bgeei O75909.
CleanExi HS_CCNK.
ExpressionAtlasi O75909. baseline and differential.
Genevestigatori O75909.

Family and domain databases

Gene3Di 1.10.472.10. 1 hit.
InterProi IPR013763. Cyclin-like.
IPR015429. Cyclin_C/H/T/L.
IPR006671. Cyclin_N.
[Graphical view ]
PANTHERi PTHR10026. PTHR10026. 1 hit.
Pfami PF00134. Cyclin_N. 1 hit.
[Graphical view ]
SMARTi SM00385. CYCLIN. 2 hits.
[Graphical view ]
SUPFAMi SSF47954. SSF47954. 2 hits.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Human cyclin K, a novel RNA polymerase II-associated cyclin possessing both carboxy-terminal domain kinase and Cdk-activating kinase activity."
    Edwards M.C., Wong C., Elledge S.J.
    Mol. Cell. Biol. 18:4291-4300(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), FUNCTION, SUBUNIT, TISSUE SPECIFICITY.
  2. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
  3. NIEHS SNPs program
    Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  4. "The DNA sequence and analysis of human chromosome 14."
    Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C., Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A., Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H., Du H.
    , Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M., Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V., Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F., Waterston R., Hood L., Weissenbach J.
    Nature 421:601-607(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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] (ISOFORM 2).
    Tissue: Uterus.
  6. Elledge S., Gerber S., Rozet J., Perrault I., Ducroq D., Munnich A., Kaplan J.
    Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-348 (ISOFORMS 1/3).
  7. Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F.
    Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 191-580 (ISOFORM 4).
    Tissue: Brain.
  8. "Full-length cDNA libraries and normalization."
    Li W.B., Gruber C., Jessee J., Polayes D.
    Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 279-580 (ISOFORM 4).
    Tissue: Neuroblastoma.
  9. "Cyclin K functions as a CDK9 regulatory subunit and participates in RNA polymerase II transcription."
    Fu T.J., Peng J., Lee G., Price D.H., Flores O.
    J. Biol. Chem. 274:34527-34530(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH CDK9.
    Tissue: T-cell.
  10. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-340, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
    Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
    Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-324 AND SER-340, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-324 AND SER-340, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-324; SER-329 AND SER-340, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  15. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. "The Cyclin K/Cdk12 complex maintains genomic stability via regulation of expression of DNA damage response genes."
    Blazek D., Kohoutek J., Bartholomeeusen K., Johansen E., Hulinkova P., Luo Z., Cimermancic P., Ule J., Peterlin B.M.
    Genes Dev. 25:2158-2172(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBUNIT, SUBCELLULAR LOCATION.
  17. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-324 AND SER-340, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  18. "Crystal structure of human cyclin K, a positive regulator of cyclin-dependent kinase 9."
    Baek K., Brown R.S., Birrane G., Ladias J.A.
    J. Mol. Biol. 366:563-573(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 11-267.
  19. Cited for: X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 1-267 IN COMPLEX WITH CDK12, INTERACTION WITH CDK12.

Entry informationi

Entry nameiCCNK_HUMAN
AccessioniPrimary (citable) accession number: O75909
Secondary accession number(s): Q59FT6
, Q86U16, Q96B63, Q9NNY9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: December 16, 2008
Last modified: October 29, 2014
This is version 141 of the entry and version 2 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 14
    Human chromosome 14: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3