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Q9H6W3

- NO66_HUMAN

UniProt

Q9H6W3 - NO66_HUMAN

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Protein
Bifunctional lysine-specific demethylase and histidyl-hydroxylase NO66
Gene
NO66, C14orf169, MAPJD
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Oxygenase that can act as both a histone lysine demethylase and a ribosomal histidine hydroxylase. Specifically demethylates 'Lys-4' (H3K4me) and 'Lys-36' (H3K36me) of histone H3, thereby playing a central role in histone code. Preferentially demethylates trimethylated H3 'Lys-4' (H3K4me3) and monomethylated H3 'Lys-4' (H3K4me1) residues, while it has weaker activity for dimethylated H3 'Lys-36' (H3K36me2). Also catalyzes the hydroxylation of 60S ribosomal protein L8 on 'His-216'. Acts as a regulator of osteoblast differentiation via its interaction with SP7/OSX by demethylating H3K4me and H3K36me, thereby inhibiting SP7/OSX-mediated promoter activation By similarity. May also play a role in ribosome biogenesis and in the replication or remodeling of certain heterochromatic region. Participates in MYC-induced transcriptional activation.3 Publications

Catalytic activityi

Protein N6,N(6)-dimethyl-L-lysine + 2-oxoglutarate + O2 = protein N(6)-methyl-L-lysine + succinate + formaldehyde + CO2.1 Publication
Protein N(6)-methyl-L-lysine + 2-oxoglutarate + O2 = protein L-lysine + succinate + formaldehyde + CO2.1 Publication
L-histidine-[60S ribosomal protein L8] + 2-oxoglutarate + O2 = (3S)-3-hydroxy-L-histidine-[60S ribosomal protein L8] + succinate + CO2.1 Publication

Cofactori

Binds 1 Fe2+ ion per subunit By similarity.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi340 – 3401Iron; catalytic By similarity
Metal bindingi342 – 3421Iron; catalytic By similarity
Metal bindingi405 – 4051Iron; catalytic By similarity

GO - Molecular functioni

  1. histone demethylase activity (H3-K36 specific) Source: UniProtKB
  2. histone demethylase activity (H3-K4 specific) Source: UniProtKB
  3. iron ion binding Source: UniProtKB
  4. oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, 2-oxoglutarate as one donor, and incorporation of one atom each of oxygen into both donors Source: UniProtKB
  5. protein binding Source: UniProtKB
Complete GO annotation...

GO - Biological processi

  1. histone H3-K36 demethylation Source: UniProtKB
  2. histone H3-K4 demethylation Source: UniProtKB
  3. negative regulation of osteoblast differentiation Source: UniProtKB
  4. negative regulation of transcription, DNA-templated Source: UniProtKB
  5. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator, Dioxygenase, Oxidoreductase, Repressor

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

Iron, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Bifunctional lysine-specific demethylase and histidyl-hydroxylase NO66 (EC:1.14.11.-, EC:1.14.11.27)
Alternative name(s):
60S ribosomal protein L8 histidine hydroxylase
Histone lysine demethylase NO66
Myc-associated protein with JmjC domain
Nucleolar protein 66
Short name:
hsNO66
Ribosomal oxygenase NO66
Short name:
ROX
Gene namesi
Name:NO66
Synonyms:C14orf169, MAPJD
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Unplaced

Organism-specific databases

HGNCiHGNC:20968. C14orf169.

Subcellular locationi

Nucleusnucleolus. Nucleusnucleoplasm
Note: Granular part of nucleoli. Nucleoplasm, nucleoplasmic foci, some of them associated with nucleoli.2 Publications

GO - Cellular componenti

  1. nucleolus Source: UniProtKB-SubCell
  2. nucleoplasm Source: UniProtKB-SubCell
  3. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134919088.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 641641Bifunctional lysine-specific demethylase and histidyl-hydroxylase NO66
PRO_0000264613Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine1 Publication
Modified residuei109 – 1091Phosphoserine2 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ9H6W3.
PeptideAtlasiQ9H6W3.
PRIDEiQ9H6W3.

PTM databases

PhosphoSiteiQ9H6W3.

Expressioni

Tissue specificityi

Widely expressed. Overexpressed in lung carcinomas.2 Publications

Gene expression databases

CleanExiHS_C14orf169.
GenevestigatoriQ9H6W3.

Interactioni

Subunit structurei

Interacts with SP7/OSX; the interaction is direct By similarity. Interacts with MYC. Interacts with PHF19; leading to its recruitment to H3K36me3 sites.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Sp7Q8VI676EBI-2513645,EBI-7608836From a different organism.

Protein-protein interaction databases

BioGridi122818. 4 interactions.
IntActiQ9H6W3. 3 interactions.
MINTiMINT-5009834.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi184 – 19310
Helixi198 – 21013
Helixi215 – 2217
Turni222 – 2254
Beta strandi228 – 2303
Turni235 – 2406
Helixi244 – 25310
Turni259 – 2613
Beta strandi262 – 2687
Beta strandi271 – 2744
Beta strandi278 – 2803
Helixi283 – 2919
Beta strandi295 – 2995
Helixi301 – 3033
Helixi306 – 31914
Beta strandi324 – 3307
Beta strandi332 – 3343
Beta strandi343 – 35311
Beta strandi355 – 3595
Helixi365 – 3673
Turni379 – 3813
Beta strandi386 – 3916
Beta strandi396 – 3994
Beta strandi405 – 4084
Beta strandi415 – 4228
Helixi428 – 44619
Helixi448 – 4514
Helixi458 – 4603
Helixi464 – 4663
Helixi472 – 48716
Helixi488 – 4914
Helixi494 – 50815
Helixi516 – 5205
Helixi523 – 5253
Beta strandi529 – 5313
Beta strandi535 – 5373
Beta strandi547 – 56115
Beta strandi564 – 5707
Beta strandi583 – 5875
Helixi589 – 5913
Helixi592 – 6009
Turni601 – 6033
Helixi608 – 6103
Beta strandi612 – 6154
Helixi616 – 62813
Beta strandi632 – 6365

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4CCJX-ray2.15A/B/C/D183-641[»]
4CCKX-ray2.15A/B/C/D183-641[»]
4CCMX-ray2.51A/B183-641[»]
4CCNX-ray2.23A/B183-641[»]
4CCOX-ray2.30A/B183-641[»]
4DIQX-ray2.40A/B167-641[»]
4E4HX-ray2.28A/B/C/D183-641[»]
ProteinModelPortaliQ9H6W3.
SMRiQ9H6W3. Positions 183-638.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini294 – 439146JmjC
Add
BLAST

Sequence similaritiesi

Contains 1 JmjC domain.

Phylogenomic databases

HOVERGENiHBG060021.
KOiK16914.
PhylomeDBiQ9H6W3.

Family and domain databases

InterProiIPR003347. JmjC_dom.
[Graphical view]
PfamiPF08007. Cupin_4. 1 hit.
[Graphical view]
SMARTiSM00558. JmjC. 1 hit.
[Graphical view]
PROSITEiPS51184. JMJC. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9H6W3-1) [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

MDGLQASAGP LRRGRPKRRR KPQPHSGSVL ALPLRSRKIR KQLRSVVSRM    50
AALRTQTLPS ENSEESRVES TADDLGDALP GGAAVAAVPD AARREPYGHL 100
GPAELLEASP AARSLQTPSA RLVPASAPPA RLVEVPAAPV RVVETSALLC 150
TAQHLAAVQS SGAPATASGP QVDNTGGEPA WDSPLRRVLA ELNRIPSSRR 200
RAARLFEWLI APMPPDHFYR RLWEREAVLV RRQDHTYYQG LFSTADLDSM 250
LRNEEVQFGQ HLDAARYING RRETLNPPGR ALPAAAWSLY QAGCSLRLLC 300
PQAFSTTVWQ FLAVLQEQFG SMAGSNVYLT PPNSQGFAPH YDDIEAFVLQ 350
LEGRKLWRVY RPRVPTEELA LTSSPNFSQD DLGEPVLQTV LEPGDLLYFP 400
RGFIHQAECQ DGVHSLHLTL STYQRNTWGD FLEAILPLAV QAAMEENVEF 450
RRGLPRDFMD YMGAQHSDSK DPRRTAFMEK VRVLVARLGH FAPVDAVADQ 500
RAKDFIHDSL PPVLTDRERA LSVYGLPIRW EAGEPVNVGA QLTTETEVHM 550
LQDGIARLVG EGGHLFLYYT VENSRVYHLE EPKCLEIYPQ QADAMELLLG 600
SYPEFVRVGD LPCDSVEDQL SLATTLYDKG LLLTKMPLAL N 641
Length:641
Mass (Da):71,086
Last modified:January 19, 2010 - v2
Checksum:iE66A4342B1D1BFF2
GO
Isoform 2 (identifier: Q9H6W3-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-212: Missing.

Note: No experimental confirmation available.

Show »
Length:429
Mass (Da):48,687
Checksum:iF07631F3A3F8CDB7
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti17 – 171K → R.3 Publications
Corresponds to variant rs10144469 [ dbSNP | Ensembl ].
VAR_062422
Natural varianti218 – 2181F → S.
Corresponds to variant rs758109 [ dbSNP | Ensembl ].
VAR_057819
Natural varianti239 – 2391Q → H.
Corresponds to variant rs34970526 [ dbSNP | Ensembl ].
VAR_060191
Natural varianti364 – 3641V → A.3 Publications
Corresponds to variant rs3813563 [ dbSNP | Ensembl ].
VAR_062423

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 212212Missing in isoform 2.
VSP_038663Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti392 – 3921E → G in BAG61814. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY390535 mRNA. Translation: AAR27292.1.
AK025455 mRNA. Translation: BAB15138.1.
AK299994 mRNA. Translation: BAG61814.1.
AC005280 Genomic DNA. No translation available.
BC011350 mRNA. Translation: AAH11350.1.
BC071954 mRNA. Translation: AAH71954.1.
RefSeqiNP_078920.2. NM_024644.4. [Q9H6W3-1]
UniGeneiHs.509916.

Genome annotation databases

GeneIDi79697.
KEGGihsa:79697.
UCSCiuc001xok.1. human. [Q9H6W3-1]

Polymorphism databases

DMDMi284018103.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY390535 mRNA. Translation: AAR27292.1 .
AK025455 mRNA. Translation: BAB15138.1 .
AK299994 mRNA. Translation: BAG61814.1 .
AC005280 Genomic DNA. No translation available.
BC011350 mRNA. Translation: AAH11350.1 .
BC071954 mRNA. Translation: AAH71954.1 .
RefSeqi NP_078920.2. NM_024644.4. [Q9H6W3-1 ]
UniGenei Hs.509916.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
4CCJ X-ray 2.15 A/B/C/D 183-641 [» ]
4CCK X-ray 2.15 A/B/C/D 183-641 [» ]
4CCM X-ray 2.51 A/B 183-641 [» ]
4CCN X-ray 2.23 A/B 183-641 [» ]
4CCO X-ray 2.30 A/B 183-641 [» ]
4DIQ X-ray 2.40 A/B 167-641 [» ]
4E4H X-ray 2.28 A/B/C/D 183-641 [» ]
ProteinModelPortali Q9H6W3.
SMRi Q9H6W3. Positions 183-638.
ModBasei Search...

Protein-protein interaction databases

BioGridi 122818. 4 interactions.
IntActi Q9H6W3. 3 interactions.
MINTi MINT-5009834.

PTM databases

PhosphoSitei Q9H6W3.

Polymorphism databases

DMDMi 284018103.

Proteomic databases

MaxQBi Q9H6W3.
PeptideAtlasi Q9H6W3.
PRIDEi Q9H6W3.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 79697.
KEGGi hsa:79697.
UCSCi uc001xok.1. human. [Q9H6W3-1 ]

Organism-specific databases

CTDi 79697.
GeneCardsi GC14P073958.
H-InvDB HIX0011794.
HGNCi HGNC:20968. C14orf169.
MIMi 611919. gene.
neXtProti NX_Q9H6W3.
PharmGKBi PA134919088.
GenAtlasi Search...

Phylogenomic databases

HOVERGENi HBG060021.
KOi K16914.
PhylomeDBi Q9H6W3.

Miscellaneous databases

GenomeRNAii 79697.
NextBioi 68992.
PROi Q9H6W3.
SOURCEi Search...

Gene expression databases

CleanExi HS_C14orf169.
Genevestigatori Q9H6W3.

Family and domain databases

InterProi IPR003347. JmjC_dom.
[Graphical view ]
Pfami PF08007. Cupin_4. 1 hit.
[Graphical view ]
SMARTi SM00558. JmjC. 1 hit.
[Graphical view ]
PROSITEi PS51184. JMJC. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "NO66, a highly conserved dual location protein in the nucleolus and in a special type of synchronously replicating chromatin."
    Eilbracht J., Reichenzeller M., Hergt M., Schnoelzer M., Heid H., Stoehr M., Franke W.W., Schmidt-Zachmann M.S.
    Mol. Biol. Cell 15:1816-1832(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, VARIANTS ARG-17 AND ALA-364.
  2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), VARIANTS ARG-17 AND ALA-364.
  3. "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].
  4. "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 1), VARIANTS ARG-17 AND ALA-364.
    Tissue: Lymph and Mammary gland.
  5. "Identification of Myc-associated protein with JmjC domain as a novel therapeutic target oncogene for lung cancer."
    Suzuki C., Takahashi K., Hayama S., Ishikawa N., Kato T., Ito T., Tsuchiya E., Nakamura Y., Daigo Y.
    Mol. Cancer Ther. 6:542-551(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH MYC, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  6. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-109, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  7. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-109, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  8. "Polycomb PHF19 binds H3K36me3 and recruits PRC2 and demethylase NO66 to embryonic stem cell genes during differentiation."
    Brien G.L., Gambero G., O'Connell D.J., Jerman E., Turner S.A., Egan C.M., Dunne E.J., Jurgens M.C., Wynne K., Piao L., Lohan A.J., Ferguson N., Shi X., Sinha K.M., Loftus B.J., Cagney G., Bracken A.P.
    Nat. Struct. Mol. Biol. 19:1273-1281(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PHF19.
  9. Cited for: FUNCTION AS RPL8 HYDROXYLASE, CATALYTIC ACTIVITY.
  10. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiNO66_HUMAN
AccessioniPrimary (citable) accession number: Q9H6W3
Secondary accession number(s): B4DT02
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 12, 2006
Last sequence update: January 19, 2010
Last modified: September 3, 2014
This is version 100 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. 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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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