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Q92613

- JADE3_HUMAN

UniProt

Q92613 - JADE3_HUMAN

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Protein

Protein Jade-3

Gene

JADE3

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

Functioni

Component of the HBO1 complex which has a histone H4-specific acetyltransferase activity, a reduced activity toward histone H3 and is responsible for the bulk of histone H4 acetylation in vivo.1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri200 – 25051PHD-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  1. zinc ion binding Source: InterPro

GO - Biological processi

  1. histone H3 acetylation Source: UniProtKB
  2. histone H4-K12 acetylation Source: UniProtKB
  3. histone H4-K5 acetylation Source: UniProtKB
  4. histone H4-K8 acetylation Source: UniProtKB
Complete GO annotation...

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_172610. HATs acetylate histones.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein Jade-3
Alternative name(s):
Jade family PHD finger protein 3
PHD finger protein 16
Gene namesi
Name:JADE3
Synonyms:KIAA0215, PHF16
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome X

Organism-specific databases

HGNCiHGNC:22982. JADE3.

Subcellular locationi

GO - Cellular componenti

  1. histone acetyltransferase complex Source: UniProtKB
Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134993233.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 823823Protein Jade-3PRO_0000059309Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei30 – 301N6-acetyllysine1 Publication
Modified residuei32 – 321N6-acetyllysine1 Publication
Modified residuei38 – 381N6-acetyllysine1 Publication
Modified residuei85 – 851Phosphoserine2 Publications
Modified residuei566 – 5661Phosphoserine4 Publications
Modified residuei601 – 6011N6-acetyllysineBy similarity
Modified residuei638 – 6381N6-acetyllysine1 Publication
Modified residuei735 – 7351N6-acetyllysineBy similarity
Modified residuei774 – 7741Phosphoserine1 Publication
Modified residuei776 – 7761Phosphoserine1 Publication
Modified residuei780 – 7801Phosphoserine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ92613.
PaxDbiQ92613.
PRIDEiQ92613.

PTM databases

PhosphoSiteiQ92613.

Expressioni

Tissue specificityi

Ubiquitously expressed, with highest levels in placenta and uterus.1 Publication

Inductioni

By estradiol in estrogen-responsive breast cancer cells.1 Publication

Gene expression databases

BgeeiQ92613.
CleanExiHS_PHF16.
ExpressionAtlasiQ92613. baseline and differential.
GenevestigatoriQ92613.

Organism-specific databases

HPAiHPA006007.

Interactioni

Subunit structurei

Component of the HBO1 complex composed at least of ING4 or ING5, KAT7/HBO1, MEAF6, and one of JADE1, JADE2 and JADE3.1 Publication

Protein-protein interaction databases

BioGridi115113. 6 interactions.
STRINGi9606.ENSP00000218343.

Structurei

3D structure databases

ProteinModelPortaliQ92613.
SMRiQ92613. Positions 198-248, 302-347.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the JADE family.Curated
Contains 1 PHD-type zinc finger.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri200 – 25051PHD-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiCOG5141.
GeneTreeiENSGT00740000114866.
HOGENOMiHOG000220882.
HOVERGENiHBG053585.
InParanoidiQ92613.
OMAiASVCRYD.
OrthoDBiEOG738044.
PhylomeDBiQ92613.
TreeFamiTF316118.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR019542. Enhancer_polycomb-like_N.
IPR019786. Zinc_finger_PHD-type_CS.
IPR011011. Znf_FYVE_PHD.
IPR001965. Znf_PHD.
IPR019787. Znf_PHD-finger.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PfamiPF10513. EPL1. 1 hit.
PF00628. PHD. 1 hit.
[Graphical view]
SMARTiSM00249. PHD. 2 hits.
[Graphical view]
SUPFAMiSSF57903. SSF57903. 1 hit.
PROSITEiPS01359. ZF_PHD_1. 1 hit.
PS50016. ZF_PHD_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q92613-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MKRHRPVSSS DSSDESPSTS FTSGSMYRIK SKIPNEHKKP AEVFRKDLIS
60 70 80 90 100
AMKLPDSHHI NPDSYYLFAD TWKEEWEKGV QVPASPDTVP QPSLRIIAEK
110 120 130 140 150
VKDVLFIRPR KYIHCSSPDT TEPGYINIME LAASVCRYDL DDMDIFWLQE
160 170 180 190 200
LNEDLAEMGC GPVDENLMEK TVEVLERHCH ENMNHAIETE EGLGIEYDED
210 220 230 240 250
VICDVCRSPD SEEGNDMVFC DKCNVCVHQA CYGILKVPEG SWLCRSCVLG
260 270 280 290 300
IYPQCVLCPK KGGALKTTKT GTKWAHVSCA LWIPEVSIAC PERMEPITKI
310 320 330 340 350
SHIPPSRWAL VCNLCKLKTG ACIQCSIKSC ITAFHVTCAF EHGLEMKTIL
360 370 380 390 400
DEGDEVKFKS YCLKHSQNRQ KLGEAEYPHH RAKEQSQAKS EKTSLRAQKL
410 420 430 440 450
RELEEEFYSL VRVEDVAAEL GMPTLAVDFI YNYWKLKRKS NFNKPLFPPK
460 470 480 490 500
EDEENGLVQP KEESIHTRMR MFMHLRQDLE RVRNLCYMIS RREKLKLSHN
510 520 530 540 550
KIQEQIFGLQ VQLLNQEIDA GLPLTNALEN SLFYPPPRIT LKLKMPKSTP
560 570 580 590 600
EDHRNSSTET DQQPHSPDSS SSVHSIRNMQ VPQESLEMRT KSYPRYPLES
610 620 630 640 650
KNNRLLASLS HSRSEAKESS PAWRTPSSEC YHGQSLGKPL VLQAALHGQS
660 670 680 690 700
SIGNGKSQPN SKFAKSNGLE GSWSGNVTQK DSSSEMFCDQ EPVFSPHLVS
710 720 730 740 750
QGSFRKSTVE HFSRSFKETT NRWVKNTEDL QCYVKPTKNM SPKEQFWGRQ
760 770 780 790 800
VLRRSAGRAP YQENDGYCPD LELSDSEAES DGNKEKVRVR KDSSDRENPP
810 820
HDSRRDCHGK SKTHPLSHSS MQR
Length:823
Mass (Da):93,808
Last modified:February 1, 1997 - v1
Checksum:i4E47E2A124D0CE38
GO

Sequence cautioni

The sequence BAA13205.2 differs from that shown. Reason: Erroneous initiation. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF127774 mRNA. Translation: AAD51905.1.
D86969 mRNA. Translation: BAA13205.2. Different initiation.
Z83822 Genomic DNA. No translation available.
BC114487 mRNA. Translation: AAI14488.1.
BC113880 mRNA. Translation: AAI13881.1.
BN000289 mRNA. Translation: CAE30502.1.
CCDSiCCDS14271.1.
RefSeqiNP_001070913.1. NM_001077445.2.
NP_055550.1. NM_014735.4.
UniGeneiHs.371977.

Genome annotation databases

EnsembliENST00000611250; ENSP00000479377; ENSG00000102221.
ENST00000614628; ENSP00000481850; ENSG00000102221.
GeneIDi9767.
KEGGihsa:9767.
UCSCiuc004dgx.3. human.

Polymorphism databases

DMDMi34098663.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF127774 mRNA. Translation: AAD51905.1 .
D86969 mRNA. Translation: BAA13205.2 . Different initiation.
Z83822 Genomic DNA. No translation available.
BC114487 mRNA. Translation: AAI14488.1 .
BC113880 mRNA. Translation: AAI13881.1 .
BN000289 mRNA. Translation: CAE30502.1 .
CCDSi CCDS14271.1.
RefSeqi NP_001070913.1. NM_001077445.2.
NP_055550.1. NM_014735.4.
UniGenei Hs.371977.

3D structure databases

ProteinModelPortali Q92613.
SMRi Q92613. Positions 198-248, 302-347.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 115113. 6 interactions.
STRINGi 9606.ENSP00000218343.

PTM databases

PhosphoSitei Q92613.

Polymorphism databases

DMDMi 34098663.

Proteomic databases

MaxQBi Q92613.
PaxDbi Q92613.
PRIDEi Q92613.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000611250 ; ENSP00000479377 ; ENSG00000102221 .
ENST00000614628 ; ENSP00000481850 ; ENSG00000102221 .
GeneIDi 9767.
KEGGi hsa:9767.
UCSCi uc004dgx.3. human.

Organism-specific databases

CTDi 9767.
GeneCardsi GC0XP046773.
HGNCi HGNC:22982. JADE3.
HPAi HPA006007.
MIMi 300618. gene.
neXtProti NX_Q92613.
PharmGKBi PA134993233.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5141.
GeneTreei ENSGT00740000114866.
HOGENOMi HOG000220882.
HOVERGENi HBG053585.
InParanoidi Q92613.
OMAi ASVCRYD.
OrthoDBi EOG738044.
PhylomeDBi Q92613.
TreeFami TF316118.

Enzyme and pathway databases

Reactomei REACT_172610. HATs acetylate histones.

Miscellaneous databases

GeneWikii PHF16.
GenomeRNAii 9767.
NextBioi 36762.
PROi Q92613.
SOURCEi Search...

Gene expression databases

Bgeei Q92613.
CleanExi HS_PHF16.
ExpressionAtlasi Q92613. baseline and differential.
Genevestigatori Q92613.

Family and domain databases

Gene3Di 3.30.40.10. 1 hit.
InterProi IPR019542. Enhancer_polycomb-like_N.
IPR019786. Zinc_finger_PHD-type_CS.
IPR011011. Znf_FYVE_PHD.
IPR001965. Znf_PHD.
IPR019787. Znf_PHD-finger.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view ]
Pfami PF10513. EPL1. 1 hit.
PF00628. PHD. 1 hit.
[Graphical view ]
SMARTi SM00249. PHD. 2 hits.
[Graphical view ]
SUPFAMi SSF57903. SSF57903. 1 hit.
PROSITEi PS01359. ZF_PHD_1. 1 hit.
PS50016. ZF_PHD_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Identification of human estrogen-inducible transcripts that potentially mediate the apoptotic response in breast cancer."
    Szelei J., Soto A.M., Geck P., Desronvil M., Prechtl N.V., Weill B.C., Sonnenschein C.
    J. Steroid Biochem. Mol. Biol. 72:89-102(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, INDUCTION BY ESTRADIOL.
  2. "Prediction of the coding sequences of unidentified human genes. VI. The coding sequences of 80 new genes (KIAA0201-KIAA0280) deduced by analysis of cDNA clones from cell line KG-1 and brain."
    Nagase T., Seki N., Ishikawa K., Ohira M., Kawarabayasi Y., Ohara O., Tanaka A., Kotani H., Miyajima N., Nomura N.
    DNA Res. 3:321-329(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Bone marrow.
  3. "The DNA sequence of the human X chromosome."
    Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.
    , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
    Nature 434:325-337(2005) [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].
  5. "Identification of Jade1, a gene encoding a PHD zinc finger protein, in a gene trap mutagenesis screen for genes involved in anteroposterior axis development."
    Tzouanacou E., Tweedie S., Wilson V.
    Mol. Cell. Biol. 23:8553-8562(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION.
  6. "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-566, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  7. "ING tumor suppressor proteins are critical regulators of chromatin acetylation required for genome expression and perpetuation."
    Doyon Y., Cayrou C., Ullah M., Landry A.-J., Cote V., Selleck W., Lane W.S., Tan S., Yang X.-J., Cote J.
    Mol. Cell 21:51-64(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN HISTONE H4 ACETYLATION, IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE HBO1 COMPLEX.
  8. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
    Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
    Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
    Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
    J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-85 AND SER-566, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-774; SER-776 AND SER-780, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. "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].
  12. "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-85, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  13. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-30; LYS-32; LYS-38 AND LYS-638, 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-566, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  15. "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-566, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiJADE3_HUMAN
AccessioniPrimary (citable) accession number: Q92613
Secondary accession number(s): Q6IE79
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 15, 2003
Last sequence update: February 1, 1997
Last modified: October 29, 2014
This is version 114 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome X
    Human chromosome X: 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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3