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Q92833 (JARD2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 118. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Protein Jumonji
Alternative name(s):
Jumonji/ARID domain-containing protein 2
Gene names
Name:JARID2
Synonyms:JMJ
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1246 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Regulator of histone methyltransferase complexes that plays an essential role in embryonic development, including heart and liver development, neural tube fusion process and hematopoiesis. Acts by modulating histone methyltransferase activity and promoting the recruitment of histone methyltransferase complexes to their target genes. Binds DNA and mediates the recruitment of the PRC2 complex to target genes in embryonic stem cells. Does not have histone demethylase activity but regulates activity of various histone methyltransferase complexes. In embryonic stem cells, it associates with the PRC2 complex and inhibits trimethylation of 'Lys-27' of histone H3 (H3K27me3) by the PRC2 complex, thereby playing a key role in differentiation of embryonic stem cells and normal development. In cardiac cells, it is required to repress expression of cyclin-D1 (CCND1) by activating methylation of 'Lys-9' of histone H3 (H3K9me) by the GLP1/EHMT1 and G9a/EHMT2 histone methyltransferases. Also acts as a transcriptional repressor of ANF via its interaction with GATA4 and NKX2-5. Participates in the negative regulation of cell proliferation signaling. Ref.7

Subunit structure

Associates with a histone methyltransferase complex containing GLP1/EHMT1 and G9a/EHMT2. Interacts with SUZ12; the interaction is direct. Interacts with GATA4 (via the N-terminal region). Interacts with NKX2-5 (via the C-terminal region). Interacts with RB1. Interacts with ZNF496 By similarity. Associates with the PRC2 complex, which includes EED, EZH1, EZH2, SUZ12, RBBP4 and AEBP2; JARID2 is probably not a core component of the PRC2 complex and associates to PRC2 via its interaction with SUZ12.

Subcellular location

Nucleus. Note: Colocalizes with the PRC2 complex on chromatin. Ref.7

Tissue specificity

During embryogenesis, predominantly expressed in neurons and particularly in dorsal root ganglion cells.

Domain

The ARID domain is required to target the PRC2 complex to its target genes By similarity.

The GSGFP motif is required for the interaction with SUZ12 By similarity.

Sequence similarities

Contains 1 ARID domain.

Contains 1 JmjC domain.

Contains 1 JmjN domain.

Sequence caution

The sequence AAC50822.1 differs from that shown. Reason: Frameshift at position 1233.

Ontologies

Keywords
   Biological processDifferentiation
Transcription
Transcription regulation
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
   Molecular functionChromatin regulator
Developmental protein
Repressor
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcentral nervous system development

Traceable author statement Ref.1. Source: ProtInc

chromatin modification

Inferred from electronic annotation. Source: UniProtKB-KW

liver development

Inferred from electronic annotation. Source: Ensembl

negative regulation of cell proliferation

Inferred from electronic annotation. Source: Ensembl

negative regulation of histone methylation

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of transcription from RNA polymerase II promoter

Inferred from electronic annotation. Source: Ensembl

negative regulation of transcription, DNA-templated

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of histone H3-K9 methylation

Inferred from sequence or structural similarity. Source: UniProtKB

spleen development

Inferred from electronic annotation. Source: Ensembl

stem cell differentiation

Inferred from sequence or structural similarity. Source: UniProtKB

thymus development

Inferred from electronic annotation. Source: Ensembl

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componenthistone methyltransferase complex

Inferred from sequence or structural similarity. Source: UniProtKB

nucleus

Inferred from direct assay Ref.7. Source: UniProtKB

   Molecular_functionDNA binding

Inferred from electronic annotation. Source: Ensembl

chromatin binding

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q92833-1)

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.
Isoform 2 (identifier: Q92833-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-60: MSKERPKRNI...GIAGSLKTVN → MAAPRVCQVQFLVAYLEEPGIE
     949-1246: WYCIPAEEEN...SSSKSASSSS → CLSVEPVFPH...AWRGVLGPRL
Note: No experimental confirmation available.
Isoform 3 (identifier: Q92833-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-172: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 12461246Protein Jumonji
PRO_0000200591

Regions

Domain557 – 59842JmjN
Domain621 – 71393ARID
Domain884 – 1048165JmjC
Motif104 – 1107Nuclear localization signal By similarity
Motif874 – 8785GSGFP motif
Compositional bias1234 – 124613Poly-Ser

Amino acid modifications

Modified residue781Phosphoserine Ref.8
Modified residue3781N6-acetyllysine Ref.6
Modified residue4551Phosphoserine Ref.8

Natural variations

Alternative sequence1 – 172172Missing in isoform 3.
VSP_045041
Alternative sequence1 – 6060MSKER…LKTVN → MAAPRVCQVQFLVAYLEEPG IE in isoform 2.
VSP_038756
Alternative sequence949 – 1246298WYCIP…ASSSS → CLSVEPVFPHLSVAVGSIVD LGISFLPCGDTRVMYPVESV AWRGVLGPRL in isoform 2.
VSP_038757

Experimental info

Sequence conflict2501K → E in BAH13011. Ref.2
Sequence conflict5991C → S in BAH13011. Ref.2
Sequence conflict6731D → E in AAC50822. Ref.1
Sequence conflict6811A → S in AAC50822. Ref.1
Sequence conflict6881R → K in AAC50822. Ref.1
Sequence conflict6921D → E in AAC50822. Ref.1
Sequence conflict7051L → I in AAC50822. Ref.1
Sequence conflict7541F → L in AAC50822. Ref.1
Sequence conflict12121S → H in AAC50822. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified March 15, 2005. Version 2.
Checksum: E4929984259110DB

FASTA1,246138,734
        10         20         30         40         50         60 
MSKERPKRNI IQKKYDDSDG IPWSEERVVR KVLYLSLKEF KNSQKRQHAE GIAGSLKTVN 

        70         80         90        100        110        120 
GLLGNDQSKG LGPASEQSEN EKDDASQVSS TSNDVSSSDF EEGPSRKRPR LQAQRKFAQS 

       130        140        150        160        170        180 
QPNSPSTTPV KIVEPLLPPP ATQISDLSKR KPKTEDFLTF LCLRGSPALP NSMVYFGSSQ 

       190        200        210        220        230        240 
DEEEVEEEDD ETEDVKTATN NASSSCQSTP RKGKTHKHVH NGHVFNGSSR STREKEPVQK 

       250        260        270        280        290        300 
HKSKEATPAK EKHSDHRADS RREQASANHP AAAPSTGSSA KGLAATHHHP PLHRSAQDLR 

       310        320        330        340        350        360 
KQVSKVNGVT RMSSLGAGVT SAKKMREVRP SPSKTVKYTA TVTKGAVTYT KAKRELVKDT 

       370        380        390        400        410        420 
KPNHHKPSSA VNHTISGKTE SSNAKTRKQV LSLGGASKST GPAVNGLKVS GRLNPKSCTK 

       430        440        450        460        470        480 
EVGGRQLREG LQLREGLRNS KRRLEEAHQA EKPQSPPKKM KGAAGPAEGP GKKAPAERGL 

       490        500        510        520        530        540 
LNGHVKKEVP ERSLERNRPK RATAGKSTPG RQAHGKADSA SCENRSTSQP ESVHKPQDSG 

       550        560        570        580        590        600 
KAEKGGGKAG WAAMDEIPVL RPSAKEFHDP LIYIESVRAQ VEKFGMCRVI PPPDWRPECK 

       610        620        630        640        650        660 
LNDEMRFVTQ IQHIHKLGRR WGPNVQRLAC IKKHLKSQGI TMDELPLIGG CELDLACFFR 

       670        680        690        700        710        720 
LINEMGGMQQ VTDLKKWNKL ADMLRIPRTA QDRLAKLQEA YCQYLLSYDS LSPEEHRRLE 

       730        740        750        760        770        780 
KEVLMEKEIL EKRKGPLEGH TENDHHKFHP LPRFEPKNGL IHGVAPRNGF RSKLKEVGQA 

       790        800        810        820        830        840 
QLKTGRRRLF AQEKEVVKEE EEDKGVLNDF HKCIYKGRSV SLTTFYRTAR NIMSMCFSKE 

       850        860        870        880        890        900 
PAPAEIEQEY WRLVEEKDCH VAVHCGKVDT NTHGSGFPVG KSEPFSRHGW NLTVLPNNTG 

       910        920        930        940        950        960 
SILRHLGAVP GVTIPWLNIG MVFSTSCWSR DQNHLPYIDY LHTGADCIWY CIPAEEENKL 

       970        980        990       1000       1010       1020 
EDVVHTLLQA NGTPGLQMLE SNVMISPEVL CKEGIKVHRT VQQSGQFVVC FPGSFVSKVC 

      1030       1040       1050       1060       1070       1080 
CGYSVSETVH FATTQWTSMG FETAKEMKRR HIAKPFSMEK LLYQIAQAEA KKENGPTLST 

      1090       1100       1110       1120       1130       1140 
ISALLDELRD TELRQRRQLF EAGLHSSARY GSHDGSSTVA DGKKKPRKWL QLETSERRCQ 

      1150       1160       1170       1180       1190       1200 
ICQHLCYLSM VVQENENVVF CLECALRHVE KQKSCRGLKL MYRYDEEQII SLVNQICGKV 

      1210       1220       1230       1240 
SGKNGSIENC LSKPTPKRGP RKRATVDVPP SRLSASSSSK SASSSS 

« Hide

Isoform 2 [UniParc].

Checksum: 985C77D3B34F699B
Show »

FASTA960106,139
Isoform 3 [UniParc].

Checksum: A913DFCF25573C4A
Show »

FASTA1,074119,689

References

« Hide 'large scale' references
[1]"Characterization of the human jumonji gene."
Berge-Lefranc J.-L., Jay P., Massacrier A., Cau P., Mattei M.-G., Bauer S., Marsollier C., Berta P., Fontes M.
Hum. Mol. Genet. 5:1637-1641(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[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. expand/collapse author list , 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; 2 AND 3).
Tissue: Thymus and Trachea.
[3]"The DNA sequence and analysis of human chromosome 6."
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D. expand/collapse author list , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
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 1).
Tissue: Mammary gland and Testis.
[6]"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-378, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[7]"JARID2 regulates binding of the Polycomb repressive complex 2 to target genes in ES cells."
Pasini D., Cloos P.A., Walfridsson J., Olsson L., Bukowski J.P., Johansen J.V., Bak M., Tommerup N., Rappsilber J., Helin K.
Nature 464:306-310(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, ASSOCIATION WITH THE PRC2 COMPLEX.
[8]"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-78 AND SER-455, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U57592 mRNA. Translation: AAC50822.1. Frameshift.
AK292861 mRNA. Translation: BAF85550.1.
AK299349 mRNA. Translation: BAH13011.1.
AK303610 mRNA. Translation: BAH13996.1.
AL136162, AL021938 Genomic DNA. Translation: CAI15719.1.
AL021938, AL136162 Genomic DNA. Translation: CAI19873.1.
CH471087 Genomic DNA. Translation: EAW55357.1.
BC046184 mRNA. Translation: AAH46184.1.
BC046246 mRNA. Translation: AAH46246.1.
RefSeqNP_001253969.1. NM_001267040.1.
NP_004964.2. NM_004973.3.
XP_005249146.1. XM_005249089.1.
UniGeneHs.269059.

3D structure databases

ProteinModelPortalQ92833.
SMRQ92833. Positions 554-732, 805-1070.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109923. 10 interactions.
DIPDIP-45494N.
IntActQ92833. 3 interactions.
STRING9606.ENSP00000341280.

PTM databases

PhosphoSiteQ92833.

Polymorphism databases

DMDM61252601.

Proteomic databases

PaxDbQ92833.
PRIDEQ92833.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000341776; ENSP00000341280; ENSG00000008083. [Q92833-1]
ENST00000397311; ENSP00000380478; ENSG00000008083. [Q92833-3]
GeneID3720.
KEGGhsa:3720.
UCSCuc003nbj.4. human. [Q92833-1]

Organism-specific databases

CTD3720.
GeneCardsGC06P015246.
HGNCHGNC:6196. JARID2.
HPAHPA044909.
MIM601594. gene.
neXtProtNX_Q92833.
PharmGKBPA29995.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG327026.
HOGENOMHOG000013203.
HOVERGENHBG052160.
InParanoidQ92833.
KOK11478.
OMARPECKLN.
OrthoDBEOG76MK7F.
PhylomeDBQ92833.
TreeFamTF323264.

Gene expression databases

ArrayExpressQ92833.
BgeeQ92833.
CleanExHS_JARID2.
GenevestigatorQ92833.

Family and domain databases

Gene3D1.10.150.60. 1 hit.
InterProIPR001606. ARID/BRIGHT_DNA-bd.
IPR003347. JmjC_dom.
IPR003349. TF_JmjN.
IPR004198. Znf_C5HC2.
[Graphical view]
PfamPF01388. ARID. 1 hit.
PF02373. JmjC. 1 hit.
PF02375. JmjN. 1 hit.
PF02928. zf-C5HC2. 1 hit.
[Graphical view]
SMARTSM00501. BRIGHT. 1 hit.
SM00558. JmjC. 1 hit.
SM00545. JmjN. 1 hit.
[Graphical view]
SUPFAMSSF46774. SSF46774. 1 hit.
PROSITEPS51011. ARID. 1 hit.
PS51184. JMJC. 1 hit.
PS51183. JMJN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiJARID2.
GenomeRNAi3720.
NextBio14577.
PROQ92833.
SOURCESearch...

Entry information

Entry nameJARD2_HUMAN
AccessionPrimary (citable) accession number: Q92833
Secondary accession number(s): A8K9Z6 expand/collapse secondary AC list , B7Z5S5, B7Z8L0, Q5U5L5, Q86X63
Entry history
Integrated into UniProtKB/Swiss-Prot: January 11, 2001
Last sequence update: March 15, 2005
Last modified: April 16, 2014
This is version 118 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 6

Human chromosome 6: entries, gene names and cross-references to MIM