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Reviewed, UniProtKB/Swiss-Prot Q96KQ7 (EHMT2_HUMAN)

Last modified June 16, 2009. Version 93. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Histone-lysine N-methyltransferase, H3 lysine-9 specific 3
    EC=2.1.1.43
Alternative name(s):
    Histone H3-K9 methyltransferase 3
    H3-K9-HMTase 3
    Euchromatic histone-lysine N-methyltransferase 2
    HLA-B-associated transcript 8
    Protein G9a
    Lysine N-methyltransferase 1C
Gene names
Name: EHMT2
Synonyms: BAT8, C6orf30, G9A, KMT1C, NG36
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1210 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Histone methyltransferase. Preferentially methylates 'Lys-9' of histone H3 and 'Lys-27' of histone H3 (in vitro). H3 'Lys-9' methylation represents a specific tag for epigenetic transcriptional repression by recruiting HP1 proteins to methylated histones. Probably targeted to histone H3 by different DNA-binding proteins like E2F6, MGA, MAX and/or DP1. Also methylates histone H1 By similarity.

Catalytic activity

S-adenosyl-L-methionine + histone L-lysine = S-adenosyl-L-homocysteine + histone N(6)-methyl-L-lysine. Ref.7

Subunit structure

Part of the E2F6.com-1 complex in G0 phase composed of E2F6, MGA, MAX, TFDP1, CBX3, BAT8, EUHMTASE1, RING1, RNF2, MBLR, L3MBTL2 and YAF2. Interacts with GFI1B, WIZ and EHMT1. Ref.9 Ref.10

Subcellular location

Nucleus. Note: Associates with euchromatic regions. Does not associate with heterochromatin. Ref.7

Tissue specificity

Expressed in all tissues examined, with high levels in fetal liver, thymus, lymph node, spleen and peripheral blood leukocytes and lower level in bone marrow. Ref.3

Domain

The SET domain mediates interaction with WIZ.

Post-translational modification

Phosphorylated upon DNA damage, probably by ATM or ATR. Ref.11 Ref.12 Ref.13 Ref.14

Sequence similarities

Belongs to the histone-lysine methyltransferase family. Suvar3-9 subfamily.

Contains 7 ANK repeats.

Contains 1 post-SET domain.

Contains 1 pre-SET domain.

Contains 1 SET domain.

Caution

Ref.3 reported that while NG36 and G9a were originally thought to derive from two separate genes, all G9A transcripts also contain the in frame coding sequence of NG36.

It is uncertain whether Met-1 or Met-21 is the initiator methionine.

Sequence caution

The sequence AAD21811.1 differs from that shown. Reason: Erroneous gene model prediction.

The sequence AAD21812.1 differs from that shown. Reason: Erroneous gene model prediction.

The sequence BAB63294.1 differs from that shown. Reason: Erroneous gene model prediction.

The sequence BAB63295.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainANK repeat
Repeat
   LigandMetal-binding
S-adenosyl-L-methionine
Zinc
   Molecular functionChromatin regulator
Methyltransferase
Transferase
   PTMPhosphoprotein
   Technical term3D-structure
Gene Ontology (GO)
   Biological processchromatin modification

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentnucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionhistone-lysine N-methyltransferase activity

Inferred from electronic annotation. Source: EC

protein binding Ref.6

Non-traceable author statement. Source: UniProtKB

zinc ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Binary interactions

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Note: Additional isoforms seem to exist.
Isoform 1 (identifier: Q96KQ7-1)

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: Q96KQ7-2)

Also known as: NG36G9a-SPI;

The sequence of this isoform differs from the canonical sequence as follows:
     373-406: Missing.
Isoform 3 (identifier: Q96KQ7-3)

Also known as: NG36;

The sequence of this isoform differs from the canonical sequence as follows:
     195-202: PPVPEKRP → VSGMGEMG
     203-1210: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 12101210Histone-lysine N-methyltransferase, H3 lysine-9 specific 3
PRO_0000186068

Regions

Repeat649 – 67830ANK 1
Repeat684 – 71330ANK 2
Repeat717 – 74630ANK 3
Repeat750 – 78031ANK 4
Repeat784 – 81330ANK 5
Repeat817 – 84630ANK 6
Repeat850 – 87930ANK 7
Domain972 – 103564Pre-SET
Domain1037 – 1159123SET
Domain1164 – 118017Post-SET
Region1048 – 10503S-adenosyl-L-methionine binding
Region1112 – 11132S-adenosyl-L-methionine binding
Compositional bias2 – 1312Poly-Ala
Compositional bias160 – 1634Poly-Ala
Compositional bias300 – 32627Poly-Glu

Sites

Metal binding9741Zinc 1
Metal binding9741Zinc 2
Metal binding9761Zinc 1
Metal binding9801Zinc 1
Metal binding9801Zinc 3
Metal binding9851Zinc 1
Metal binding9871Zinc 2
Metal binding10171Zinc 2
Metal binding10171Zinc 3
Metal binding10211Zinc 2
Metal binding10231Zinc 3
Metal binding10271Zinc 3
Metal binding11151Zinc 4
Metal binding11681Zinc 4
Metal binding11701Zinc 4
Metal binding11751Zinc 4
Binding site10851S-adenosyl-L-methionine

Amino acid modifications

Modified residue1401Phosphoserine Ref.13 Ref.14
Modified residue1731Phosphoserine Ref.14
Modified residue2321Phosphoserine Ref.13 Ref.14
Modified residue2461Phosphoserine Ref.11 Ref.14
Modified residue5551Phosphothreonine By similarity
Modified residue5691Phosphoserine Ref.12
Modified residue12101Phosphothreonine Ref.14

Natural variations

Alternative sequence195 – 2028PPVPEKRP → VSGMGEMG in isoform 3.
VSP_002212
Alternative sequence203 – 12101008Missing in isoform 3.
VSP_002213
Alternative sequence373 – 40634Missing in isoform 2.
VSP_002211
Natural variant551T → N: dbSNP rs7887. Ref.3 Ref.2 Ref.5
VAR_027973
Natural variant11651Y → F: dbSNP rs13919.
VAR_027974

Experimental info

Sequence conflict1781P → S in CAC86666. Ref.3
Sequence conflict9851C → R in CAC86666. Ref.3
Sequence conflict9941C → R in CAA49491. Ref.6

Secondary structure

................................................ 1210
Helix Strand Turn

Details...

Sequences

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

Last modified October 17, 2006. Version 3.
Checksum: A6C5DC6B72801520

FASTA1,210132,370
        10         20         30         40         50         60 
MAAAAGAAAA AAAEGEAPAE MGALLLEKET RGATERVHGS LGDTPRSEET LPKATPDSLE 

        70         80         90        100        110        120 
PAGPSSPASV TVTVGDEGAD TPVGATPLIG DESENLEGDG DLRGGRILLG HATKSFPSSP 

       130        140        150        160        170        180 
SKGGSCPSRA KMSMTGAGKS PPSVQSLAMR LLSMPGAQGA AAAGSEPPPA TTSPEGQPKV 

       190        200        210        220        230        240 
HRARKTMSKP GNGQPPVPEK RPPEIQHFRM SDDVHSLGKV TSDLAKRRKL NSGGGLSEEL 

       250        260        270        280        290        300 
GSARRSGEVT LTKGDPGSLE EWETVVGDDF SLYYDSYSVD ERVDSDSKSE VEALTEQLSE 

       310        320        330        340        350        360 
EEEEEEEEEE EEEEEEEEEE EEEDEESGNQ SDRSGSSGRR KAKKKWRKDS PWVKPSRKRR 

       370        380        390        400        410        420 
KREPPRAKEP RGVNGVGSSG PSEYMEVPLG SLELPSEGTL SPNHAGVSND TSSLETERGF 

       430        440        450        460        470        480 
EELPLCSCRM EAPKIDRISE RAGHKCMATE SVDGELSGCN AAILKRETMR PSSRVALMVL 

       490        500        510        520        530        540 
CETHRARMVK HHCCPGCGYF CTAGTFLECH PDFRVAHRFH KACVSQLNGM VFCPHCGEDA 

       550        560        570        580        590        600 
SEAQEVTIPR GDGVTPPAGT AAPAPPPLSQ DVPGRADTSQ PSARMRGHGE PRRPPCDPLA 

       610        620        630        640        650        660 
DTIDSSGPSL TLPNGGCLSA VGLPLGPGRE ALEKALVIQE SERRKKLRFH PRQLYLSVKQ 

       670        680        690        700        710        720 
GELQKVILML LDNLDPNFQS DQQSKRTPLH AAAQKGSVEI CHVLLQAGAN INAVDKQQRT 

       730        740        750        760        770        780 
PLMEAVVNNH LEVARYMVQR GGCVYSKEED GSTCLHHAAK IGNLEMVSLL LSTGQVDVNA 

       790        800        810        820        830        840 
QDSGGWTPII WAAEHKHIEV IRMLLTRGAD VTLTDNEENI CLHWASFTGS AAIAEVLLNA 

       850        860        870        880        890        900 
RCDLHAVNYH GDTPLHIAAR ESYHDCVLLF LSRGANPELR NKEGDTAWDL TPERSDVWFA 

       910        920        930        940        950        960 
LQLNRKLRLG VGNRAIRTEK IICRDVARGY ENVPIPCVNG VDGEPCPEDY KYISENCETS 

       970        980        990       1000       1010       1020 
TMNIDRNITH LQHCTCVDDC SSSNCLCGQL SIRCWYDKDG RLLQEFNKIE PPLIFECNQA 

      1030       1040       1050       1060       1070       1080 
CSCWRNCKNR VVQSGIKVRL QLYRTAKMGW GVRALQTIPQ GTFICEYVGE LISDAEADVR 

      1090       1100       1110       1120       1130       1140 
EDDSYLFDLD NKDGEVYCID ARYYGNISRF INHLCDPNII PVRVFMLHQD LRFPRIAFFS 

      1150       1160       1170       1180       1190       1200 
SRDIRTGEEL GFDYGDRFWD IKSKYFTCQC GSEKCKHSAE AIALEQSRLA RLDPHPELLP 

      1210 
ELGSLPPVNT 

« Hide

Isoform 2 (NG36G9a-SPI).

Checksum: 887FC5E322B772B9
Show »

FASTA1,176129,019
Isoform 3 (NG36).

Checksum: 339618C3DA895788
Show »

FASTA20219,864

References

« Hide 'large scale' references
[1]"Analysis of the gene-dense major histocompatibility complex class III region and its comparison to mouse."
Xie T., Rowen L., Aguado B., Ahearn M.E., Madan A., Qin S., Campbell R.D., Hood L.
Genome Res. 13:2621-2636(2003) [PubMed: 14656967] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[2]"Homo sapiens 2,229,817bp genomic DNA of 6p21.3 HLA class I region."
Hirakawa M., Yamaguchi H., Imai K., Shimada J., Shiina S., Tamiya G., Oka A., Inoko H.
Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT ASN-55.
[3]"Novel NG36/G9a gene products encoded within the human and mouse MHC class III regions."
Brown S.E., Campbell R.D., Sanderson C.M.
Mamm. Genome 12:916-924(2001) [PubMed: 11707778] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), ALTERNATIVE SPLICING (ISOFORM 2), TISSUE SPECIFICITY, VARIANT ASN-55.
[4]"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: 14702039] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
Tissue: Salivary gland.
[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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 6-1210 (ISOFORM 1), VARIANT ASN-55.
Tissue: Muscle and Uterus.
[6]"The G9a gene in the human major histocompatibility complex encodes a novel protein containing ankyrin-like repeats."
Milner C.M., Campbell R.D.
Biochem. J. 290:811-818(1993) [PubMed: 8457211] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 195-1210, CHARACTERIZATION.
Tissue: Histiocytic lymphoma.
[7]"Set domain-containing protein, G9a, is a novel lysine-preferring mammalian histone methyltransferase with hyperactivity and specific selectivity to lysines 9 and 27 of histone H3."
Tachibana M., Sugimoto K., Fukushima T., Shinkai Y.
J. Biol. Chem. 276:25309-25317(2001) [PubMed: 11316813] [Abstract]
Cited for: ENZYME ACTIVITY, SUBCELLULAR LOCATION.
[8]"A complex with chromatin modifiers that occupies E2F- and Myc-responsive genes in G0 cells."
Ogawa H., Ishiguro K., Gaubatz S., Livingston D.M., Nakatani Y.
Science 296:1132-1136(2002) [PubMed: 12004135] [Abstract]
Cited for: IDENTIFICATION IN COMPLEX WITH E2F6; TFDP1; MAX; MGA; EUHMTASE1; CBX3; RING1; RNF2; MBLR; L3MBTL2 AND YAF2.
[9]"Gfi1b alters histone methylation at target gene promoters and sites of gamma-satellite containing heterochromatin."
Vassen L., Fiolka K., Moeroey T.
EMBO J. 25:2409-2419(2006) [PubMed: 16688220] [Abstract]
Cited for: INTERACTION WITH GFI1B.
[10]"Zinc finger protein Wiz links G9a/GLP histone methyltransferases to the co-repressor molecule CtBP."
Ueda J., Tachibana M., Ikura T., Shinkai Y.
J. Biol. Chem. 281:20120-20128(2006) [PubMed: 16702210] [Abstract]
Cited for: INTERACTION WITH WIZ AND EHMT1.
[11]"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: 16964243] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-246, MASS SPECTROMETRY.
Tissue: Epithelium.
[12]"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage."
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.
Science 316:1160-1166(2007) [PubMed: 17525332] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-569, MASS SPECTROMETRY.
[13]"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: 18220336] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-140 AND SER-232, MASS SPECTROMETRY.
[14]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-140; SER-173; SER-232; SER-246 AND THR-1210, MASS SPECTROMETRY.
[15]"The crystal structure of the SET domain of human euchromatic histone methyltransferase 2."
Structural genomics consortium (SGC)
Submitted (JAN-2007) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 913-1193 IN COMPLEX WITH S-ADENOSYL-L-HOMOCYSTEINE AND ZINC IONS.
+Additional computationally mapped references.

Cross-references

Sequence databases

AF134726 Genomic DNA. Translation: AAD21811.1. Sequence problems.
AF134726 Genomic DNA. Translation: AAD21812.1. Sequence problems.
BA000025 Genomic DNA. Translation: BAB63294.1. Sequence problems.
BA000025 Genomic DNA. Translation: BAB63295.1. Sequence problems.
AJ315532 mRNA. Translation: CAC86666.1.
AK056936 mRNA. Translation: BAB71314.1.
BC002686 mRNA. Translation: AAH02686.2. Different initiation.
BC009351 mRNA. Translation: AAH09351.1. Different initiation.
BC018718 mRNA. Translation: AAH18718.1. Different initiation.
BC020970 mRNA. Translation: AAH20970.2. Different initiation.
X69838 mRNA. Translation: CAA49491.1. Different initiation.
IPIIPI00096972.
IPI00220795.
IPI00220796.
RefSeqNP_006700.3.
NP_079532.5.
UniGeneHs.709218

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
2O8JX-ray1.80A/B/C/D913-1193[»]
3DM1X-ray2.40B/D/F/H179-190[»]
ModBaseSearch...

Protein-protein interaction databases

IntActQ96KQ7. 17 interactions.

PTM databases

PhosphoSiteQ96KQ7.

Proteomic databases

PRIDEQ96KQ7.

Genome annotation databases

EnsemblENSG00000137324. Homo sapiens. [Contig view]
ENSG00000204371. Homo sapiens. [Contig view]
ENSG00000206376. Homo sapiens. [Contig view]
GeneID10919.
KEGGhsa:10919.

Organism-specific databases

GeneCardsGC06M031956.
H-InvDBHIX0005738.
HIX0025250.
HIX0057920.
HIX0058043.
HIX0058094.
HGNCHGNC:14129. EHMT2.
MIM604599. gene.
PharmGKBPA25267.
GenAtlasSearch...

Phylogenomic databases

HOVERGENQ96KQ7.

Enzyme and pathway databases

BRENDA2.1.1.43. 247.
Pathway_Interaction_DBar_tf_pathway. Regulation of Androgen receptor activity.

Gene expression databases

ArrayExpressQ96KQ7.
BgeeQ96KQ7.
CleanExHS_EHMT2.
GermOnlineENSG00000204371. Homo sapiens.

Family and domain databases

InterProIPR002110. ANK.
IPR003616. Post-SET_Zn_bd.
IPR007728. Pre-SET_Zn_bd.
IPR003606. Pre-SET_Zn_bd_sub.
IPR001214. SET.
[Graphical view]
Gene3DG3DSA:1.25.40.20. ANK. 1 hit.
PfamPF00023. Ank. 6 hits.
PF05033. Pre-SET. 1 hit.
PF00856. SET. 1 hit.
[Graphical view]
SMARTSM00248. ANK. 6 hits.
SM00508. PostSET. 1 hit.
SM00468. PreSET. 1 hit.
SM00317. SET. 1 hit.
[Graphical view]
PROSITEPS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 5 hits.
PS50868. POST_SET. False negative.
PS50867. PRE_SET. 1 hit.
PS50280. SET. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio41475.
SOURCESearch...

Entry information

Entry nameEHMT2_HUMAN
AccessionPrimary (citable) accession number: Q96KQ7
Secondary accession number(s): Q14349 expand/collapse secondary AC list , Q6PK06, Q96MH5, Q96QD0, Q9UQL8, Q9Y331
Entry history
Integrated into UniProtKB/Swiss-Prot: November 15, 2002
Last sequence update: October 17, 2006
Last modified: June 16, 2009
This is version 93 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

Human chromosome 6

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

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents