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Protein

Alpha-ketoglutarate-dependent dioxygenase alkB homolog 2

Gene

ALKBH2

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

Functioni

Dioxygenase that repairs alkylated DNA and RNA containing 1-methyladenine and 3-methylcytosine by oxidative demethylation. Can also repair alkylated DNA containing 1-ethenoadenine (in vitro). Has strong preference for double-stranded DNA. Has low efficiency with single-stranded substrates. Requires molecular oxygen, alpha-ketoglutarate and iron.5 Publications

Catalytic activityi

DNA-base-CH3 + 2-oxoglutarate + O2 = DNA-base + formaldehyde + succinate + CO2.

Cofactori

Fe2+2 PublicationsPROSITE-ProRule annotationNote: Binds 1 Fe2+ ion per subunit.2 PublicationsPROSITE-ProRule annotation

Enzyme regulationi

Activated by ascorbate and magnesium ions.2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi171 – 1711Iron; catalytic
Metal bindingi173 – 1731Iron; catalytic
Binding sitei174 – 1741Substrate
Metal bindingi236 – 2361Iron; catalytic

GO - Molecular functioni

  1. cytosine C-5 DNA demethylase activity Source: UniProtKB
  2. DNA-N1-methyladenine dioxygenase activity Source: UniProtKB
  3. ferrous iron binding Source: UniProtKB

GO - Biological processi

  1. DNA dealkylation involved in DNA repair Source: UniProtKB
  2. DNA demethylation Source: BHF-UCL
  3. DNA repair Source: Reactome
  4. oxidative demethylation Source: BHF-UCL
  5. oxidative DNA demethylation Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Dioxygenase, Oxidoreductase

Keywords - Biological processi

DNA damage, DNA repair

Keywords - Ligandi

Iron, Magnesium, Metal-binding

Enzyme and pathway databases

ReactomeiREACT_526. ABH2 mediated Reversal of Alkylation Damage.

Names & Taxonomyi

Protein namesi
Recommended name:
Alpha-ketoglutarate-dependent dioxygenase alkB homolog 2 (EC:1.14.11.33)
Alternative name(s):
Alkylated DNA repair protein alkB homolog 2
DNA oxidative demethylase ALKBH2
Oxy DC1
Gene namesi
Name:ALKBH2
Synonyms:ABH2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 12

Organism-specific databases

HGNCiHGNC:32487. ALKBH2.

Subcellular locationi

Nucleus 2 Publications
Note: Detected in replication foci during S-phase.

GO - Cellular componenti

  1. microtubule cytoskeleton Source: HPA
  2. nucleoplasm Source: HPA
  3. nucleus Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi173 – 1731D → A: Loss of activity. 1 Publication
Mutagenesisi236 – 2361H → A: Reduced activity. 1 Publication

Organism-specific databases

PharmGKBiPA143485292.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 261261Alpha-ketoglutarate-dependent dioxygenase alkB homolog 2PRO_0000239275Add
BLAST

Proteomic databases

MaxQBiQ6NS38.
PaxDbiQ6NS38.
PRIDEiQ6NS38.

PTM databases

PhosphoSiteiQ6NS38.

Expressioni

Tissue specificityi

Detected in colon, small intestine, ovary, testis, prostate, skeletal muscle, heart, liver and urinary bladder.2 Publications

Gene expression databases

BgeeiQ6NS38.
CleanExiHS_ALKBH2.
ExpressionAtlasiQ6NS38. baseline and differential.
GenevestigatoriQ6NS38.

Organism-specific databases

HPAiCAB011198.

Interactioni

Protein-protein interaction databases

BioGridi125741. 3 interactions.
IntActiQ6NS38. 1 interaction.
STRINGi9606.ENSP00000343021.

Structurei

Secondary structure

1
261
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi58 – 625Combined sources
Beta strandi65 – 717Combined sources
Helixi75 – 8814Combined sources
Helixi94 – 974Combined sources
Beta strandi98 – 1014Combined sources
Beta strandi104 – 1074Combined sources
Beta strandi109 – 1168Combined sources
Beta strandi122 – 1243Combined sources
Beta strandi127 – 1293Combined sources
Helixi136 – 14914Combined sources
Beta strandi154 – 16310Combined sources
Beta strandi168 – 1714Combined sources
Beta strandi176 – 1783Combined sources
Beta strandi184 – 1918Combined sources
Beta strandi193 – 1997Combined sources
Helixi200 – 2023Combined sources
Beta strandi204 – 2063Combined sources
Beta strandi214 – 2185Combined sources
Beta strandi222 – 2276Combined sources
Helixi230 – 2334Combined sources
Beta strandi234 – 2385Combined sources
Beta strandi248 – 2547Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3BTXX-ray2.00A56-258[»]
3BTYX-ray2.35A56-258[»]
3BTZX-ray3.00A57-258[»]
3BU0X-ray2.50A56-258[»]
3BUCX-ray2.59A56-258[»]
3H8OX-ray2.50A56-261[»]
3H8RX-ray1.77A56-261[»]
3H8XX-ray2.50A56-261[»]
3RZGX-ray1.62A56-261[»]
3RZHX-ray2.25A56-261[»]
3RZJX-ray2.50A56-261[»]
3RZKX-ray2.78A56-261[»]
3RZLX-ray2.60A/D56-261[»]
3RZMX-ray3.06A56-260[»]
3S57X-ray1.60A56-258[»]
3S5AX-ray1.70A56-258[»]
4MG2X-ray2.30A56-258[»]
4MGTX-ray2.60A56-258[»]
ProteinModelPortaliQ6NS38.
SMRiQ6NS38. Positions 56-258.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ6NS38.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini152 – 257106Fe2OG dioxygenasePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni102 – 1043Substrate binding
Regioni122 – 1243Substrate binding
Regioni159 – 1613Alpha-ketoglutarate binding
Regioni248 – 2547Alpha-ketoglutarate binding

Sequence similaritiesi

Belongs to the alkB family.Curated
Contains 1 Fe2OG dioxygenase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG3145.
GeneTreeiENSGT00530000063618.
HOGENOMiHOG000263606.
HOVERGENiHBG080832.
InParanoidiQ6NS38.
KOiK10859.
OMAiQATYGDT.
OrthoDBiEOG77T159.
PhylomeDBiQ6NS38.
TreeFamiTF331732.

Family and domain databases

Gene3Di2.60.120.590. 1 hit.
InterProiIPR027450. AlkB-like.
IPR005123. Oxoglu/Fe-dep_dioxygenase.
[Graphical view]
PfamiPF13532. 2OG-FeII_Oxy_2. 1 hit.
[Graphical view]
PROSITEiPS51471. FE2OG_OXY. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q6NS38-1) [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

        10         20         30         40         50
MDRFLVKGAQ GGLLRKQEEQ EPTGEEPAVL GGDKESTRKR PRREAPGNGG
60 70 80 90 100
HSAGPSWRHI RAEGLDCSYT VLFGKAEADE IFQELEKEVE YFTGALARVQ
110 120 130 140 150
VFGKWHSVPR KQATYGDAGL TYTFSGLTLS PKPWIPVLER IRDHVSGVTG
160 170 180 190 200
QTFNFVLINR YKDGCDHIGE HRDDERELAP GSPIASVSFG ACRDFVFRHK
210 220 230 240 250
DSRGKSPSRR VAVVRLPLAH GSLLMMNHPT NTHWYHSLPV RKKVLAPRVN
260
LTFRKILLTK K
Length:261
Mass (Da):29,322
Last modified:July 5, 2004 - v1
Checksum:iA376E13F92621A01
GO
Isoform 2 (identifier: Q6NS38-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     95-261: ALARVQVFGK...TFRKILLTKK → IKMAVTTSGS...SGCRWPTGAY

Note: No experimental confirmation available.

Show »
Length:157
Mass (Da):17,083
Checksum:iCB86433F4323248A
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti43 – 431R → G in AAV28301. 1 PublicationCurated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti203 – 2031R → H.
Corresponds to variant rs33962311 [ dbSNP | Ensembl ].
VAR_048223

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei95 – 261167ALARV…LLTKK → IKMAVTTSGSTEMMKENWPL GAPLPLSPSVPAETLSSGIR IPVGKAPPGGWRWSGCRWPT GAY in isoform 2. 1 PublicationVSP_042923Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY754389 mRNA. Translation: AAV28301.1.
AB277859 mRNA. Translation: BAF56576.1.
AC011596 Genomic DNA. No translation available.
BC070489 mRNA. Translation: AAH70489.1.
CCDSiCCDS31897.1. [Q6NS38-1]
CCDS55883.1. [Q6NS38-2]
RefSeqiNP_001001655.1. NM_001001655.2. [Q6NS38-1]
NP_001138846.1. NM_001145374.1. [Q6NS38-1]
NP_001138847.1. NM_001145375.1. [Q6NS38-1]
NP_001192108.1. NM_001205179.1. [Q6NS38-2]
NP_001192109.1. NM_001205180.1. [Q6NS38-2]
XP_005253892.1. XM_005253835.2. [Q6NS38-1]
XP_005253893.1. XM_005253836.1. [Q6NS38-2]
UniGeneiHs.374458.

Genome annotation databases

EnsembliENST00000343075; ENSP00000343021; ENSG00000189046. [Q6NS38-1]
ENST00000429722; ENSP00000398181; ENSG00000189046. [Q6NS38-1]
ENST00000440112; ENSP00000399820; ENSG00000189046. [Q6NS38-2]
ENST00000619381; ENSP00000478765; ENSG00000189046. [Q6NS38-2]
GeneIDi121642.
KEGGihsa:121642.
UCSCiuc001tnx.2. human. [Q6NS38-1]
uc009zvd.2. human. [Q6NS38-2]

Polymorphism databases

DMDMi74736661.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY754389 mRNA. Translation: AAV28301.1.
AB277859 mRNA. Translation: BAF56576.1.
AC011596 Genomic DNA. No translation available.
BC070489 mRNA. Translation: AAH70489.1.
CCDSiCCDS31897.1. [Q6NS38-1]
CCDS55883.1. [Q6NS38-2]
RefSeqiNP_001001655.1. NM_001001655.2. [Q6NS38-1]
NP_001138846.1. NM_001145374.1. [Q6NS38-1]
NP_001138847.1. NM_001145375.1. [Q6NS38-1]
NP_001192108.1. NM_001205179.1. [Q6NS38-2]
NP_001192109.1. NM_001205180.1. [Q6NS38-2]
XP_005253892.1. XM_005253835.2. [Q6NS38-1]
XP_005253893.1. XM_005253836.1. [Q6NS38-2]
UniGeneiHs.374458.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3BTXX-ray2.00A56-258[»]
3BTYX-ray2.35A56-258[»]
3BTZX-ray3.00A57-258[»]
3BU0X-ray2.50A56-258[»]
3BUCX-ray2.59A56-258[»]
3H8OX-ray2.50A56-261[»]
3H8RX-ray1.77A56-261[»]
3H8XX-ray2.50A56-261[»]
3RZGX-ray1.62A56-261[»]
3RZHX-ray2.25A56-261[»]
3RZJX-ray2.50A56-261[»]
3RZKX-ray2.78A56-261[»]
3RZLX-ray2.60A/D56-261[»]
3RZMX-ray3.06A56-260[»]
3S57X-ray1.60A56-258[»]
3S5AX-ray1.70A56-258[»]
4MG2X-ray2.30A56-258[»]
4MGTX-ray2.60A56-258[»]
ProteinModelPortaliQ6NS38.
SMRiQ6NS38. Positions 56-258.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi125741. 3 interactions.
IntActiQ6NS38. 1 interaction.
STRINGi9606.ENSP00000343021.

Chemistry

DrugBankiDB00126. Vitamin C.

PTM databases

PhosphoSiteiQ6NS38.

Polymorphism databases

DMDMi74736661.

Proteomic databases

MaxQBiQ6NS38.
PaxDbiQ6NS38.
PRIDEiQ6NS38.

Protocols and materials databases

DNASUi121642.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000343075; ENSP00000343021; ENSG00000189046. [Q6NS38-1]
ENST00000429722; ENSP00000398181; ENSG00000189046. [Q6NS38-1]
ENST00000440112; ENSP00000399820; ENSG00000189046. [Q6NS38-2]
ENST00000619381; ENSP00000478765; ENSG00000189046. [Q6NS38-2]
GeneIDi121642.
KEGGihsa:121642.
UCSCiuc001tnx.2. human. [Q6NS38-1]
uc009zvd.2. human. [Q6NS38-2]

Organism-specific databases

CTDi121642.
GeneCardsiGC12M109525.
HGNCiHGNC:32487. ALKBH2.
HPAiCAB011198.
MIMi610602. gene.
neXtProtiNX_Q6NS38.
PharmGKBiPA143485292.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG3145.
GeneTreeiENSGT00530000063618.
HOGENOMiHOG000263606.
HOVERGENiHBG080832.
InParanoidiQ6NS38.
KOiK10859.
OMAiQATYGDT.
OrthoDBiEOG77T159.
PhylomeDBiQ6NS38.
TreeFamiTF331732.

Enzyme and pathway databases

ReactomeiREACT_526. ABH2 mediated Reversal of Alkylation Damage.

Miscellaneous databases

EvolutionaryTraceiQ6NS38.
GenomeRNAii121642.
NextBioi80790.
PROiQ6NS38.
SOURCEiSearch...

Gene expression databases

BgeeiQ6NS38.
CleanExiHS_ALKBH2.
ExpressionAtlasiQ6NS38. baseline and differential.
GenevestigatoriQ6NS38.

Family and domain databases

Gene3Di2.60.120.590. 1 hit.
InterProiIPR027450. AlkB-like.
IPR005123. Oxoglu/Fe-dep_dioxygenase.
[Graphical view]
PfamiPF13532. 2OG-FeII_Oxy_2. 1 hit.
[Graphical view]
PROSITEiPS51471. FE2OG_OXY. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and expression of human 2OG-Fe(II) oxy DC1."
    Lin Y., Xie Y., Mao Y.
    Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  2. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    Tissue: Testis.
  3. "The finished DNA sequence of human chromosome 12."
    Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.
    , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
    Nature 440:346-351(2006) [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).
    Tissue: Skin.
  5. Cited for: FUNCTION, ENZYME REGULATION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  6. "Human and bacterial oxidative demethylases repair alkylation damage in both RNA and DNA."
    Aas P.A., Otterlei M., Falnes P.O., Vaagboe C.B., Skorpen F., Akbari M., Sundheim O., Bjoeraas M., Slupphaug G., Seeberg E., Krokan H.E.
    Nature 421:859-863(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  7. "Repair of methylation damage in DNA and RNA by mammalian AlkB homologues."
    Lee D.-H., Jin S.-G., Cai S., Chen Y., Pfeifer G.P., O'Connor T.R.
    J. Biol. Chem. 280:39448-39459(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF ASP-173 AND HIS-236, TISSUE SPECIFICITY.
  8. Cited for: FUNCTION, ENZYME REGULATION, COFACTOR.
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "Crystal structures of DNA/RNA repair enzymes AlkB and ABH2 bound to dsDNA."
    Yang C.G., Yi C., Duguid E.M., Sullivan C.T., Jian X., Rice P.A., He C.
    Nature 452:961-965(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 56-258 IN COMPLEXES WITH DS-DNA; ALPHA-KETOGLUTARATE AND METAL IONS, FUNCTION, COFACTOR.
  11. "Structure determination of DNA methylation lesions N1-meA and N3-meC in duplex DNA using a cross-linked protein-DNA system."
    Lu L., Yi C., Jian X., Zheng G., He C.
    Nucleic Acids Res. 38:4415-4425(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.77 ANGSTROMS) OF 56-261 IN COMPLEXES WITH DOUBLE-STRANDED DNA CONTAINING 1-METHYLADENINE OR 3-METHYLCYTOSINE.

Entry informationi

Entry nameiALKB2_HUMAN
AccessioniPrimary (citable) accession number: Q6NS38
Secondary accession number(s): A4PET2, Q5XLE3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2006
Last sequence update: July 5, 2004
Last modified: February 4, 2015
This is version 98 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 12
    Human chromosome 12: 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.