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Protein

Ribonuclease H2 subunit A

Gene

RNASEH2A

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

Functioni

Catalytic subunit of RNase HII, an endonuclease that specifically degrades the RNA of RNA:DNA hybrids. Participates in DNA replication, possibly by mediating the removal of lagging-strand Okazaki fragment RNA primers during DNA replication. Mediates the excision of single ribonucleotides from DNA:RNA duplexes.2 Publications

Catalytic activityi

Endonucleolytic cleavage to 5'-phosphomonoester.1 Publication

Cofactori

Mn2+By similarity, Mg2+By similarityNote: Manganese or magnesium. Binds 1 divalent metal ion per monomer in the absence of substrate. May bind a second metal ion after substrate binding.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi34 – 341Divalent metal cationBy similarity
Metal bindingi35 – 351Divalent metal cationBy similarity
Metal bindingi141 – 1411Divalent metal cationBy similarity

GO - Molecular functioni

  1. metal ion binding Source: UniProtKB-KW
  2. ribonuclease activity Source: ProtInc
  3. RNA binding Source: InterPro
  4. RNA-DNA hybrid ribonuclease activity Source: UniProtKB

GO - Biological processi

  1. DNA replication Source: UniProtKB
  2. mismatch repair Source: MGI
  3. RNA catabolic process Source: UniProtKB
  4. RNA phosphodiester bond hydrolysis Source: GOC
  5. RNA phosphodiester bond hydrolysis, endonucleolytic Source: GOC
Complete GO annotation...

Keywords - Molecular functioni

Endonuclease, Hydrolase, Nuclease

Keywords - Ligandi

Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Ribonuclease H2 subunit A (EC:3.1.26.4)
Short name:
RNase H2 subunit A
Alternative name(s):
Aicardi-Goutieres syndrome 4 protein
Short name:
AGS4
RNase H(35)
Ribonuclease HI large subunit
Short name:
RNase HI large subunit
Ribonuclease HI subunit A
Gene namesi
Name:RNASEH2A
Synonyms:RNASEHI, RNHIA
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 19

Organism-specific databases

HGNCiHGNC:18518. RNASEH2A.

Subcellular locationi

Nucleus Curated

GO - Cellular componenti

  1. nucleus Source: UniProtKB-SubCell
  2. ribonuclease H2 complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Involvement in diseasei

Aicardi-Goutieres syndrome 43 Publications

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA form of Aicardi-Goutieres syndrome, a genetically heterogeneous disease characterized by cerebral atrophy, leukoencephalopathy, intracranial calcifications, chronic cerebrospinal fluid (CSF) lymphocytosis, increased CSF alpha-interferon, and negative serologic investigations for common prenatal infection. Clinical features as thrombocytopenia, hepatosplenomegaly and elevated hepatic transaminases along with intermittent fever may erroneously suggest an infective process. Severe neurological dysfunctions manifest in infancy as progressive microcephaly, spasticity, dystonic posturing and profound psychomotor retardation. Death often occurs in early childhood.

See also OMIM:610333
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti2 – 32DL → YP in AGS4.
VAR_070623
Natural varianti37 – 371G → S in AGS4; strongly impairs enzyme activity but not interaction with RNASEH2B and RNASEH2C. 2 Publications
VAR_027377
Natural varianti108 – 1081R → W in AGS4. 1 Publication
VAR_070625
Natural varianti186 – 1861R → W in AGS4. 2 Publications
VAR_070626
Natural varianti230 – 2301F → L in AGS4. 1 Publication
VAR_070628
Natural varianti235 – 2351R → Q in AGS4. 1 Publication
VAR_070629
Natural varianti240 – 2401T → M in AGS4. 1 Publication
VAR_070630
Natural varianti291 – 2911R → H in AGS4. 1 Publication
VAR_070632

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi67 – 671D → A: Loss of enzyme activity. 1 Publication
Mutagenesisi69 – 691K → A: Strongly reduced enzyme activity. 1 Publication
Mutagenesisi112 – 1121N → A: Reduced enzyme activity. 1 Publication
Mutagenesisi210 – 2101Y → A: Strongly reduced enzyme activity. 1 Publication
Mutagenesisi210 – 2101Y → F: Loss of enzyme activity. 1 Publication
Mutagenesisi240 – 2401T → A: Strongly reduced enzyme activity. 1 Publication

Keywords - Diseasei

Aicardi-Goutieres syndrome, Disease mutation

Organism-specific databases

MIMi610333. phenotype.
Orphaneti51. Aicardi-Goutieres syndrome.
PharmGKBiPA38565.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 299299Ribonuclease H2 subunit APRO_0000111710Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine2 Publications
Modified residuei204 – 2041Phosphothreonine1 Publication
Modified residuei216 – 2161Phosphothreonine1 Publication
Modified residuei257 – 2571PhosphoserineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiO75792.
PaxDbiO75792.
PRIDEiO75792.

PTM databases

PhosphoSiteiO75792.

Expressioni

Gene expression databases

BgeeiO75792.
CleanExiHS_RNASEH2A.
GenevestigatoriO75792.

Organism-specific databases

HPAiHPA042692.
HPA051652.

Interactioni

Subunit structurei

The RNase H2 complex is a heterotrimer composed of the catalytic subunit RNASEH2A and the non-catalytic subunits RNASEH2B and RNASEH2C.1 Publication

Protein-protein interaction databases

BioGridi115789. 12 interactions.
STRINGi9606.ENSP00000221486.

Structurei

Secondary structure

1
299
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi4 – 74Combined sources
Beta strandi15 – 173Combined sources
Helixi23 – 264Combined sources
Beta strandi29 – 368Combined sources
Beta strandi41 – 433Combined sources
Beta strandi45 – 5410Combined sources
Helixi57 – 626Combined sources
Helixi73 – 8412Combined sources
Beta strandi86 – 883Combined sources
Beta strandi90 – 967Combined sources
Helixi98 – 1058Combined sources
Beta strandi107 – 1093Combined sources
Helixi113 – 13018Combined sources
Beta strandi135 – 14410Combined sources
Helixi146 – 15611Combined sources
Beta strandi160 – 1667Combined sources
Helixi168 – 1714Combined sources
Helixi173 – 19119Combined sources
Helixi214 – 2229Combined sources
Turni226 – 2283Combined sources
Helixi239 – 24810Combined sources
Helixi286 – 2905Combined sources
Beta strandi293 – 2953Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3P56X-ray4.06A/D1-299[»]
3PUFX-ray3.10A/D/G/J/M/P1-299[»]
ProteinModelPortaliO75792.
SMRiO75792. Positions 2-299.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO75792.

Family & Domainsi

Sequence similaritiesi

Belongs to the RNase HII family. Eukaryotic subfamily.Curated

Phylogenomic databases

eggNOGiCOG0164.
GeneTreeiENSGT00390000010768.
HOGENOMiHOG000100290.
HOVERGENiHBG023585.
InParanoidiO75792.
KOiK10743.
OMAiLNEVSMD.
OrthoDBiEOG7KM5T4.
PhylomeDBiO75792.
TreeFamiTF314302.

Family and domain databases

Gene3Di1.10.10.460. 1 hit.
3.30.420.10. 1 hit.
InterProiIPR004649. RNase_H2_suA.
IPR001352. RNase_HII/HIII.
IPR024567. RNase_HII/HIII_dom.
IPR023160. RNase_HII_hlx-loop-hlx_cap_dom.
IPR012337. RNaseH-like_dom.
[Graphical view]
PANTHERiPTHR10954. PTHR10954. 1 hit.
PfamiPF01351. RNase_HII. 1 hit.
[Graphical view]
SUPFAMiSSF53098. SSF53098. 1 hit.
TIGRFAMsiTIGR00729. TIGR00729. 1 hit.

Sequencei

Sequence statusi: Complete.

O75792-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MDLSELERDN TGRCRLSSPV PAVCRKEPCV LGVDEAGRGP VLGPMVYAIC
60 70 80 90 100
YCPLPRLADL EALKVADSKT LLESERERLF AKMEDTDFVG WALDVLSPNL
110 120 130 140 150
ISTSMLGRVK YNLNSLSHDT ATGLIQYALD QGVNVTQVFV DTVGMPETYQ
160 170 180 190 200
ARLQQSFPGI EVTVKAKADA LYPVVSAASI CAKVARDQAV KKWQFVEKLQ
210 220 230 240 250
DLDTDYGSGY PNDPKTKAWL KEHVEPVFGF PQFVRFSWRT AQTILEKEAE
260 270 280 290
DVIWEDSASE NQEGLRKITS YFLNEGSQAR PRSSHRYFLE RGLESATSL
Length:299
Mass (Da):33,395
Last modified:May 15, 2002 - v2
Checksum:i34992FE85130157B
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti152 – 1521R → Q in CAB09725. (PubMed:9789007)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti2 – 32DL → YP in AGS4.
VAR_070623
Natural varianti37 – 371G → S in AGS4; strongly impairs enzyme activity but not interaction with RNASEH2B and RNASEH2C. 2 Publications
VAR_027377
Natural varianti99 – 991N → D.1 Publication
VAR_070624
Natural varianti108 – 1081R → W in AGS4. 1 Publication
VAR_070625
Natural varianti186 – 1861R → W in AGS4. 2 Publications
VAR_070626
Natural varianti202 – 2021L → S.1 Publication
Corresponds to variant rs7247284 [ dbSNP | Ensembl ].
VAR_024617
Natural varianti205 – 2051D → E.1 Publication
VAR_070627
Natural varianti230 – 2301F → L in AGS4. 1 Publication
VAR_070628
Natural varianti235 – 2351R → Q in AGS4. 1 Publication
VAR_070629
Natural varianti240 – 2401T → M in AGS4. 1 Publication
VAR_070630
Natural varianti258 – 2581A → G.
Corresponds to variant rs15389 [ dbSNP | Ensembl ].
VAR_027378
Natural varianti260 – 2601E → G.1 Publication
VAR_070631
Natural varianti291 – 2911R → H in AGS4. 1 Publication
VAR_070632

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z97029 mRNA. Translation: CAB09725.1.
AK315327 mRNA. Translation: BAG37728.1.
CH471106 Genomic DNA. Translation: EAW84313.1.
BC011748 mRNA. Translation: AAH11748.1.
CCDSiCCDS12282.1.
RefSeqiNP_006388.2. NM_006397.2.
UniGeneiHs.532851.

Genome annotation databases

EnsembliENST00000221486; ENSP00000221486; ENSG00000104889.
GeneIDi10535.
KEGGihsa:10535.
UCSCiuc002mvg.1. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z97029 mRNA. Translation: CAB09725.1.
AK315327 mRNA. Translation: BAG37728.1.
CH471106 Genomic DNA. Translation: EAW84313.1.
BC011748 mRNA. Translation: AAH11748.1.
CCDSiCCDS12282.1.
RefSeqiNP_006388.2. NM_006397.2.
UniGeneiHs.532851.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3P56X-ray4.06A/D1-299[»]
3PUFX-ray3.10A/D/G/J/M/P1-299[»]
ProteinModelPortaliO75792.
SMRiO75792. Positions 2-299.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115789. 12 interactions.
STRINGi9606.ENSP00000221486.

PTM databases

PhosphoSiteiO75792.

Proteomic databases

MaxQBiO75792.
PaxDbiO75792.
PRIDEiO75792.

Protocols and materials databases

DNASUi10535.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000221486; ENSP00000221486; ENSG00000104889.
GeneIDi10535.
KEGGihsa:10535.
UCSCiuc002mvg.1. human.

Organism-specific databases

CTDi10535.
GeneCardsiGC19P012918.
GeneReviewsiRNASEH2A.
HGNCiHGNC:18518. RNASEH2A.
HPAiHPA042692.
HPA051652.
MIMi606034. gene.
610333. phenotype.
neXtProtiNX_O75792.
Orphaneti51. Aicardi-Goutieres syndrome.
PharmGKBiPA38565.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0164.
GeneTreeiENSGT00390000010768.
HOGENOMiHOG000100290.
HOVERGENiHBG023585.
InParanoidiO75792.
KOiK10743.
OMAiLNEVSMD.
OrthoDBiEOG7KM5T4.
PhylomeDBiO75792.
TreeFamiTF314302.

Miscellaneous databases

EvolutionaryTraceiO75792.
GeneWikiiRNASEH2A.
GenomeRNAii10535.
NextBioi39969.
PROiO75792.
SOURCEiSearch...

Gene expression databases

BgeeiO75792.
CleanExiHS_RNASEH2A.
GenevestigatoriO75792.

Family and domain databases

Gene3Di1.10.10.460. 1 hit.
3.30.420.10. 1 hit.
InterProiIPR004649. RNase_H2_suA.
IPR001352. RNase_HII/HIII.
IPR024567. RNase_HII/HIII_dom.
IPR023160. RNase_HII_hlx-loop-hlx_cap_dom.
IPR012337. RNaseH-like_dom.
[Graphical view]
PANTHERiPTHR10954. PTHR10954. 1 hit.
PfamiPF01351. RNase_HII. 1 hit.
[Graphical view]
SUPFAMiSSF53098. SSF53098. 1 hit.
TIGRFAMsiTIGR00729. TIGR00729. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning of the cDNA encoding the large subunit of human RNase HI, a homologue of the prokaryotic RNase HII."
    Frank P., Braunshofer-Reiter C., Wintersberger U., Grimm R., Buesen W.
    Proc. Natl. Acad. Sci. U.S.A. 95:12872-12877(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  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].
    Tissue: Thalamus.
  3. 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].
    Tissue: Brain.
  5. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-204 AND THR-216, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  6. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  7. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. "The structural and biochemical characterization of human RNase H2 complex reveals the molecular basis for substrate recognition and Aicardi-Goutieres syndrome defects."
    Figiel M., Chon H., Cerritelli S.M., Cybulska M., Crouch R.J., Nowotny M.
    J. Biol. Chem. 286:10540-10550(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS), SUBUNIT, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, MUTAGENESIS OF ASP-67; LYS-69; ASN-112; TYR-210 AND THR-240.
  10. Cited for: VARIANT AGS4 SER-37, CHARACTERIZATION OF VARIANT AGS4 SER-37, FUNCTION, INTERACTION WITH RNASEH2B AND RNASEH2C.
  11. "Clinical and molecular phenotype of Aicardi-Goutieres syndrome."
    Rice G., Patrick T., Parmar R., Taylor C.F., Aeby A., Aicardi J., Artuch R., Montalto S.A., Bacino C.A., Barroso B., Baxter P., Benko W.S., Bergmann C., Bertini E., Biancheri R., Blair E.M., Blau N., Bonthron D.T.
    , Briggs T., Brueton L.A., Brunner H.G., Burke C.J., Carr I.M., Carvalho D.R., Chandler K.E., Christen H.J., Corry P.C., Cowan F.M., Cox H., D'Arrigo S., Dean J., De Laet C., De Praeter C., Dery C., Ferrie C.D., Flintoff K., Frints S.G., Garcia-Cazorla A., Gener B., Goizet C., Goutieres F., Green A.J., Guet A., Hamel B.C., Hayward B.E., Heiberg A., Hennekam R.C., Husson M., Jackson A.P., Jayatunga R., Jiang Y.H., Kant S.G., Kao A., King M.D., Kingston H.M., Klepper J., van der Knaap M.S., Kornberg A.J., Kotzot D., Kratzer W., Lacombe D., Lagae L., Landrieu P.G., Lanzi G., Leitch A., Lim M.J., Livingston J.H., Lourenco C.M., Lyall E.G., Lynch S.A., Lyons M.J., Marom D., McClure J.P., McWilliam R., Melancon S.B., Mewasingh L.D., Moutard M.L., Nischal K.K., Ostergaard J.R., Prendiville J., Rasmussen M., Rogers R.C., Roland D., Rosser E.M., Rostasy K., Roubertie A., Sanchis A., Schiffmann R., Scholl-Burgi S., Seal S., Shalev S.A., Corcoles C.S., Sinha G.P., Soler D., Spiegel R., Stephenson J.B., Tacke U., Tan T.Y., Till M., Tolmie J.L., Tomlin P., Vagnarelli F., Valente E.M., Van Coster R.N., Van der Aa N., Vanderver A., Vles J.S., Voit T., Wassmer E., Weschke B., Whiteford M.L., Willemsen M.A., Zankl A., Zuberi S.M., Orcesi S., Fazzi E., Lebon P., Crow Y.J.
    Am. J. Hum. Genet. 81:713-725(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS AGS4 SER-37; TRP-108; TRP-186; LEU-230; GLN-235; MET-240 AND HIS-291, VARIANTS ASP-99; SER-202; GLU-205 AND GLY-260.
  12. Cited for: VARIANTS AGS4 2-TYR-PRO-3 AND TRP-186.

Entry informationi

Entry nameiRNH2A_HUMAN
AccessioniPrimary (citable) accession number: O75792
Secondary accession number(s): B2RCY1, Q96F11
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: May 15, 2002
Last modified: January 7, 2015
This is version 137 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 19
    Human chromosome 19: 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.