Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

O75792

- RNH2A_HUMAN

UniProt

O75792 - RNH2A_HUMAN

Protein

Ribonuclease H2 subunit A

Gene

RNASEH2A

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 134 (01 Oct 2014)
      Sequence version 2 (15 May 2002)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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

    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.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

    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

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    Aicardi-Goutieres syndrome 4 (AGS4) [MIM:610333]: A 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.3 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    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. 7 interactions.
    STRINGi9606.ENSP00000221486.

    Structurei

    Secondary structure

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

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    HOGENOMiHOG000100290.
    HOVERGENiHBG023585.
    InParanoidiO75792.
    KOiK10743.
    OMAiGPPEKYQ.
    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

    MDLSELERDN TGRCRLSSPV PAVCRKEPCV LGVDEAGRGP VLGPMVYAIC    50
    YCPLPRLADL EALKVADSKT LLESERERLF AKMEDTDFVG WALDVLSPNL 100
    ISTSMLGRVK YNLNSLSHDT ATGLIQYALD QGVNVTQVFV DTVGMPETYQ 150
    ARLQQSFPGI EVTVKAKADA LYPVVSAASI CAKVARDQAV KKWQFVEKLQ 200
    DLDTDYGSGY PNDPKTKAWL KEHVEPVFGF PQFVRFSWRT AQTILEKEAE 250
    DVIWEDSASE NQEGLRKITS YFLNEGSQAR PRSSHRYFLE RGLESATSL 299
    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z97029 mRNA. Translation: CAB09725.1 .
    AK315327 mRNA. Translation: BAG37728.1 .
    CH471106 Genomic DNA. Translation: EAW84313.1 .
    BC011748 mRNA. Translation: AAH11748.1 .
    CCDSi CCDS12282.1.
    RefSeqi NP_006388.2. NM_006397.2.
    UniGenei Hs.532851.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3P56 X-ray 4.06 A/D 1-299 [» ]
    3PUF X-ray 3.10 A/D/G/J/M/P 1-299 [» ]
    ProteinModelPortali O75792.
    SMRi O75792. Positions 2-299.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 115789. 7 interactions.
    STRINGi 9606.ENSP00000221486.

    PTM databases

    PhosphoSitei O75792.

    Proteomic databases

    MaxQBi O75792.
    PaxDbi O75792.
    PRIDEi O75792.

    Protocols and materials databases

    DNASUi 10535.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000221486 ; ENSP00000221486 ; ENSG00000104889 .
    GeneIDi 10535.
    KEGGi hsa:10535.
    UCSCi uc002mvg.1. human.

    Organism-specific databases

    CTDi 10535.
    GeneCardsi GC19P012918.
    GeneReviewsi RNASEH2A.
    HGNCi HGNC:18518. RNASEH2A.
    HPAi HPA042692.
    HPA051652.
    MIMi 606034. gene.
    610333. phenotype.
    neXtProti NX_O75792.
    Orphaneti 51. Aicardi-Goutieres syndrome.
    PharmGKBi PA38565.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0164.
    HOGENOMi HOG000100290.
    HOVERGENi HBG023585.
    InParanoidi O75792.
    KOi K10743.
    OMAi GPPEKYQ.
    OrthoDBi EOG7KM5T4.
    PhylomeDBi O75792.
    TreeFami TF314302.

    Miscellaneous databases

    EvolutionaryTracei O75792.
    GeneWikii RNASEH2A.
    GenomeRNAii 10535.
    NextBioi 39969.
    PROi O75792.
    SOURCEi Search...

    Gene expression databases

    Bgeei O75792.
    CleanExi HS_RNASEH2A.
    Genevestigatori O75792.

    Family and domain databases

    Gene3Di 1.10.10.460. 1 hit.
    3.30.420.10. 1 hit.
    InterProi IPR004649. 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 ]
    PANTHERi PTHR10954. PTHR10954. 1 hit.
    Pfami PF01351. RNase_HII. 1 hit.
    [Graphical view ]
    SUPFAMi SSF53098. SSF53098. 1 hit.
    TIGRFAMsi TIGR00729. TIGR00729. 1 hit.
    ProtoNeti Search...

    Publicationsi

    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: October 1, 2014
    This is version 134 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