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Q5TBB1

- RNH2B_HUMAN

UniProt

Q5TBB1 - RNH2B_HUMAN

Protein

Ribonuclease H2 subunit B

Gene

RNASEH2B

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 86 (01 Oct 2014)
      Sequence version 1 (12 Apr 2005)
      Previous versions | rss
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    Functioni

    Non catalytic subunit of RNase H2, 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

    GO - Molecular functioni

    1. RNA-DNA hybrid ribonuclease activity Source: Ensembl

    GO - Biological processi

    1. in utero embryonic development Source: Ensembl
    2. negative regulation of gene expression Source: Ensembl
    3. positive regulation of fibroblast proliferation Source: Ensembl
    4. regulation of DNA damage checkpoint Source: Ensembl
    5. regulation of G2/M transition of mitotic cell cycle Source: Ensembl
    6. ribonucleotide metabolic process Source: Ensembl
    7. RNA catabolic process Source: UniProtKB

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ribonuclease H2 subunit B
    Short name:
    RNase H2 subunit B
    Alternative name(s):
    Aicardi-Goutieres syndrome 2 protein
    Short name:
    AGS2
    Deleted in lymphocytic leukemia 8
    Ribonuclease HI subunit B
    Gene namesi
    Name:RNASEH2B
    Synonyms:DLEU8
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 13

    Organism-specific databases

    HGNCiHGNC:25671. RNASEH2B.

    Subcellular locationi

    Nucleus Curated

    GO - Cellular componenti

    1. nucleus Source: HPA
    2. ribonuclease H2 complex Source: UniProtKB

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    Aicardi-Goutieres syndrome 2 (AGS2) [MIM:610181]: 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 varianti43 – 431P → H in AGS2. 1 Publication
    VAR_070611
    Natural varianti60 – 601L → R in AGS2; heterozygous compound with T-177. 2 Publications
    VAR_027280
    Natural varianti73 – 731W → L in AGS2; reduces stability of the RNase complex. 1 Publication
    VAR_070612
    Natural varianti83 – 831G → S in AGS2; reduces stability of the RNase complex. 1 Publication
    VAR_070613
    Natural varianti86 – 861H → R in AGS2; heterozygous compound with T-177; reduces stability of the RNase complex. 2 Publications
    VAR_027281
    Natural varianti138 – 1381L → F in AGS2. 1 Publication
    VAR_070614
    Natural varianti159 – 1591S → I in AGS2. 1 Publication
    VAR_070615
    Natural varianti162 – 1621K → T in AGS2. 2 Publications
    VAR_027282
    Natural varianti163 – 1631T → I in AGS2; heterozygous compound with T-177. 2 Publications
    VAR_027283
    Natural varianti177 – 1771A → T in AGS2; frequent mutation. 2 Publications
    VAR_027284
    Natural varianti183 – 1831V → M in AGS2. 1 Publication
    VAR_070616
    Natural varianti185 – 1851V → G in AGS2. 2 Publications
    VAR_027285
    Natural varianti219 – 2191Y → H in AGS2; heterozygous compound with a nonsense mutation; reduces stability of the RNase complex. 2 Publications
    VAR_027286
    Natural varianti229 – 2291S → P in AGS2. 1 Publication
    VAR_070617

    Keywords - Diseasei

    Aicardi-Goutieres syndrome, Disease mutation

    Organism-specific databases

    MIMi610181. phenotype.
    Orphaneti51. Aicardi-Goutieres syndrome.
    PharmGKBiPA162401418.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed2 Publications
    Chaini2 – 312311Ribonuclease H2 subunit BPRO_0000248378Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine2 Publications
    Modified residuei295 – 2951N6-acetyllysine1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiQ5TBB1.
    PaxDbiQ5TBB1.
    PRIDEiQ5TBB1.

    PTM databases

    PhosphoSiteiQ5TBB1.

    Expressioni

    Tissue specificityi

    Widely expressed.1 Publication

    Gene expression databases

    ArrayExpressiQ5TBB1.
    BgeeiQ5TBB1.
    CleanExiHS_RNASEH2B.
    GenevestigatoriQ5TBB1.

    Organism-specific databases

    HPAiHPA040084.
    HPA041469.

    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

    BioGridi122751. 8 interactions.
    STRINGi9606.ENSP00000337623.

    Structurei

    Secondary structure

    1
    312
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi14 – 218
    Beta strandi36 – 416
    Turni43 – 453
    Beta strandi47 – 548
    Turni55 – 584
    Beta strandi59 – 668
    Beta strandi72 – 754
    Beta strandi78 – 814
    Beta strandi85 – 906
    Helixi94 – 10714
    Helixi113 – 1164
    Helixi123 – 1308
    Helixi134 – 1385
    Turni139 – 1413
    Beta strandi142 – 1454
    Beta strandi155 – 1584
    Helixi160 – 18122
    Helixi206 – 21611
    Turni217 – 2193
    Helixi222 – 2309
    Helixi297 – 2993

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3P56X-ray4.06B/E2-226[»]
    3P87X-ray2.99G/H/I/J/K/L290-312[»]
    3PUFX-ray3.10B/E/H/K/N/Q14-233[»]
    ProteinModelPortaliQ5TBB1.
    SMRiQ5TBB1. Positions 14-232.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ5TBB1.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the RNase H2 subunit B family.Curated

    Phylogenomic databases

    eggNOGiNOG320404.
    HOVERGENiHBG056010.
    InParanoidiQ5TBB1.
    KOiK10744.
    OMAiLVNPCSG.
    OrthoDBiEOG741Z2J.
    PhylomeDBiQ5TBB1.
    TreeFamiTF105250.

    Family and domain databases

    InterProiIPR019024. RNase_H2_suB.
    [Graphical view]
    PfamiPF09468. RNase_H2-Ydr279. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q5TBB1-1) [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

    MAAGVDCGDG VGARQHVFLV SEYLKDASKK MKNGLMFVKL VNPCSGEGAI    50
    YLFNMCLQQL FEVKVFKEKH HSWFINQSVQ SGGLLHFATP VDPLFLLLHY 100
    LIKADKEGKF QPLDQVVVDN VFPNCILLLK LPGLEKLLHH VTEEKGNPEI 150
    DNKKYYKYSK EKTLKWLEKK VNQTVAALKT NNVNVSSRVQ STAFFSGDQA 200
    STDKEEDYIR YAHGLISDYI PKELSDDLSK YLKLPEPSAS LPNPPSKKIK 250
    LSDEPVEAKE DYTKFNTKDL KTEKKNSKMT AAQKALAKVD KSGMKSIDTF 300
    FGVKNKKKIG KV 312
    Length:312
    Mass (Da):35,139
    Last modified:April 12, 2005 - v1
    Checksum:i98B1A8E073A50D68
    GO
    Isoform 2 (identifier: Q5TBB1-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         248-257: KIKLSDEPVE → MAAQRQKRGK
         258-312: Missing.

    Note: No experimental confirmation available. Gene prediction based on EST data.

    Show »
    Length:257
    Mass (Da):29,005
    Checksum:iD96DCA78CB52F6DF
    GO

    Sequence cautioni

    The sequence AAH01397.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.
    The sequence AAH07332.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.
    The sequence AAH10174.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti61 – 611F → L in AAX13343. 1 PublicationCurated
    Sequence conflicti61 – 611F → L in BAB13892. (PubMed:14702039)Curated
    Sequence conflicti305 – 3051N → K in AAH05088. (PubMed:15489334)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti43 – 431P → H in AGS2. 1 Publication
    VAR_070611
    Natural varianti60 – 601L → R in AGS2; heterozygous compound with T-177. 2 Publications
    VAR_027280
    Natural varianti73 – 731W → L in AGS2; reduces stability of the RNase complex. 1 Publication
    VAR_070612
    Natural varianti83 – 831G → S in AGS2; reduces stability of the RNase complex. 1 Publication
    VAR_070613
    Natural varianti86 – 861H → R in AGS2; heterozygous compound with T-177; reduces stability of the RNase complex. 2 Publications
    VAR_027281
    Natural varianti138 – 1381L → F in AGS2. 1 Publication
    VAR_070614
    Natural varianti159 – 1591S → I in AGS2. 1 Publication
    VAR_070615
    Natural varianti162 – 1621K → T in AGS2. 2 Publications
    VAR_027282
    Natural varianti163 – 1631T → I in AGS2; heterozygous compound with T-177. 2 Publications
    VAR_027283
    Natural varianti177 – 1771A → T in AGS2; frequent mutation. 2 Publications
    VAR_027284
    Natural varianti183 – 1831V → M in AGS2. 1 Publication
    VAR_070616
    Natural varianti185 – 1851V → G in AGS2. 2 Publications
    VAR_027285
    Natural varianti219 – 2191Y → H in AGS2; heterozygous compound with a nonsense mutation; reduces stability of the RNase complex. 2 Publications
    VAR_027286
    Natural varianti229 – 2291S → P in AGS2. 1 Publication
    VAR_070617

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei248 – 25710KIKLSDEPVE → MAAQRQKRGK in isoform 2. CuratedVSP_054039
    Alternative sequencei258 – 31255Missing in isoform 2. CuratedVSP_054040Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY764036 mRNA. Translation: AAX13343.1.
    AK021774 mRNA. Translation: BAB13892.1.
    AK223340 mRNA. Translation: BAD97060.1.
    AL137881 Genomic DNA. No translation available.
    CH471075 Genomic DNA. Translation: EAX08864.1.
    BC001397 mRNA. Translation: AAH01397.1. Sequence problems.
    BC005088 mRNA. Translation: AAH05088.1.
    BC007332 mRNA. Translation: AAH07332.1. Sequence problems.
    BC010174 mRNA. Translation: AAH10174.1. Sequence problems.
    CCDSiCCDS45047.1. [Q5TBB1-2]
    CCDS9425.1. [Q5TBB1-1]
    RefSeqiNP_001135751.1. NM_001142279.2. [Q5TBB1-2]
    NP_078846.2. NM_024570.3. [Q5TBB1-1]
    UniGeneiHs.306291.

    Genome annotation databases

    EnsembliENST00000336617; ENSP00000337623; ENSG00000136104. [Q5TBB1-1]
    ENST00000422660; ENSP00000389877; ENSG00000136104. [Q5TBB1-2]
    GeneIDi79621.
    KEGGihsa:79621.
    UCSCiuc001vfa.4. human. [Q5TBB1-1]
    uc001vfb.4. human.

    Polymorphism databases

    DMDMi74745929.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY764036 mRNA. Translation: AAX13343.1 .
    AK021774 mRNA. Translation: BAB13892.1 .
    AK223340 mRNA. Translation: BAD97060.1 .
    AL137881 Genomic DNA. No translation available.
    CH471075 Genomic DNA. Translation: EAX08864.1 .
    BC001397 mRNA. Translation: AAH01397.1 . Sequence problems.
    BC005088 mRNA. Translation: AAH05088.1 .
    BC007332 mRNA. Translation: AAH07332.1 . Sequence problems.
    BC010174 mRNA. Translation: AAH10174.1 . Sequence problems.
    CCDSi CCDS45047.1. [Q5TBB1-2 ]
    CCDS9425.1. [Q5TBB1-1 ]
    RefSeqi NP_001135751.1. NM_001142279.2. [Q5TBB1-2 ]
    NP_078846.2. NM_024570.3. [Q5TBB1-1 ]
    UniGenei Hs.306291.

    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 B/E 2-226 [» ]
    3P87 X-ray 2.99 G/H/I/J/K/L 290-312 [» ]
    3PUF X-ray 3.10 B/E/H/K/N/Q 14-233 [» ]
    ProteinModelPortali Q5TBB1.
    SMRi Q5TBB1. Positions 14-232.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 122751. 8 interactions.
    STRINGi 9606.ENSP00000337623.

    PTM databases

    PhosphoSitei Q5TBB1.

    Polymorphism databases

    DMDMi 74745929.

    Proteomic databases

    MaxQBi Q5TBB1.
    PaxDbi Q5TBB1.
    PRIDEi Q5TBB1.

    Protocols and materials databases

    DNASUi 79621.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000336617 ; ENSP00000337623 ; ENSG00000136104 . [Q5TBB1-1 ]
    ENST00000422660 ; ENSP00000389877 ; ENSG00000136104 . [Q5TBB1-2 ]
    GeneIDi 79621.
    KEGGi hsa:79621.
    UCSCi uc001vfa.4. human. [Q5TBB1-1 ]
    uc001vfb.4. human.

    Organism-specific databases

    CTDi 79621.
    GeneCardsi GC13P051483.
    GeneReviewsi RNASEH2B.
    HGNCi HGNC:25671. RNASEH2B.
    HPAi HPA040084.
    HPA041469.
    MIMi 610181. phenotype.
    610326. gene.
    neXtProti NX_Q5TBB1.
    Orphaneti 51. Aicardi-Goutieres syndrome.
    PharmGKBi PA162401418.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG320404.
    HOVERGENi HBG056010.
    InParanoidi Q5TBB1.
    KOi K10744.
    OMAi LVNPCSG.
    OrthoDBi EOG741Z2J.
    PhylomeDBi Q5TBB1.
    TreeFami TF105250.

    Miscellaneous databases

    EvolutionaryTracei Q5TBB1.
    GenomeRNAii 79621.
    NextBioi 68689.
    PROi Q5TBB1.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q5TBB1.
    Bgeei Q5TBB1.
    CleanExi HS_RNASEH2B.
    Genevestigatori Q5TBB1.

    Family and domain databases

    InterProi IPR019024. RNase_H2_suB.
    [Graphical view ]
    Pfami PF09468. RNase_H2-Ydr279. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "DLEU8, a novel conserved gene located in the CLL 13q14 deletion locus."
      Corcoran M.M.
      Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases
      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.
      , 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] (ISOFORM 1).
    3. Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
      Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Testis.
    4. "The DNA sequence and analysis of human chromosome 13."
      Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L., Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T.
      , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P., Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L., Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S., Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R., Rogers J., Ross M.T.
      Nature 428:522-528(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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] OF 1-308 (ISOFORM 1).
      Tissue: Skin.
    7. "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-295, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    9. "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 ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    10. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. "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) OF 14-233, SUBUNIT, FUNCTION, CHARACTERIZATION OF VARIANTS AGS2 LEU-73; SER-83; ARG-86 AND HIS-219.
    12. Cited for: VARIANTS AGS2 ARG-60; ARG-86; THR-162; ILE-163; THR-177; GLY-185 AND HIS-219, FUNCTION, TISSUE SPECIFICITY, INTERACTION WITH RNASEH2A AND RNASEH2C.
    13. "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 AGS2 HIS-43; ARG-60; LEU-73; SER-83; ARG-86; PHE-138; ILE-159; THR-162; ILE-163; THE-177; MET-183; GLY-185 AND HIS-219.
    14. Cited for: VARIANTS AGS2 THR-177 AND PRO-229.

    Entry informationi

    Entry nameiRNH2B_HUMAN
    AccessioniPrimary (citable) accession number: Q5TBB1
    Secondary accession number(s): G3XAJ1
    , Q05DR2, Q6PK48, Q9HAF7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 5, 2006
    Last sequence update: April 12, 2005
    Last modified: October 1, 2014
    This is version 86 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 13
      Human chromosome 13: 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