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Q5TBB1

- RNH2B_HUMAN

UniProt

Q5TBB1 - RNH2B_HUMAN

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Protein

Ribonuclease H2 subunit B

Gene

RNASEH2B

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

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
Complete GO annotation...

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
Complete GO annotation...

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

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 – 218Combined sources
Beta strandi36 – 416Combined sources
Turni43 – 453Combined sources
Beta strandi47 – 548Combined sources
Turni55 – 584Combined sources
Beta strandi59 – 668Combined sources
Beta strandi72 – 754Combined sources
Beta strandi78 – 814Combined sources
Beta strandi85 – 906Combined sources
Helixi94 – 10714Combined sources
Helixi113 – 1164Combined sources
Helixi123 – 1308Combined sources
Helixi134 – 1385Combined sources
Turni139 – 1413Combined sources
Beta strandi142 – 1454Combined sources
Beta strandi155 – 1584Combined sources
Helixi160 – 18122Combined sources
Helixi206 – 21611Combined sources
Turni217 – 2193Combined sources
Helixi222 – 2309Combined sources
Helixi297 – 2993Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
GeneTreeiENSGT00390000011439.
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

        10         20         30         40         50
MAAGVDCGDG VGARQHVFLV SEYLKDASKK MKNGLMFVKL VNPCSGEGAI
60 70 80 90 100
YLFNMCLQQL FEVKVFKEKH HSWFINQSVQ SGGLLHFATP VDPLFLLLHY
110 120 130 140 150
LIKADKEGKF QPLDQVVVDN VFPNCILLLK LPGLEKLLHH VTEEKGNPEI
160 170 180 190 200
DNKKYYKYSK EKTLKWLEKK VNQTVAALKT NNVNVSSRVQ STAFFSGDQA
210 220 230 240 250
STDKEEDYIR YAHGLISDYI PKELSDDLSK YLKLPEPSAS LPNPPSKKIK
260 270 280 290 300
LSDEPVEAKE DYTKFNTKDL KTEKKNSKMT AAQKALAKVD KSGMKSIDTF
310
FGVKNKKKIG KV
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.Curated
The sequence AAH07332.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.Curated
The sequence AAH10174.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.Curated

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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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.
GeneTreei ENSGT00390000011439.
HOVERGENi HBG056010.
InParanoidi Q5TBB1.
KOi K10744.
OMAi LVNPCSG.
OrthoDBi EOG741Z2J.
PhylomeDBi Q5TBB1.
TreeFami TF105250.

Miscellaneous databases

ChiTaRSi RNASEH2B. human.
EvolutionaryTracei Q5TBB1.
GenomeRNAii 79621.
NextBioi 68689.
PROi Q5TBB1.
SOURCEi Search...

Gene expression databases

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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 88 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