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Q5TBB1 (RNH2B_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 84. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:RNASEH2B
Synonyms:DLEU8
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length312 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.11 Ref.12

Subunit structure

The RNase H2 complex is a heterotrimer composed of the catalytic subunit RNASEH2A and the non-catalytic subunits RNASEH2B and RNASEH2C. Ref.11

Subcellular location

Nucleus Probable.

Tissue specificity

Widely expressed. Ref.12

Involvement in disease

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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.11 Ref.12 Ref.13 Ref.14

Sequence similarities

Belongs to the RNase H2 subunit B family.

Sequence caution

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.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q5TBB1-1)

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.
Isoform 2 (identifier: Q5TBB1-2)

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.9
Chain2 – 312311Ribonuclease H2 subunit B
PRO_0000248378

Amino acid modifications

Modified residue21N-acetylalanine Ref.9 Ref.10
Modified residue2951N6-acetyllysine Ref.7

Natural variations

Alternative sequence248 – 25710KIKLSDEPVE → MAAQRQKRGK in isoform 2.
VSP_054039
Alternative sequence258 – 31255Missing in isoform 2.
VSP_054040
Natural variant431P → H in AGS2. Ref.13
VAR_070611
Natural variant601L → R in AGS2; heterozygous compound with T-177. Ref.12 Ref.13
VAR_027280
Natural variant731W → L in AGS2; reduces stability of the RNase complex. Ref.11 Ref.13
VAR_070612
Natural variant831G → S in AGS2; reduces stability of the RNase complex. Ref.11 Ref.13
VAR_070613
Natural variant861H → R in AGS2; heterozygous compound with T-177; reduces stability of the RNase complex. Ref.11 Ref.12 Ref.13
VAR_027281
Natural variant1381L → F in AGS2. Ref.13
VAR_070614
Natural variant1591S → I in AGS2. Ref.13
VAR_070615
Natural variant1621K → T in AGS2. Ref.12 Ref.13
VAR_027282
Natural variant1631T → I in AGS2; heterozygous compound with T-177. Ref.12 Ref.13
VAR_027283
Natural variant1771A → T in AGS2; frequent mutation. Ref.12 Ref.14
VAR_027284
Natural variant1831V → M in AGS2. Ref.13
VAR_070616
Natural variant1851V → G in AGS2. Ref.12 Ref.13
VAR_027285
Natural variant2191Y → H in AGS2; heterozygous compound with a nonsense mutation; reduces stability of the RNase complex. Ref.11 Ref.12 Ref.13
VAR_027286
Natural variant2291S → P in AGS2. Ref.14
VAR_070617

Experimental info

Sequence conflict611F → L in AAX13343. Ref.1
Sequence conflict611F → L in BAB13892. Ref.2
Sequence conflict3051N → K in AAH05088. Ref.6

Secondary structure

...................................... 312
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified April 12, 2005. Version 1.
Checksum: 98B1A8E073A50D68

FASTA31235,139
        10         20         30         40         50         60 
MAAGVDCGDG VGARQHVFLV SEYLKDASKK MKNGLMFVKL VNPCSGEGAI YLFNMCLQQL 

        70         80         90        100        110        120 
FEVKVFKEKH HSWFINQSVQ SGGLLHFATP VDPLFLLLHY LIKADKEGKF QPLDQVVVDN 

       130        140        150        160        170        180 
VFPNCILLLK LPGLEKLLHH VTEEKGNPEI DNKKYYKYSK EKTLKWLEKK VNQTVAALKT 

       190        200        210        220        230        240 
NNVNVSSRVQ STAFFSGDQA STDKEEDYIR YAHGLISDYI PKELSDDLSK YLKLPEPSAS 

       250        260        270        280        290        300 
LPNPPSKKIK LSDEPVEAKE DYTKFNTKDL KTEKKNSKMT AAQKALAKVD KSGMKSIDTF 

       310 
FGVKNKKKIG KV 

« Hide

Isoform 2 [UniParc].

Checksum: D96DCA78CB52F6DF
Show »

FASTA25729,005

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
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]"Mutations in genes encoding ribonuclease H2 subunits cause Aicardi-Goutieres syndrome and mimic congenital viral brain infection."
Crow Y.J., Leitch A., Hayward B.E., Garner A., Parmar R., Griffith E., Ali M., Semple C., Aicardi J., Babul-Hirji R., Baumann C., Baxter P., Bertini E., Chandler K.E., Chitayat D., Cau D., Dery C., Fazzi E. expand/collapse author list , Goizet C., King M.D., Klepper J., Lacombe D., Lanzi G., Lyall H., Martinez-Frias M.L., Mathieu M., McKeown C., Monier A., Oade Y., Quarrell O.W., Rittey C.D., Rogers R.C., Sanchis A., Stephenson J.B.P., Tacke U., Till M., Tolmie J.L., Tomlin P., Voit T., Weschke B., Woods C.G., Lebon P., Bonthron D.T., Ponting C.P., Jackson A.P.
Nat. Genet. 38:910-916(2006) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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]"Expanding the phenotypic spectrum of lupus erythematosus in Aicardi-Goutieres syndrome."
Ramantani G., Kohlhase J., Hertzberg C., Innes A.M., Engel K., Hunger S., Borozdin W., Mah J.K., Ungerath K., Walkenhorst H., Richardt H.H., Buckard J., Bevot A., Siegel C., von Stuelpnagel C., Ikonomidou C., Thomas K., Proud V. expand/collapse author list , Niemann F., Wieczorek D., Haeusler M., Niggemann P., Baltaci V., Conrad K., Lebon P., Lee-Kirsch M.A.
Arthritis Rheum. 62:1469-1477(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS AGS2 THR-177 AND PRO-229.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS9425.1.
RefSeqNP_001135751.1. NM_001142279.2. [Q5TBB1-2]
NP_078846.2. NM_024570.3. [Q5TBB1-1]
UniGeneHs.306291.

3D structure databases

PDBe
RCSB-PDB
PDBj
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[»]
ProteinModelPortalQ5TBB1.
SMRQ5TBB1. Positions 14-232.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid122751. 8 interactions.
STRING9606.ENSP00000337623.

PTM databases

PhosphoSiteQ5TBB1.

Polymorphism databases

DMDM74745929.

Proteomic databases

MaxQBQ5TBB1.
PaxDbQ5TBB1.
PRIDEQ5TBB1.

Protocols and materials databases

DNASU79621.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000336617; ENSP00000337623; ENSG00000136104.
ENST00000422660; ENSP00000389877; ENSG00000136104.
GeneID79621.
KEGGhsa:79621.
UCSCuc001vfa.4. human. [Q5TBB1-1]

Organism-specific databases

CTD79621.
GeneCardsGC13P051483.
GeneReviewsRNASEH2B.
HGNCHGNC:25671. RNASEH2B.
HPAHPA040084.
HPA041469.
MIM610181. phenotype.
610326. gene.
neXtProtNX_Q5TBB1.
Orphanet51. Aicardi-Goutieres syndrome.
PharmGKBPA162401418.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG320404.
HOVERGENHBG056010.
InParanoidQ5TBB1.
KOK10744.
OMALVNPCSG.
OrthoDBEOG741Z2J.
PhylomeDBQ5TBB1.
TreeFamTF105250.

Gene expression databases

ArrayExpressQ5TBB1.
BgeeQ5TBB1.
CleanExHS_RNASEH2B.
GenevestigatorQ5TBB1.

Family and domain databases

InterProIPR019024. RNase_H2_suB.
[Graphical view]
PfamPF09468. RNase_H2-Ydr279. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ5TBB1.
GenomeRNAi79621.
NextBio68689.
PROQ5TBB1.
SOURCESearch...

Entry information

Entry nameRNH2B_HUMAN
AccessionPrimary (citable) accession number: Q5TBB1
Secondary accession number(s): G3XAJ1 expand/collapse secondary AC list , Q05DR2, Q6PK48, Q9HAF7
Entry history
Integrated into UniProtKB/Swiss-Prot: September 5, 2006
Last sequence update: April 12, 2005
Last modified: July 9, 2014
This is version 84 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 13

Human chromosome 13: entries, gene names and cross-references to MIM