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O75792

- RNH2A_HUMAN

UniProt

O75792 - RNH2A_HUMAN

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Protein
Ribonuclease H2 subunit A
Gene
RNASEH2A, RNASEHI, RNHIA
Organism
Homo sapiens (Human)
Status
Reviewed - 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

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.1 Publication

Sites

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

GO - Molecular functioni

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

GO - Biological processi

  1. DNA replication Source: UniProtKB
  2. RNA catabolic process Source: UniProtKB
  3. RNA phosphodiester bond hydrolysis Source: GOC
  4. RNA phosphodiester bond hydrolysis, endonucleolytic Source: GOC
  5. mismatch repair Source: MGI
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
Synonyms:RNASEHI, RNHIA
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 19

Organism-specific databases

HGNCiHGNC:18518. RNASEH2A.

Subcellular locationi

Nucleus Inferred

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 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.
Note: The disease is caused by mutations affecting the gene represented in this entry.3 Publications
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 A
PRO_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 – 2571Phosphoserine By 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

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.

Miscellaneous databases

EvolutionaryTraceiO75792.

Family & Domainsi

Sequence similaritiesi

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

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 conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti152 – 1521R → Q in CAB09725. 1 Publication

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...

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

« 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: July 9, 2014
This is version 133 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

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