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Q96FI4

- NEIL1_HUMAN

UniProt

Q96FI4 - NEIL1_HUMAN

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Protein
Endonuclease 8-like 1
Gene
NEIL1
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Involved in base excision repair of DNA damaged by oxidation or by mutagenic agents. Acts as DNA glycosylase that recognizes and removes damaged bases. Has a preference for oxidized pyrimidines, such as thymine glycol, formamidopyrimidine (Fapy) and 5-hydroxyuracil. Has marginal activity towards 8-oxoguanine. Has AP (apurinic/apyrimidinic) lyase activity and introduces nicks in the DNA strand. Cleaves the DNA backbone by beta-delta elimination to generate a single-strand break at the site of the removed base with both 3'- and 5'-phosphates. Has DNA glycosylase/lyase activity towards mismatched uracil and thymine, in particular in U:C and T:C mismatches. Specifically binds 5-hydroxymethylcytosine (5hmC), suggesting that it acts as a specific reader of 5hmC.4 Publications

Catalytic activityi

Removes damaged bases from DNA, leaving an abasic site.
The C-O-P bond 3' to the apurinic or apyrimidinic site in DNA is broken by a beta-elimination reaction, leaving a 3'-terminal unsaturated sugar and a product with a terminal 5'-phosphate.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei2 – 21Schiff-base intermediate with DNA Inferred
Active sitei3 – 31Proton donor Inferred
Active sitei54 – 541Proton donor; for beta-elimination activity Inferred
Binding sitei176 – 1761DNA By similarity
Active sitei339 – 3391Proton donor; for delta-elimination activity Inferred
Binding sitei339 – 3391DNA By similarity

GO - Molecular functioni

  1. DNA N-glycosylase activity Source: Ensembl
  2. DNA-(apurinic or apyrimidinic site) lyase activity Source: UniProtKB-EC
  3. damaged DNA binding Source: InterPro
  4. hydrolase activity, acting on glycosyl bonds Source: UniProtKB
  5. protein C-terminus binding Source: UniProtKB
  6. zinc ion binding Source: InterPro

GO - Biological processi

  1. base-excision repair Source: UniProtKB
  2. negative regulation of nuclease activity Source: UniProtKB
  3. nucleotide-excision repair Source: InterPro
  4. response to oxidative stress Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase, Lyase

Keywords - Biological processi

DNA damage, DNA repair

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

BRENDAi3.2.2.23. 2681.

Names & Taxonomyi

Protein namesi
Recommended name:
Endonuclease 8-like 1 (EC:3.2.2.-, EC:4.2.99.18)
Alternative name(s):
DNA glycosylase/AP lyase Neil1
DNA-(apurinic or apyrimidinic site) lyase Neil1
Endonuclease VIII-like 1
FPG1
Nei homolog 1
Short name:
NEH1
Nei-like protein 1
Gene namesi
Name:NEIL1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 15

Organism-specific databases

HGNCiHGNC:18448. NEIL1.

Subcellular locationi

Cytoplasmcytoskeletonmicrotubule organizing centercentrosome. Nucleus. Chromosome
Note: During mitosis, associates with centrosomes and condensed chromatin.1 Publication

GO - Cellular componenti

  1. chromosome Source: UniProtKB-SubCell
  2. cytoplasm Source: UniProtKB
  3. microtubule organizing center Source: UniProtKB-SubCell
  4. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Cytoplasm, Cytoskeleton, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi2 – 21P → T: Loss of glycosylase and AP lyase activity. 2 Publications
Mutagenesisi2 – 21Missing: Loss of glycosylase activity. 2 Publications
Mutagenesisi3 – 31E → Q: Loss of glycosylase and AP lyase activity. 1 Publication
Mutagenesisi54 – 541K → L: Loss of glycosylase activity. 1 Publication
Mutagenesisi277 – 2771R → A: Strongly reduced glycosylase activity. Has little effect on AP lyase activity. 1 Publication

Organism-specific databases

PharmGKBiPA38334.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed
Chaini2 – 390389Endonuclease 8-like 1
PRO_0000170905Add
BLAST

Proteomic databases

PaxDbiQ96FI4.
PRIDEiQ96FI4.

PTM databases

PhosphoSiteiQ96FI4.

Expressioni

Tissue specificityi

Ubiquitous.1 Publication

Inductioni

Up-regulated during S-phase.1 Publication

Gene expression databases

ArrayExpressiQ96FI4.
BgeeiQ96FI4.
CleanExiHS_NEIL1.
GenevestigatoriQ96FI4.

Organism-specific databases

HPAiHPA054084.

Interactioni

Protein-protein interaction databases

BioGridi122787. 5 interactions.
STRINGi9606.ENSP00000347170.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi4 – 1815
Beta strandi23 – 264
Beta strandi41 – 5212
Beta strandi55 – 628
Beta strandi73 – 786
Turni80 – 823
Beta strandi84 – 896
Helixi90 – 923
Beta strandi97 – 1037
Beta strandi105 – 1084
Beta strandi110 – 1156
Beta strandi122 – 1276
Turni137 – 1393
Helixi141 – 15010
Turni151 – 1533
Helixi155 – 1584
Helixi161 – 1644
Turni168 – 1703
Helixi176 – 18611
Helixi194 – 1985
Helixi199 – 2013
Helixi212 – 2187
Turni219 – 2213
Helixi225 – 24016
Helixi249 – 25911
Beta strandi269 – 2724
Beta strandi278 – 2836

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1TDHX-ray2.10A1-390[»]
4NRVX-ray2.60A2-290[»]
ProteinModelPortaliQ96FI4.
SMRiQ96FI4. Positions 2-290.

Miscellaneous databases

EvolutionaryTraceiQ96FI4.

Family & Domainsi

Sequence similaritiesi

Belongs to the FPG family.

Phylogenomic databases

eggNOGiNOG75119.
HOGENOMiHOG000067872.
HOVERGENiHBG052592.
InParanoidiQ96FI4.
KOiK10567.
OMAiHLASHFV.
PhylomeDBiQ96FI4.
TreeFamiTF333272.

Family and domain databases

InterProiIPR015886. DNA_glyclase/AP_lyase_DNA-bd.
IPR012319. DNA_glycosylase/AP_lyase_cat.
IPR015371. Endonuclease-VIII_DNA-bd.
IPR010979. Ribosomal_S13-like_H2TH.
[Graphical view]
PfamiPF01149. Fapy_DNA_glyco. 1 hit.
PF06831. H2TH. 1 hit.
PF09292. Neil1-DNA_bind. 1 hit.
[Graphical view]
SMARTiSM00898. Fapy_DNA_glyco. 1 hit.
[Graphical view]
SUPFAMiSSF46946. SSF46946. 1 hit.
SSF81624. SSF81624. 1 hit.
PROSITEiPS51068. FPG_CAT. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q96FI4-1 [UniParc]FASTAAdd to Basket

« Hide

MPEGPELHLA SQFVNEACRA LVFGGCVEKS SVSRNPEVPF ESSAYRISAS    50
ARGKELRLIL SPLPGAQPQQ EPLALVFRFG MSGSFQLVPR EELPRHAHLR 100
FYTAPPGPRL ALCFVDIRRF GRWDLGGKWQ PGRGPCVLQE YQQFRENVLR 150
NLADKAFDRP ICEALLDQRF FNGIGNYLRA EILYRLKIPP FEKARSVLEA 200
LQQHRPSPEL TLSQKIRTKL QNPDLLELCH SVPKEVVQLG GKGYGSESGE 250
EDFAAFRAWL RCYGMPGMSS LQDRHGRTIW FQGDPGPLAP KGRKSRKKKS 300
KATQLSPEDR VEDALPPSKA PSRTRRAKRD LPKRTATQRP EGTSLQQDPE 350
APTVPKKGRR KGRQAASGHC RPRKVKADIP SLEPEGTSAS 390
Length:390
Mass (Da):43,684
Last modified:January 23, 2007 - v3
Checksum:iB2B058486C4EF835
GO

Sequence cautioni

The sequence AK128372 differs from that shown. Reason: Erroneous CDS prediction.

RNA editingi

The edited form removes thymine glycol from duplex DNA 30 times more slowly than the form encoded in the genome, whereas editing enhances repair of the guanidinohydantoin lesion by NEIL1. The recoding site is a preferred editing site for the RNA editing adenosine deaminase ADAR1.1 Publication

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti82 – 821S → C.1 Publication
Corresponds to variant rs5745905 [ dbSNP | Ensembl ].
VAR_020580
Natural varianti83 – 831G → D.1 Publication
Corresponds to variant rs5745906 [ dbSNP | Ensembl ].
VAR_020581
Natural varianti136 – 1361C → R.1 Publication
Corresponds to variant rs5745907 [ dbSNP | Ensembl ].
VAR_020582
Natural varianti159 – 1591R → Q.1 Publication
VAR_065963
Natural varianti181 – 1811E → K Found in a patient with nephrotic syndrome also carrying mutation P-159 in MYO1E. 1 Publication
VAR_065964
Natural varianti182 – 1821I → M.
Corresponds to variant rs7183491 [ dbSNP | Ensembl ].
VAR_020583
Natural varianti242 – 2421K → R in RNA edited version.
VAR_065018
Natural varianti252 – 2521D → N.1 Publication
Corresponds to variant rs5745926 [ dbSNP | Ensembl ].
VAR_020584

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti147 – 1471N → S in BAB15337. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB079068 mRNA. Translation: BAC06476.1.
AK026055 mRNA. Translation: BAB15337.1.
AK128372 mRNA. No translation available.
AY257544 Genomic DNA. Translation: AAO74826.1.
AC068338 Genomic DNA. No translation available.
CH471136 Genomic DNA. Translation: EAW99255.1.
CH471136 Genomic DNA. Translation: EAW99260.1.
BC010876 mRNA. Translation: AAH10876.1.
CCDSiCCDS10278.1.
RefSeqiNP_001243481.1. NM_001256552.1.
NP_078884.2. NM_024608.3.
XP_005254716.1. XM_005254659.2.
XP_006720743.1. XM_006720680.1.
XP_006720744.1. XM_006720681.1.
XP_006720745.1. XM_006720682.1.
UniGeneiHs.512732.

Genome annotation databases

EnsembliENST00000355059; ENSP00000347170; ENSG00000140398.
ENST00000564784; ENSP00000457352; ENSG00000140398.
ENST00000569035; ENSP00000455730; ENSG00000140398.
GeneIDi79661.
KEGGihsa:79661.
UCSCiuc002bad.4. human.

Polymorphism databases

DMDMi56404654.

Keywords - Coding sequence diversityi

Polymorphism, RNA editing

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology
NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB079068 mRNA. Translation: BAC06476.1 .
AK026055 mRNA. Translation: BAB15337.1 .
AK128372 mRNA. No translation available.
AY257544 Genomic DNA. Translation: AAO74826.1 .
AC068338 Genomic DNA. No translation available.
CH471136 Genomic DNA. Translation: EAW99255.1 .
CH471136 Genomic DNA. Translation: EAW99260.1 .
BC010876 mRNA. Translation: AAH10876.1 .
CCDSi CCDS10278.1.
RefSeqi NP_001243481.1. NM_001256552.1.
NP_078884.2. NM_024608.3.
XP_005254716.1. XM_005254659.2.
XP_006720743.1. XM_006720680.1.
XP_006720744.1. XM_006720681.1.
XP_006720745.1. XM_006720682.1.
UniGenei Hs.512732.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1TDH X-ray 2.10 A 1-390 [» ]
4NRV X-ray 2.60 A 2-290 [» ]
ProteinModelPortali Q96FI4.
SMRi Q96FI4. Positions 2-290.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 122787. 5 interactions.
STRINGi 9606.ENSP00000347170.

PTM databases

PhosphoSitei Q96FI4.

Polymorphism databases

DMDMi 56404654.

Proteomic databases

PaxDbi Q96FI4.
PRIDEi Q96FI4.

Protocols and materials databases

DNASUi 79661.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000355059 ; ENSP00000347170 ; ENSG00000140398 .
ENST00000564784 ; ENSP00000457352 ; ENSG00000140398 .
ENST00000569035 ; ENSP00000455730 ; ENSG00000140398 .
GeneIDi 79661.
KEGGi hsa:79661.
UCSCi uc002bad.4. human.

Organism-specific databases

CTDi 79661.
GeneCardsi GC15P075639.
H-InvDB HIX0202149.
HGNCi HGNC:18448. NEIL1.
HPAi HPA054084.
MIMi 608844. gene.
neXtProti NX_Q96FI4.
PharmGKBi PA38334.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG75119.
HOGENOMi HOG000067872.
HOVERGENi HBG052592.
InParanoidi Q96FI4.
KOi K10567.
OMAi HLASHFV.
PhylomeDBi Q96FI4.
TreeFami TF333272.

Enzyme and pathway databases

BRENDAi 3.2.2.23. 2681.

Miscellaneous databases

EvolutionaryTracei Q96FI4.
GeneWikii NEIL1.
GenomeRNAii 79661.
NextBioi 68852.
PROi Q96FI4.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q96FI4.
Bgeei Q96FI4.
CleanExi HS_NEIL1.
Genevestigatori Q96FI4.

Family and domain databases

InterProi IPR015886. DNA_glyclase/AP_lyase_DNA-bd.
IPR012319. DNA_glycosylase/AP_lyase_cat.
IPR015371. Endonuclease-VIII_DNA-bd.
IPR010979. Ribosomal_S13-like_H2TH.
[Graphical view ]
Pfami PF01149. Fapy_DNA_glyco. 1 hit.
PF06831. H2TH. 1 hit.
PF09292. Neil1-DNA_bind. 1 hit.
[Graphical view ]
SMARTi SM00898. Fapy_DNA_glyco. 1 hit.
[Graphical view ]
SUPFAMi SSF46946. SSF46946. 1 hit.
SSF81624. SSF81624. 1 hit.
PROSITEi PS51068. FPG_CAT. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "A back-up glycosylase in Nth1 knock-out mice is a functional Nei (endonuclease VIII) homologue."
    Takao M., Kanno S., Kobayashi K., Zhang Q.-M., Yonei S., van der Horst G.T.J., Yasui A.
    J. Biol. Chem. 277:42205-42213(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION.
    Tissue: Testis.
  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].
  3. NIEHS SNPs program
    Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS CYS-82; ASP-83; ARG-136 AND ASN-252.
  4. "Analysis of the DNA sequence and duplication history of human chromosome 15."
    Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K., Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N., Abouelleil A.
    , Arachchi H.M., Baradarani L., Birditt B., Bloom S., Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K., DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B., Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.
    Nature 440:671-675(2006) [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].
    Tissue: Lung.
  7. "A novel human DNA glycosylase that removes oxidative DNA damage and is homologous to Escherichia coli endonuclease VIII."
    Bandaru V., Sunkara S., Wallace S.S., Bond J.P.
    DNA Repair 1:517-529(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF PRO-2 AND GLU-3, FUNCTION.
  8. "Identification and characterization of a human DNA glycosylase for repair of modified bases in oxidatively damaged DNA."
    Hazra T.K., Izumi T., Boldogh I., Imhoff B., Kow Y.W., Jaruga P., Dizdaroglu M., Mitra S.
    Proc. Natl. Acad. Sci. U.S.A. 99:3523-3528(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF PRO-2, FUNCTION, INDUCTION, TISSUE SPECIFICITY.
  9. "Repair of oxidized bases in DNA bubble structures by human DNA glycosylases NEIL1 and NEIL2."
    Dou H., Mitra S., Hazra T.K.
    J. Biol. Chem. 278:49679-49684(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF LYS-54.
  10. "Human NEIL1 localizes with the centrosomes and condensed chromosomes during mitosis."
    Hildrestrand G.A., Rolseth V., Bjoras M., Luna L.
    DNA Repair 6:1425-1433(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  11. "RNA editing changes the lesion specificity for the DNA repair enzyme NEIL1."
    Yeo J., Goodman R.A., Schirle N.T., David S.S., Beal P.A.
    Proc. Natl. Acad. Sci. U.S.A. 107:20715-20719(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: RNA EDITING OF POSITION 242.
  12. "The crystal structure of human endonuclease VIII-like 1 (NEIL1) reveals a zincless finger motif required for glycosylase activity."
    Doublie S., Bandaru V., Bond J.P., Wallace S.S.
    Proc. Natl. Acad. Sci. U.S.A. 101:10284-10289(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 1-334, MUTAGENESIS OF ARG-277.
  13. Cited for: VARIANTS GLN-159 AND LYS-181.

Entry informationi

Entry nameiNEIL1_HUMAN
AccessioniPrimary (citable) accession number: Q96FI4
Secondary accession number(s): D3DW75
, Q6ZRA7, Q86XW7, Q9H6C3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 7, 2004
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 122 of the entry and version 3 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, Multifunctional enzyme, Reference proteome

Documents

  1. Human chromosome 15
    Human chromosome 15: 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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