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Protein

Fanconi anemia group E protein

Gene

FANCE

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

Functioni

As part of the Fanconi anemia (FA) complex functions in DNA cross-links repair. Required for the nuclear accumulation of FANCC and provides a critical bridge between the FA complex and FANCD2.2 Publications

GO - Biological processi

  1. DNA repair Source: Reactome
Complete GO annotation...

Keywords - Biological processi

DNA damage, DNA repair

Enzyme and pathway databases

ReactomeiREACT_18410. Fanconi Anemia pathway.

Names & Taxonomyi

Protein namesi
Recommended name:
Fanconi anemia group E protein
Short name:
Protein FACE
Gene namesi
Name:FANCE
Synonyms:FACE
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 6

Organism-specific databases

HGNCiHGNC:3586. FANCE.

Subcellular locationi

Nucleus 2 Publications

GO - Cellular componenti

  1. Fanconi anaemia nuclear complex Source: UniProtKB
  2. nucleoplasm Source: Reactome
  3. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Involvement in diseasei

Fanconi anemia complementation group E

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA disorder affecting all bone marrow elements and resulting in anemia, leukopenia and thrombopenia. It is associated with cardiac, renal and limb malformations, dermal pigmentary changes, and a predisposition to the development of malignancies. At the cellular level it is associated with hypersensitivity to DNA-damaging agents, chromosomal instability (increased chromosome breakage) and defective DNA repair.

See also OMIM:600901

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi346 – 3461T → A: Non-phosphorylatable by CHEK1, not polyubiquitinated and unable to complement the mitomycin C hypersensitivity of cells lacking FANCE; when associated with A-374. 1 Publication
Mutagenesisi374 – 3741S → A: Non-phosphorylatable by CHEK1, not polyubiquitinated and unable to complement the mitomycin C hypersensitivity of cells lacking FANCE; when associated with A-346. 1 Publication

Keywords - Diseasei

Disease mutation, Fanconi anemia

Organism-specific databases

MIMi600901. phenotype.
Orphaneti84. Fanconi anemia.
PharmGKBiPA28000.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 536536Fanconi anemia group E proteinPRO_0000087187Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei249 – 2491Phosphoserine3 Publications
Modified residuei346 – 3461Phosphothreonine; by CHEK11 Publication
Modified residuei374 – 3741Phosphoserine; by CHEK11 Publication

Post-translational modificationi

Phosphorylated. Phosphorylation by CHEK1 at Thr-346 and Ser-374 regulates its function in DNA cross-links repair.1 Publication
Ubiquitinated. Phosphorylation by CHEK1 induces polyubiquitination and degradation.1 Publication

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ9HB96.
PaxDbiQ9HB96.
PRIDEiQ9HB96.

PTM databases

PhosphoSiteiQ9HB96.

Expressioni

Gene expression databases

BgeeiQ9HB96.
CleanExiHS_FANCE.
GenevestigatoriQ9HB96.

Organism-specific databases

HPAiCAB014893.

Interactioni

Subunit structurei

Belongs to the multisubunit FA complex composed of FANCA, FANCB, FANCC, FANCE, FANCF, FANCG, FANCL/PHF9 and FANCM. The complex is not found in FA patients. Interacts with FANCC and FANCD2.5 Publications

Protein-protein interaction databases

BioGridi108475. 17 interactions.
DIPiDIP-32845N.
IntActiQ9HB96. 4 interactions.
MINTiMINT-157013.
STRINGi9606.ENSP00000229769.

Structurei

Secondary structure

1
536
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi282 – 29918Combined sources
Helixi311 – 3144Combined sources
Helixi315 – 3184Combined sources
Helixi321 – 33111Combined sources
Helixi333 – 3353Combined sources
Helixi338 – 35013Combined sources
Helixi357 – 37418Combined sources
Helixi381 – 39313Combined sources
Helixi395 – 40814Combined sources
Helixi414 – 42512Combined sources
Helixi431 – 44313Combined sources
Helixi448 – 45811Combined sources
Helixi466 – 47712Combined sources
Helixi487 – 49913Combined sources
Helixi501 – 5033Combined sources
Helixi506 – 51611Combined sources
Beta strandi518 – 5236Combined sources
Helixi524 – 53411Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2ILRX-ray2.00A273-536[»]
ProteinModelPortaliQ9HB96.
SMRiQ9HB96. Positions 275-535.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9HB96.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni150 – 371222Interaction with FANCCAdd
BLAST

Phylogenomic databases

eggNOGiNOG42377.
GeneTreeiENSGT00390000000705.
HOGENOMiHOG000013179.
InParanoidiQ9HB96.
KOiK10892.
OMAiIQDQVPR.
OrthoDBiEOG7ZWD1V.
PhylomeDBiQ9HB96.
TreeFamiTF330720.

Family and domain databases

InterProiIPR021025. Fanconi_anaemia_gr_E_prot_C.
[Graphical view]
PfamiPF11510. FA_FANCE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9HB96-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MATPDAGLPG AEGVEPAPWA QLEAPARLLL QALQAGPEGA RRGLGVLRAL
60 70 80 90 100
GSRGWEPFDW GRLLEALCRE EPVVQGPDGR LELKPLLLRL PRICQRNLMS
110 120 130 140 150
LLMAVRPSLP ESGLLSVLQI AQQDLAPDPD AWLRALGELL RRDLGVGTSM
160 170 180 190 200
EGASPLSERC QRQLQSLCRG LGLGGRRLKS PQAPDPEEEE NRDSQQPGKR
210 220 230 240 250
RKDSEEEAAS PEGKRVPKRL RCWEEEEDHE KERPEHKSLE SLADGGSASP
260 270 280 290 300
IKDQPVMAVK TGEDGSNLDD AKGLAESLEL PKAIQDQLPR LQQLLKTLEE
310 320 330 340 350
GLEGLEDAPP VELQLLHECS PSQMDLLCAQ LQLPQLSDLG LLRLCTWLLA
360 370 380 390 400
LSPDLSLSNA TVLTRSLFLG RILSLTSSAS RLLTTALTSF CAKYTYPVCS
410 420 430 440 450
ALLDPVLQAP GTGPAQTELL CCLVKMESLE PDAQVLMLGQ ILELPWKEET
460 470 480 490 500
FLVLQSLLER QVEMTPEKFS VLMEKLCKKG LAATTSMAYA KLMLTVMTKY
510 520 530
QANITETQRL GLAMALEPNT TFLRKSLKAA LKHLGP
Length:536
Mass (Da):58,711
Last modified:March 1, 2001 - v1
Checksum:i0E94D8C469C791A5
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti89 – 891R → L.1 Publication
Corresponds to variant rs45600543 [ dbSNP | Ensembl ].
VAR_023372
Natural varianti184 – 1841P → Q in FA; uncertain pathological significance. 1 Publication
VAR_038022
Natural varianti204 – 2041S → L.1 Publication
Corresponds to variant rs7761870 [ dbSNP | Ensembl ].
VAR_023373
Natural varianti340 – 3401G → R.1 Publication
Corresponds to variant rs45524646 [ dbSNP | Ensembl ].
VAR_023374
Natural varianti343 – 3431R → Q.1 Publication
Corresponds to variant rs45467798 [ dbSNP | Ensembl ].
VAR_023375
Natural varianti502 – 5021A → T.1 Publication
Corresponds to variant rs9462088 [ dbSNP | Ensembl ].
VAR_023376

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF265210 mRNA. Translation: AAG16743.1.
DQ020173 Genomic DNA. Translation: AAY26395.1.
AK292522 mRNA. Translation: BAF85211.1.
AL022721 Genomic DNA. Translation: CAD92504.1.
CH471081 Genomic DNA. Translation: EAX03830.1.
BC046359 mRNA. Translation: AAH46359.1.
CCDSiCCDS4805.1.
RefSeqiNP_068741.1. NM_021922.2.
UniGeneiHs.302003.

Genome annotation databases

EnsembliENST00000229769; ENSP00000229769; ENSG00000112039.
GeneIDi2178.
KEGGihsa:2178.
UCSCiuc003oko.1. human.

Polymorphism databases

DMDMi45476978.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology
Fanconi Anemia Mutation Database
NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF265210 mRNA. Translation: AAG16743.1.
DQ020173 Genomic DNA. Translation: AAY26395.1.
AK292522 mRNA. Translation: BAF85211.1.
AL022721 Genomic DNA. Translation: CAD92504.1.
CH471081 Genomic DNA. Translation: EAX03830.1.
BC046359 mRNA. Translation: AAH46359.1.
CCDSiCCDS4805.1.
RefSeqiNP_068741.1. NM_021922.2.
UniGeneiHs.302003.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2ILRX-ray2.00A273-536[»]
ProteinModelPortaliQ9HB96.
SMRiQ9HB96. Positions 275-535.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108475. 17 interactions.
DIPiDIP-32845N.
IntActiQ9HB96. 4 interactions.
MINTiMINT-157013.
STRINGi9606.ENSP00000229769.

PTM databases

PhosphoSiteiQ9HB96.

Polymorphism databases

DMDMi45476978.

Proteomic databases

MaxQBiQ9HB96.
PaxDbiQ9HB96.
PRIDEiQ9HB96.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000229769; ENSP00000229769; ENSG00000112039.
GeneIDi2178.
KEGGihsa:2178.
UCSCiuc003oko.1. human.

Organism-specific databases

CTDi2178.
GeneCardsiGC06P037294.
GeneReviewsiFANCE.
HGNCiHGNC:3586. FANCE.
HPAiCAB014893.
MIMi600901. phenotype.
613976. gene.
neXtProtiNX_Q9HB96.
Orphaneti84. Fanconi anemia.
PharmGKBiPA28000.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG42377.
GeneTreeiENSGT00390000000705.
HOGENOMiHOG000013179.
InParanoidiQ9HB96.
KOiK10892.
OMAiIQDQVPR.
OrthoDBiEOG7ZWD1V.
PhylomeDBiQ9HB96.
TreeFamiTF330720.

Enzyme and pathway databases

ReactomeiREACT_18410. Fanconi Anemia pathway.

Miscellaneous databases

EvolutionaryTraceiQ9HB96.
GeneWikiiFANCE.
GenomeRNAii2178.
NextBioi8797.
PROiQ9HB96.
SOURCEiSearch...

Gene expression databases

BgeeiQ9HB96.
CleanExiHS_FANCE.
GenevestigatoriQ9HB96.

Family and domain databases

InterProiIPR021025. Fanconi_anaemia_gr_E_prot_C.
[Graphical view]
PfamiPF11510. FA_FANCE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [MRNA], DISEASE.
  2. NIEHS SNPs program
    Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS LEU-89; LEU-204; ARG-340; GLN-343 AND THR-502.
  3. "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: Testis.
  4. "The DNA sequence and analysis of human chromosome 6."
    Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
    , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
    Nature 425:805-811(2003) [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: Eye.
  7. "FANCE: the link between Fanconi anaemia complex assembly and activity."
    Pace P., Johnson M., Tan W.M., Mosedale G., Sng C., Hoatlin M.E., de Winter J.P., Joenje H., Gergely F., Patel K.J.
    EMBO J. 21:3414-3423(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  8. "Fanconi anemia protein complex: mapping protein interactions in the yeast 2- and 3-hybrid systems."
    Gordon S.M., Buchwald M.
    Blood 102:136-141(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH FANCC AND FANCD2.
  9. "A multiprotein nuclear complex connects Fanconi anemia and Bloom syndrome."
    Meetei A.R., Sechi S., Wallisch M., Yang D., Young M.K., Joenje H., Hoatlin M.E., Wang W.
    Mol. Cell. Biol. 23:3417-3426(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN A COMPLEX WITH FANCA; FANCC; FANCF; FANCG AND FANCL.
  10. Cited for: IDENTIFICATION IN A COMPLEX WITH FANCA; FANCB; FANCC; FANCF; FANCG AND FANCL.
  11. "A human ortholog of archaeal DNA repair protein Hef is defective in Fanconi anemia complementation group M."
    Meetei A.R., Medhurst A.L., Ling C., Xue Y., Singh T.R., Bier P., Steltenpool J., Stone S., Dokal I., Mathew C.G., Hoatlin M., Joenje H., de Winter J.P., Wang W.
    Nat. Genet. 37:958-963(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN A COMPLEX WITH FANCA; FANCB; FANCC; FANCF; FANCG; FANCL AND FANCM.
  12. "Chk1-mediated phosphorylation of FANCE is required for the Fanconi anemia/BRCA pathway."
    Wang X., Kennedy R.D., Ray K., Stuckert P., Ellenberger T., D'Andrea A.D.
    Mol. Cell. Biol. 27:3098-3108(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN DNA REPAIR, SUBCELLULAR LOCATION, PHOSPHORYLATION BY CHEK1 AT THR-346 AND SER-374, MUTAGENESIS OF THR-346 AND SER-374, UBIQUITINATION.
  13. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-249, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  14. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-249, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  15. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-249, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. "Regulation of Rev1 by the Fanconi anemia core complex."
    Kim H., Yang K., Dejsuphong D., D'Andrea A.D.
    Nat. Struct. Mol. Biol. 19:164-170(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE FA COMPLEX.
  17. Cited for: VARIANT FA GLN-184.

Entry informationi

Entry nameiFANCE_HUMAN
AccessioniPrimary (citable) accession number: Q9HB96
Secondary accession number(s): A8K907, Q4ZGH2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 15, 2004
Last sequence update: March 1, 2001
Last modified: February 4, 2015
This is version 121 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 6
    Human chromosome 6: 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

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.