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Protein

Pescadillo homolog

Gene

PES1

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

Functioni

Component of the PeBoW complex, which is required for maturation of 28S and 5.8S ribosomal RNAs and formation of the 60S ribosome.UniRule annotation3 Publications

GO - Molecular functioni

  1. poly(A) RNA binding Source: UniProtKB
  2. ribonucleoprotein complex binding Source: UniProtKB-HAMAP

GO - Biological processi

  1. cell proliferation Source: UniProtKB
  2. maturation of 5.8S rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) Source: UniProtKB
  3. maturation of LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) Source: UniProtKB
  4. nucleolus organization Source: Ensembl
  5. protein localization to organelle Source: Ensembl
  6. regulation of cell cycle Source: UniProtKB
  7. ribosomal large subunit biogenesis Source: UniProtKB
  8. rRNA processing Source: MGI
Complete GO annotation...

Keywords - Biological processi

Ribosome biogenesis, rRNA processing

Enzyme and pathway databases

SignaLinkiO00541.

Names & Taxonomyi

Protein namesi
Recommended name:
Pescadillo homologUniRule annotation
Gene namesi
Name:PES1UniRule annotation
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 22

Organism-specific databases

HGNCiHGNC:8848. PES1.

Subcellular locationi

  1. Nucleusnucleolus
  2. Nucleusnucleoplasm
  3. Chromosome

  4. Note: Appears to localize to the periphery of metaphase chromosomes during mitosis and to the prenucleolar bodies that form in mitotic cells prior to the actual nucleoli.UniRule annotation

GO - Cellular componenti

  1. condensed chromosome Source: Ensembl
  2. cytoplasm Source: HPA
  3. membrane Source: UniProtKB
  4. nucleolus Source: UniProtKB
  5. nucleoplasm Source: UniProtKB
  6. nucleus Source: HPA
  7. PeBoW complex Source: UniProtKB
  8. preribosome, large subunit precursor Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi327 – 3271F → R: Reduces incorporation into the PeBoW complex and nucleolar localization and impairs maturation of 28S ribosomal RNA. 1 Publication
Mutagenesisi347 – 3471I → R: Reduces incorporation into the PeBoW complex and nucleolar localization and impairs maturation of 28S ribosomal RNA. 1 Publication
Mutagenesisi380 – 3801R → W: Slightly impairs nucleolar localization. 1 Publication
Mutagenesisi397 – 3971W → R: Reduces incorporation into the PeBoW complex and nucleolar localization and impairs maturation of 28S ribosomal RNA. 1 Publication

Organism-specific databases

PharmGKBiPA33190.

Polymorphism and mutation databases

BioMutaiPES1.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 588588Pescadillo homologPRO_0000186188Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei98 – 981N6-acetyllysine1 Publication

Post-translational modificationi

Sumoylated.

Keywords - PTMi

Acetylation, Ubl conjugation

Proteomic databases

MaxQBiO00541.
PaxDbiO00541.
PRIDEiO00541.

2D gel databases

SWISS-2DPAGEO00541.

PTM databases

PhosphoSiteiO00541.

Expressioni

Tissue specificityi

Significant levels are detected in a variety of cancer cell lines, including glioblastoma, breast carcinoma, colon carcinoma and cervical carcinoma cells. Levels are abnormally elevated in malignant tumors of astrocytic origin.

Inductioni

By MYC.1 Publication

Gene expression databases

BgeeiO00541.
CleanExiHS_PES1.
ExpressionAtlasiO00541. baseline and differential.
GenevestigatoriO00541.

Organism-specific databases

HPAiHPA040210.
HPA062439.

Interactioni

Subunit structurei

Interacts with IRS1 and UBTF. May interact with MAP1B (By similarity). Component of the PeBoW complex, composed of BOP1, PES1 and WDR12. Within the PeBoW complex BOP1 interacts directly with PES1 and WDR12. The PeBoW complex also associates with the 66S pre-ribosome.By similarity4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
BOP1Q141373EBI-1053271,EBI-1050828

Protein-protein interaction databases

BioGridi117040. 30 interactions.
IntActiO00541. 5 interactions.
MINTiMINT-2997852.
STRINGi9606.ENSP00000346725.

Structurei

Secondary structure

1
588
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi331 – 3333Combined sources
Beta strandi336 – 3383Combined sources
Helixi340 – 34910Combined sources
Beta strandi353 – 3553Combined sources
Turni358 – 3603Combined sources
Beta strandi375 – 3773Combined sources
Turni381 – 3833Combined sources
Beta strandi390 – 3934Combined sources
Helixi396 – 4049Combined sources
Turni410 – 4123Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2EP8NMR-A322-414[»]
ProteinModelPortaliO00541.
SMRiO00541. Positions 322-414.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO00541.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini322 – 41594BRCTUniRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 257257Sufficient for nucleolar localizationAdd
BLAST
Regioni1 – 5454Required for 28S ribosomal RNA processingAdd
BLAST
Regioni306 – 415110Sufficient for interaction with MAP1BBy similarityAdd
BLAST
Regioni539 – 58850Required for 28S ribosomal RNA processingAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi456 – 53176Glu-richAdd
BLAST

Sequence similaritiesi

Belongs to the pescadillo family.UniRule annotation
Contains 1 BRCT domain.UniRule annotation

Phylogenomic databases

eggNOGiCOG5163.
GeneTreeiENSGT00390000002626.
HOGENOMiHOG000006022.
HOVERGENiHBG023409.
InParanoidiO00541.
KOiK14843.
OMAiYDKIMFG.
OrthoDBiEOG7X9G6N.
PhylomeDBiO00541.
TreeFamiTF300671.

Family and domain databases

Gene3Di3.40.50.10190. 1 hit.
HAMAPiMF_03028. Pescadillo.
InterProiIPR001357. BRCT_dom.
IPR010613. PES.
[Graphical view]
PfamiPF00533. BRCT. 1 hit.
PF06732. Pescadillo_N. 1 hit.
[Graphical view]
SMARTiSM00292. BRCT. 1 hit.
[Graphical view]
SUPFAMiSSF52113. SSF52113. 1 hit.
PROSITEiPS50172. BRCT. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: O00541-1) [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
MGGLEKKKYE RGSATNYITR NKARKKLQLS LADFRRLCIL KGIYPHEPKH
60 70 80 90 100
KKKVNKGSTA ARTFYLIKDI RFLLHEPIVN KFREYKVFVR KLRKAYGKSE
110 120 130 140 150
WNTVERLKDN KPNYKLDHII KERYPTFIDA LRDLDDALSM CFLFSTFPRT
160 170 180 190 200
GKCHVQTIQL CRRLTVEFMH YIIAARALRK VFLSIKGIYY QAEVLGQPIV
210 220 230 240 250
WITPYAFSHD HPTDVDYRVM ATFTEFYTTL LGFVNFRLYQ LLNLHYPPKL
260 270 280 290 300
EGQAQAEAKA GEGTYALDSE SCMEKLAALS ASLARVVVPA TEEEAEVDEF
310 320 330 340 350
PTDGEMSAQE EDRRKELEAQ EKHKKLFEGL KFFLNREVPR EALAFIIRSF
360 370 380 390 400
GGEVSWDKSL CIGATYDVTD SRITHQIVDR PGQQTSVIGR CYVQPQWVFD
410 420 430 440 450
SVNARLLLPV AEYFSGVQLP PHLSPFVTEK EGDYVPPEKL KLLALQRGED
460 470 480 490 500
PGNLNESEEE EEEDDNNEGD GDEEGENEEE EEDAEAGSEK EEEARLAALE
510 520 530 540 550
EQRMEGKKPR VMAGTLKLED KQRLAQEEES EAKRLAIMMM KKREKYLYQK
560 570 580
IMFGKRRKIR EANKLAEKRK AHDEAVRSEK KAKKARPE
Length:588
Mass (Da):68,003
Last modified:July 1, 1997 - v1
Checksum:iCB6201D6E34D82B1
GO
Isoform 2 (identifier: O00541-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     306-310: Missing.

Show »
Length:583
Mass (Da):67,456
Checksum:i89BEC8BB4328F707
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti264 – 2641T → S.
Corresponds to variant rs42942 [ dbSNP | Ensembl ].
VAR_034375
Natural varianti370 – 3701D → H.
Corresponds to variant rs11541876 [ dbSNP | Ensembl ].
VAR_053570
Natural varianti411 – 4111A → T.
Corresponds to variant rs34123894 [ dbSNP | Ensembl ].
VAR_053571

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei306 – 3105Missing in isoform 2. 1 PublicationVSP_013023

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U78310 mRNA. Translation: AAB61140.1.
CR456539 mRNA. Translation: CAG30425.1.
AC005006 Genomic DNA. No translation available.
BC032489 mRNA. Translation: AAH32489.1.
CCDSiCCDS13880.1. [O00541-1]
CCDS58802.1. [O00541-2]
RefSeqiNP_001230154.1. NM_001243225.1. [O00541-2]
NP_055118.1. NM_014303.3. [O00541-1]
UniGeneiHs.517543.

Genome annotation databases

EnsembliENST00000335214; ENSP00000334612; ENSG00000100029. [O00541-2]
ENST00000354694; ENSP00000346725; ENSG00000100029. [O00541-1]
GeneIDi23481.
KEGGihsa:23481.
UCSCiuc003aij.2. human. [O00541-1]
uc003aik.2. human. [O00541-2]

Polymorphism and mutation databases

BioMutaiPES1.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U78310 mRNA. Translation: AAB61140.1.
CR456539 mRNA. Translation: CAG30425.1.
AC005006 Genomic DNA. No translation available.
BC032489 mRNA. Translation: AAH32489.1.
CCDSiCCDS13880.1. [O00541-1]
CCDS58802.1. [O00541-2]
RefSeqiNP_001230154.1. NM_001243225.1. [O00541-2]
NP_055118.1. NM_014303.3. [O00541-1]
UniGeneiHs.517543.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2EP8NMR-A322-414[»]
ProteinModelPortaliO00541.
SMRiO00541. Positions 322-414.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi117040. 30 interactions.
IntActiO00541. 5 interactions.
MINTiMINT-2997852.
STRINGi9606.ENSP00000346725.

PTM databases

PhosphoSiteiO00541.

Polymorphism and mutation databases

BioMutaiPES1.

2D gel databases

SWISS-2DPAGEO00541.

Proteomic databases

MaxQBiO00541.
PaxDbiO00541.
PRIDEiO00541.

Protocols and materials databases

DNASUi23481.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000335214; ENSP00000334612; ENSG00000100029. [O00541-2]
ENST00000354694; ENSP00000346725; ENSG00000100029. [O00541-1]
GeneIDi23481.
KEGGihsa:23481.
UCSCiuc003aij.2. human. [O00541-1]
uc003aik.2. human. [O00541-2]

Organism-specific databases

CTDi23481.
GeneCardsiGC22M030972.
HGNCiHGNC:8848. PES1.
HPAiHPA040210.
HPA062439.
MIMi605819. gene.
neXtProtiNX_O00541.
PharmGKBiPA33190.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG5163.
GeneTreeiENSGT00390000002626.
HOGENOMiHOG000006022.
HOVERGENiHBG023409.
InParanoidiO00541.
KOiK14843.
OMAiYDKIMFG.
OrthoDBiEOG7X9G6N.
PhylomeDBiO00541.
TreeFamiTF300671.

Enzyme and pathway databases

SignaLinkiO00541.

Miscellaneous databases

ChiTaRSiPES1. human.
EvolutionaryTraceiO00541.
GeneWikiiPES1.
GenomeRNAii23481.
NextBioi45839.
PROiO00541.
SOURCEiSearch...

Gene expression databases

BgeeiO00541.
CleanExiHS_PES1.
ExpressionAtlasiO00541. baseline and differential.
GenevestigatoriO00541.

Family and domain databases

Gene3Di3.40.50.10190. 1 hit.
HAMAPiMF_03028. Pescadillo.
InterProiIPR001357. BRCT_dom.
IPR010613. PES.
[Graphical view]
PfamiPF00533. BRCT. 1 hit.
PF06732. Pescadillo_N. 1 hit.
[Graphical view]
SMARTiSM00292. BRCT. 1 hit.
[Graphical view]
SUPFAMiSSF52113. SSF52113. 1 hit.
PROSITEiPS50172. BRCT. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Insertional mutagenesis in zebrafish identifies two novel genes, pescadillo and dead eye, essential for embryonic development."
    Allende M.L., Amsterdam A., Becker T., Kawakami K., Gaiano N., Hopkins N.
    Genes Dev. 10:3141-3155(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
  3. "The DNA sequence of human chromosome 22."
    Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M.
    , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H.
    Nature 402:489-495(1999) [PubMed] [Europe PMC] [Abstract]
    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] (ISOFORM 1).
    Tissue: Mammary gland.
  5. Cited for: CHARACTERIZATION.
  6. "Yeast Pescadillo is required for multiple activities during 60S ribosomal subunit synthesis."
    Oeffinger M., Leung A., Lamond A., Tollervey D.
    RNA 8:626-636(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  7. Erratum
    Oeffinger M., Leung A., Lamond A., Tollervey D.
    RNA 8:851-851(2002)
  8. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. "Mammalian WDR12 is a novel member of the Pes1-Bop1 complex and is required for ribosome biogenesis and cell proliferation."
    Hoelzel M., Rohrmoser M., Schlee M., Grimm T., Harasim T., Malamoussi A., Gruber-Eber A., Kremmer E., Hiddemann W., Bornkamm G.W., Eick D.
    J. Cell Biol. 170:367-378(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH BOP1 AND WDR12, INDUCTION.
  10. "Dominant-negative Pes1 mutants inhibit ribosomal RNA processing and cell proliferation via incorporation into the PeBoW-complex."
    Grimm T., Hoelzel M., Rohrmoser M., Harasim T., Malamoussi A., Gruber-Eber A., Kremmer E., Eick D.
    Nucleic Acids Res. 34:3030-3043(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH BOP1 AND WDR12, SUBCELLULAR LOCATION.
  11. "Interdependence of Pes1, Bop1, and WDR12 controls nucleolar localization and assembly of the PeBoW complex required for maturation of the 60S ribosomal subunit."
    Rohrmoser M., Hoelzel M., Grimm T., Malamoussi A., Harasim T., Orban M., Pfisterer I., Gruber-Eber A., Kremmer E., Eick D.
    Mol. Cell. Biol. 27:3682-3694(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH BOP1 AND WDR12.
  12. "The BRCT domain of mammalian Pes1 is crucial for nucleolar localization and rRNA processing."
    Hoelzel M., Grimm T., Rohrmoser M., Malamoussi A., Harasim T., Gruber-Eber A., Kremmer E., Eick D.
    Nucleic Acids Res. 35:789-800(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH BOP1 AND WDR12, SUBCELLULAR LOCATION, MUTAGENESIS OF PHE-327; ILE-347; ARG-380 AND TRP-397.
  13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  14. "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-98, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  17. "Solution structure of the BRCT domain from human pescadillo homolog 1."
    RIKEN structural genomics initiative (RSGI)
    Submitted (OCT-2007) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 322-414.

Entry informationi

Entry nameiPESC_HUMAN
AccessioniPrimary (citable) accession number: O00541
Secondary accession number(s): Q6IC29
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 20, 2002
Last sequence update: July 1, 1997
Last modified: April 29, 2015
This is version 135 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 22
    Human chromosome 22: 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

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.