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Q9Y3B2

- EXOS1_HUMAN

UniProt

Q9Y3B2 - EXOS1_HUMAN

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Protein

Exosome complex component CSL4

Gene

EXOSC1

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

Functioni

Non-catalytic component of the RNA exosome complex which has 3'->5' exoribonuclease activity and participates in a multitude of cellular RNA processing and degradation events. In the nucleus, the RNA exosome complex is involved in proper maturation of stable RNA species such as rRNA, snRNA and snoRNA, in the elimination of RNA processing by-products and non-coding 'pervasive' transcripts, such as antisense RNA species and promoter-upstream transcripts (PROMPTs), and of mRNAs with processing defects, thereby limiting or excluding their export to the cytoplasm. The RNA exosome may be involved in Ig class switch recombination (CSR) and/or Ig variable region somatic hypermutation (SHM) by targeting AICDA deamination activity to transcribed dsDNA substrates. In the cytoplasm, the RNA exosome complex is involved in general mRNA turnover and specifically degrades inherently unstable mRNAs containing AU-rich elements (AREs) within their 3' untranslated regions, and in RNA surveillance pathways, preventing translation of aberrant mRNAs. It seems to be involved in degradation of histone mRNA. The catalytic inactive RNA exosome core complex of 9 subunits (Exo-9) is proposed to play a pivotal role in the binding and presentation of RNA for ribonucleolysis, and to serve as a scaffold for the association with catalytic subunits and accessory proteins or complexes. EXOSC1 as peripheral part of the Exo-9 complex stabilizes the hexameric ring of RNase PH-domain subunits through contacts with EXOSC6 and EXOSC8.

GO - Molecular functioni

  1. RNA binding Source: UniProtKB

GO - Biological processi

  1. exonucleolytic nuclear-transcribed mRNA catabolic process involved in deadenylation-dependent decay Source: Reactome
  2. gene expression Source: Reactome
  3. mRNA metabolic process Source: Reactome
  4. nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay Source: Reactome
  5. RNA metabolic process Source: Reactome
  6. rRNA processing Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

rRNA processing

Keywords - Ligandi

RNA-binding

Enzyme and pathway databases

ReactomeiREACT_18355. ATF4 activates genes.
REACT_20619. mRNA decay by 3' to 5' exoribonuclease.
REACT_24915. Butyrate Response Factor 1 (BRF1) destabilizes mRNA.
REACT_25042. KSRP destabilizes mRNA.
REACT_25064. Tristetraprolin (TTP) destabilizes mRNA.

Names & Taxonomyi

Protein namesi
Recommended name:
Exosome complex component CSL4
Alternative name(s):
Exosome component 1
Gene namesi
Name:EXOSC1
Synonyms:CSL4
ORF Names:CGI-108
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 10

Organism-specific databases

HGNCiHGNC:17286. EXOSC1.

Subcellular locationi

Nucleusnucleolus 1 Publication. Nucleus 1 Publication. Cytoplasm 1 Publication

GO - Cellular componenti

  1. cytosol Source: Reactome
  2. exosome (RNase complex) Source: UniProtKB
  3. nucleolus Source: UniProtKB
  4. nucleus Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Exosome, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134900737.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 195195Exosome complex component CSL4PRO_0000087127Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei21 – 211Phosphoserine3 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9Y3B2.
PaxDbiQ9Y3B2.
PRIDEiQ9Y3B2.

PTM databases

PhosphoSiteiQ9Y3B2.

Expressioni

Gene expression databases

BgeeiQ9Y3B2.
CleanExiHS_EXOSC1.
ExpressionAtlasiQ9Y3B2. baseline and differential.
GenevestigatoriQ9Y3B2.

Organism-specific databases

HPAiHPA038370.

Interactioni

Subunit structurei

Component of the RNA exosome complex. Specifically part of the catalytically inactive RNA exosome core (Exo-9) complex which is believed to associate with catalytic subunits EXOSC10, and DIS3 or DIS3L in cytoplasmic- and nuclear-specific RNA exosome complex forms. Exo-9 is formed by a hexameric ring of RNase PH domain-containing subunits specifically containing the heterodimers EXOSC4-EXOSC9, EXOSC5-EXOSC8 and EXOSC6-EXOSC7, and peripheral S1 domain-containing components EXOSC1, EXOSC2 and EXOSC3 located on the top of the ring structure. Interacts with EXOSC5, EXOSC7 and EXOSC10. Interacts with DDX60.4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
EXOSC4Q9NPD34EBI-371892,EBI-371823
EXOSC5Q9NQT410EBI-371892,EBI-371876
EXOSC7Q150246EBI-371892,EBI-371841

Protein-protein interaction databases

BioGridi119220. 27 interactions.
IntActiQ9Y3B2. 25 interactions.
MINTiMINT-3085607.
STRINGi9606.ENSP00000359939.

Structurei

Secondary structure

1
195
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi13 – 164
Turni17 – 193
Beta strandi23 – 253
Beta strandi27 – 293
Beta strandi32 – 343
Beta strandi41 – 455
Beta strandi49 – 524
Beta strandi70 – 789
Beta strandi80 – 9314
Beta strandi103 – 1064
Helixi107 – 1093
Helixi118 – 1203
Beta strandi124 – 13512
Beta strandi142 – 1454
Beta strandi148 – 1503
Beta strandi159 – 1613
Beta strandi165 – 1684
Beta strandi171 – 1733
Turni175 – 1784

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2NN6X-ray3.35I1-195[»]
ProteinModelPortaliQ9Y3B2.
SMRiQ9Y3B2. Positions 6-185.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9Y3B2.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini66 – 14782S1 motifAdd
BLAST

Sequence similaritiesi

Belongs to the CSL4 family.Curated
Contains 1 S1 motif domain.Curated

Phylogenomic databases

eggNOGiCOG1096.
GeneTreeiENSGT00390000015287.
HOGENOMiHOG000177330.
HOVERGENiHBG051516.
InParanoidiQ9Y3B2.
KOiK07573.
OMAiVTSINPR.
OrthoDBiEOG7V4B0J.
PhylomeDBiQ9Y3B2.
TreeFamiTF316607.

Family and domain databases

InterProiIPR019495. EXOSC1.
IPR025721. Exosome_cplx_N_dom.
IPR012340. NA-bd_OB-fold.
IPR022967. S1_dom.
[Graphical view]
PfamiPF14382. ECR1_N. 1 hit.
PF10447. EXOSC1. 1 hit.
[Graphical view]
SMARTiSM00316. S1. 1 hit.
[Graphical view]
SUPFAMiSSF50249. SSF50249. 1 hit.

Sequencei

Sequence statusi: Complete.

Q9Y3B2-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAPPVRYCIP GERLCNLEEG SPGSGTYTRH GYIFSSLAGC LMKSSENGAL
60 70 80 90 100
PVVSVVRETE SQLLPDVGAI VTCKVSSINS RFAKVHILYV GSMPLKNSFR
110 120 130 140 150
GTIRKEDVRA TEKDKVEIYK SFRPGDIVLA KVISLGDAQS NYLLTTAENE
160 170 180 190
LGVVVAHSES GIQMVPISWC EMQCPKTHTK EFRKVARVQP EFLQT
Length:195
Mass (Da):21,452
Last modified:November 1, 1999 - v1
Checksum:iE9C3B0A66F911195
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF151866 mRNA. Translation: AAD34103.1.
AK313717 mRNA. Translation: BAG36460.1.
AL355490 Genomic DNA. Translation: CAI40782.1.
CH471066 Genomic DNA. Translation: EAW49936.1.
BC022067 mRNA. Translation: AAH22067.1.
CCDSiCCDS7459.1.
RefSeqiNP_057130.1. NM_016046.3.
UniGeneiHs.632089.

Genome annotation databases

EnsembliENST00000370902; ENSP00000359939; ENSG00000171311.
GeneIDi51013.
KEGGihsa:51013.
UCSCiuc001kni.3. human.

Polymorphism databases

DMDMi14285410.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF151866 mRNA. Translation: AAD34103.1 .
AK313717 mRNA. Translation: BAG36460.1 .
AL355490 Genomic DNA. Translation: CAI40782.1 .
CH471066 Genomic DNA. Translation: EAW49936.1 .
BC022067 mRNA. Translation: AAH22067.1 .
CCDSi CCDS7459.1.
RefSeqi NP_057130.1. NM_016046.3.
UniGenei Hs.632089.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2NN6 X-ray 3.35 I 1-195 [» ]
ProteinModelPortali Q9Y3B2.
SMRi Q9Y3B2. Positions 6-185.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 119220. 27 interactions.
IntActi Q9Y3B2. 25 interactions.
MINTi MINT-3085607.
STRINGi 9606.ENSP00000359939.

PTM databases

PhosphoSitei Q9Y3B2.

Polymorphism databases

DMDMi 14285410.

Proteomic databases

MaxQBi Q9Y3B2.
PaxDbi Q9Y3B2.
PRIDEi Q9Y3B2.

Protocols and materials databases

DNASUi 51013.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000370902 ; ENSP00000359939 ; ENSG00000171311 .
GeneIDi 51013.
KEGGi hsa:51013.
UCSCi uc001kni.3. human.

Organism-specific databases

CTDi 51013.
GeneCardsi GC10M099205.
HGNCi HGNC:17286. EXOSC1.
HPAi HPA038370.
MIMi 606493. gene.
neXtProti NX_Q9Y3B2.
PharmGKBi PA134900737.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG1096.
GeneTreei ENSGT00390000015287.
HOGENOMi HOG000177330.
HOVERGENi HBG051516.
InParanoidi Q9Y3B2.
KOi K07573.
OMAi VTSINPR.
OrthoDBi EOG7V4B0J.
PhylomeDBi Q9Y3B2.
TreeFami TF316607.

Enzyme and pathway databases

Reactomei REACT_18355. ATF4 activates genes.
REACT_20619. mRNA decay by 3' to 5' exoribonuclease.
REACT_24915. Butyrate Response Factor 1 (BRF1) destabilizes mRNA.
REACT_25042. KSRP destabilizes mRNA.
REACT_25064. Tristetraprolin (TTP) destabilizes mRNA.

Miscellaneous databases

EvolutionaryTracei Q9Y3B2.
GeneWikii Exosome_component_1.
GenomeRNAii 51013.
NextBioi 53508.
PROi Q9Y3B2.
SOURCEi Search...

Gene expression databases

Bgeei Q9Y3B2.
CleanExi HS_EXOSC1.
ExpressionAtlasi Q9Y3B2. baseline and differential.
Genevestigatori Q9Y3B2.

Family and domain databases

InterProi IPR019495. EXOSC1.
IPR025721. Exosome_cplx_N_dom.
IPR012340. NA-bd_OB-fold.
IPR022967. S1_dom.
[Graphical view ]
Pfami PF14382. ECR1_N. 1 hit.
PF10447. EXOSC1. 1 hit.
[Graphical view ]
SMARTi SM00316. S1. 1 hit.
[Graphical view ]
SUPFAMi SSF50249. SSF50249. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Identification of novel human genes evolutionarily conserved in Caenorhabditis elegans by comparative proteomics."
    Lai C.-H., Chou C.-Y., Ch'ang L.-Y., Liu C.-S., Lin W.-C.
    Genome Res. 10:703-713(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE 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].
  3. "The DNA sequence and comparative analysis of human chromosome 10."
    Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J.
    , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
    Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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.
  6. "AU binding proteins recruit the exosome to degrade ARE-containing mRNAs."
    Chen C.-Y., Gherzi R., Ong S.-E., Chan E.L., Raijmakers R., Pruijn G.J.M., Stoecklin G., Moroni C., Mann M., Karin M.
    Cell 107:451-464(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE RNA EXOSOME CORE COMPLEX.
  7. "Protein-protein interactions between human exosome components support the assembly of RNase PH-type subunits into a six-membered PNPase-like ring."
    Raijmakers R., Vree Egberts W., van Venrooij W.J., Pruijn G.J.M.
    J. Mol. Biol. 323:653-663(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN INTERACTION.
  8. "Protein-protein interactions of hCsl4p with other human exosome subunits."
    Raijmakers R., Noordman Y.E., van Venrooij W.J., Pruijn G.J.M.
    J. Mol. Biol. 315:809-818(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, INTERACTION WITH EXOSC5; EXOSC7 AND EXOSC10.
  9. "A protein interaction framework for human mRNA degradation."
    Lehner B., Sanderson C.M.
    Genome Res. 14:1315-1323(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN INTERACTION.
  10. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
    Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
    Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. "Dis3-like 1: a novel exoribonuclease associated with the human exosome."
    Staals R.H., Bronkhorst A.W., Schilders G., Slomovic S., Schuster G., Heck A.J., Raijmakers R., Pruijn G.J.
    EMBO J. 29:2358-2367(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE RNA EXOSOME COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY.
  13. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. "DDX60, a DEXD/H box helicase, is a novel antiviral factor promoting RIG-I-like receptor-mediated signaling."
    Miyashita M., Oshiumi H., Matsumoto M., Seya T.
    Mol. Cell. Biol. 31:3802-3819(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH DDX60.
  16. "Reconstitution, activities, and structure of the eukaryotic RNA exosome."
    Liu Q., Greimann J.C., Lima C.D.
    Cell 127:1223-1237(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.35 ANGSTROMS), RECONSTITUTION OF THE RNA EXOSOME CORE COMPLEX.
  17. Erratum
    Liu Q., Greimann J.C., Lima C.D.
    Cell 131:188-189(2007)

Entry informationi

Entry nameiEXOS1_HUMAN
AccessioniPrimary (citable) accession number: Q9Y3B2
Secondary accession number(s): B2R9B3, Q5JTH3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 2001
Last sequence update: November 1, 1999
Last modified: October 29, 2014
This is version 132 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 10
    Human chromosome 10: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3