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Protein

Mitotic checkpoint protein BUB3

Gene

BUB3

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

Functioni

Has a dual function in spindle-assembly checkpoint signaling and in promoting the establishment of correct kinetochore-microtubule (K-MT) attachments. Promotes the formation of stable end-on bipolar attachments. Necessary for kinetochore localization of BUB1. Regulates chromosome segregation during oocyte meiosis. The BUB1/BUB3 complex plays a role in the inhibition of anaphase-promoting complex or cyclosome (APC/C) when spindle-assembly checkpoint is activated and inhibits the ubiquitin ligase activity of APC/C by phosphorylating its activator CDC20. This complex can also phosphorylate MAD1L1.3 Publications

GO - Biological processi

  1. anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process Source: Reactome
  2. attachment of spindle microtubules to kinetochore Source: UniProtKB
  3. cell division Source: UniProtKB-KW
  4. meiotic cell cycle Source: UniProtKB-KW
  5. mitotic cell cycle Source: Reactome
  6. mitotic sister chromatid segregation Source: Ensembl
  7. mitotic spindle assembly checkpoint Source: Reactome
  8. negative regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle Source: Reactome
  9. regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle Source: Reactome
  10. spindle assembly checkpoint Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Cell cycle, Cell division, Chromosome partition, Meiosis, Mitosis

Enzyme and pathway databases

ReactomeiREACT_1072. Inactivation of APC/C via direct inhibition of the APC/C complex.
REACT_150425. Resolution of Sister Chromatid Cohesion.
REACT_150471. Separation of Sister Chromatids.
REACT_6781. APC/C:Cdc20 mediated degradation of mitotic proteins.
REACT_682. Mitotic Prometaphase.
SignaLinkiO43684.

Names & Taxonomyi

Protein namesi
Recommended name:
Mitotic checkpoint protein BUB3
Gene namesi
Name:BUB3
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 10

Organism-specific databases

HGNCiHGNC:1151. BUB3.

Subcellular locationi

Nucleus. Chromosomecentromerekinetochore By similarity
Note: Starts to localize at kinetochores in prometaphase I (Pro-MI) stage and maintains the localization until the metaphase I-anaphase I (MI-AI) transition.By similarity

GO - Cellular componenti

  1. condensed chromosome kinetochore Source: UniProtKB-SubCell
  2. cytosol Source: Reactome
  3. kinetochore Source: UniProtKB
  4. nucleoplasm Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Centromere, Chromosome, Kinetochore, Nucleus

Pathology & Biotechi

Organism-specific databases

Orphaneti1052. Mosaic variegated aneuploidy syndrome.
PharmGKBiPA25467.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 328328Mitotic checkpoint protein BUB3PRO_0000050891Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei179 – 1791N6-acetyllysine1 Publication
Modified residuei211 – 2111Phosphoserine1 Publication
Cross-linki216 – 216Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)

Post-translational modificationi

Poly-ADP-ribosylated by PARP1.By similarity

Keywords - PTMi

Acetylation, ADP-ribosylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiO43684.
PaxDbiO43684.
PRIDEiO43684.

PTM databases

PhosphoSiteiO43684.

Expressioni

Gene expression databases

BgeeiO43684.
CleanExiHS_BUB3.
ExpressionAtlasiO43684. baseline and differential.
GenevestigatoriO43684.

Organism-specific databases

HPAiCAB037075.
HPA003601.

Interactioni

Subunit structurei

Interacts with BUB1 and BUBR1. The BUB1/BUB3 complex interacts with MAD1L1. Interacts with ZNF207/BuGZ; leading to promote stability and kinetochore loading of BUB3.4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
BUB1BO605662EBI-1050987,EBI-1001438
Dynlt3Q5XI902EBI-1050987,EBI-1781818From a different organism.

Protein-protein interaction databases

BioGridi114621. 52 interactions.
DIPiDIP-24205N.
IntActiO43684. 33 interactions.
MINTiMINT-5005850.
STRINGi9606.ENSP00000357858.

Structurei

3D structure databases

ProteinModelPortaliO43684.
SMRiO43684. Positions 6-324.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati5 – 4339WD 1Add
BLAST
Repeati46 – 8338WD 2Add
BLAST
Repeati86 – 12439WD 3Add
BLAST
Repeati128 – 16336WD 4Add
BLAST
Repeati223 – 26240WD 5Add
BLAST

Sequence similaritiesi

Belongs to the WD repeat BUB3 family.Curated
Contains 5 WD repeats.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, WD repeat

Phylogenomic databases

eggNOGiCOG2319.
GeneTreeiENSGT00530000063440.
HOGENOMiHOG000208822.
HOVERGENiHBG002942.
InParanoidiO43684.
KOiK02180.
OMAiQSKKYAF.
OrthoDBiEOG7J4472.
PhylomeDBiO43684.
TreeFamiTF105454.

Family and domain databases

Gene3Di2.130.10.10. 1 hit.
InterProiIPR020472. G-protein_beta_WD-40_rep.
IPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR017986. WD40_repeat_dom.
[Graphical view]
PfamiPF00400. WD40. 3 hits.
[Graphical view]
PRINTSiPR00320. GPROTEINBRPT.
SMARTiSM00320. WD40. 6 hits.
[Graphical view]
SUPFAMiSSF50978. SSF50978. 1 hit.
PROSITEiPS50082. WD_REPEATS_2. 2 hits.
PS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: O43684-1) [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
MTGSNEFKLN QPPEDGISSV KFSPNTSQFL LVSSWDTSVR LYDVPANSMR
60 70 80 90 100
LKYQHTGAVL DCAFYDPTHA WSGGLDHQLK MHDLNTDQEN LVGTHDAPIR
110 120 130 140 150
CVEYCPEVNV MVTGSWDQTV KLWDPRTPCN AGTFSQPEKV YTLSVSGDRL
160 170 180 190 200
IVGTAGRRVL VWDLRNMGYV QQRRESSLKY QTRCIRAFPN KQGYVLSSIE
210 220 230 240 250
GRVAVEYLDP SPEVQKKKYA FKCHRLKENN IEQIYPVNAI SFHNIHNTFA
260 270 280 290 300
TGGSDGFVNI WDPFNKKRLC QFHRYPTSIA SLAFSNDGTT LAIASSYMYE
310 320
MDDTEHPEDG IFIRQVTDAE TKPKSPCT
Length:328
Mass (Da):37,155
Last modified:June 1, 1998 - v1
Checksum:i2915572A57368E5A
GO
Isoform 2 (identifier: O43684-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     326-328: PCT → T

Show »
Length:326
Mass (Da):36,955
Checksum:iF1EA57368E5A6345
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei326 – 3283PCT → T in isoform 2. 1 PublicationVSP_038655

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF047472 mRNA. Translation: AAC28438.1.
AF047473 mRNA. Translation: AAC28439.1.
AF053304 mRNA. Translation: AAC06258.1.
AF081496 mRNA. Translation: AAC36307.1.
AK312546 mRNA. Translation: BAG35444.1.
AC012391 Genomic DNA. No translation available.
CH471066 Genomic DNA. Translation: EAW49284.1.
CH471066 Genomic DNA. Translation: EAW49285.1.
CH471066 Genomic DNA. Translation: EAW49286.1.
BC005138 mRNA. Translation: AAH05138.1.
BC022438 mRNA. Translation: AAH22438.1.
CCDSiCCDS31306.1. [O43684-2]
CCDS7635.1. [O43684-1]
RefSeqiNP_001007794.1. NM_001007793.2. [O43684-2]
NP_004716.1. NM_004725.3. [O43684-1]
UniGeneiHs.418533.

Genome annotation databases

EnsembliENST00000368858; ENSP00000357851; ENSG00000154473. [O43684-2]
ENST00000368865; ENSP00000357858; ENSG00000154473. [O43684-1]
GeneIDi9184.
KEGGihsa:9184.
UCSCiuc001lhd.2. human. [O43684-2]
uc001lhe.2. human. [O43684-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF047472 mRNA. Translation: AAC28438.1.
AF047473 mRNA. Translation: AAC28439.1.
AF053304 mRNA. Translation: AAC06258.1.
AF081496 mRNA. Translation: AAC36307.1.
AK312546 mRNA. Translation: BAG35444.1.
AC012391 Genomic DNA. No translation available.
CH471066 Genomic DNA. Translation: EAW49284.1.
CH471066 Genomic DNA. Translation: EAW49285.1.
CH471066 Genomic DNA. Translation: EAW49286.1.
BC005138 mRNA. Translation: AAH05138.1.
BC022438 mRNA. Translation: AAH22438.1.
CCDSiCCDS31306.1. [O43684-2]
CCDS7635.1. [O43684-1]
RefSeqiNP_001007794.1. NM_001007793.2. [O43684-2]
NP_004716.1. NM_004725.3. [O43684-1]
UniGeneiHs.418533.

3D structure databases

ProteinModelPortaliO43684.
SMRiO43684. Positions 6-324.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi114621. 52 interactions.
DIPiDIP-24205N.
IntActiO43684. 33 interactions.
MINTiMINT-5005850.
STRINGi9606.ENSP00000357858.

PTM databases

PhosphoSiteiO43684.

Proteomic databases

MaxQBiO43684.
PaxDbiO43684.
PRIDEiO43684.

Protocols and materials databases

DNASUi9184.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000368858; ENSP00000357851; ENSG00000154473. [O43684-2]
ENST00000368865; ENSP00000357858; ENSG00000154473. [O43684-1]
GeneIDi9184.
KEGGihsa:9184.
UCSCiuc001lhd.2. human. [O43684-2]
uc001lhe.2. human. [O43684-1]

Organism-specific databases

CTDi9184.
GeneCardsiGC10P124903.
HGNCiHGNC:1151. BUB3.
HPAiCAB037075.
HPA003601.
MIMi603719. gene.
neXtProtiNX_O43684.
Orphaneti1052. Mosaic variegated aneuploidy syndrome.
PharmGKBiPA25467.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG2319.
GeneTreeiENSGT00530000063440.
HOGENOMiHOG000208822.
HOVERGENiHBG002942.
InParanoidiO43684.
KOiK02180.
OMAiQSKKYAF.
OrthoDBiEOG7J4472.
PhylomeDBiO43684.
TreeFamiTF105454.

Enzyme and pathway databases

ReactomeiREACT_1072. Inactivation of APC/C via direct inhibition of the APC/C complex.
REACT_150425. Resolution of Sister Chromatid Cohesion.
REACT_150471. Separation of Sister Chromatids.
REACT_6781. APC/C:Cdc20 mediated degradation of mitotic proteins.
REACT_682. Mitotic Prometaphase.
SignaLinkiO43684.

Miscellaneous databases

ChiTaRSiBUB3. human.
GeneWikiiBUB3.
GenomeRNAii9184.
NextBioi34433.
PROiO43684.
SOURCEiSearch...

Gene expression databases

BgeeiO43684.
CleanExiHS_BUB3.
ExpressionAtlasiO43684. baseline and differential.
GenevestigatoriO43684.

Family and domain databases

Gene3Di2.130.10.10. 1 hit.
InterProiIPR020472. G-protein_beta_WD-40_rep.
IPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR017986. WD40_repeat_dom.
[Graphical view]
PfamiPF00400. WD40. 3 hits.
[Graphical view]
PRINTSiPR00320. GPROTEINBRPT.
SMARTiSM00320. WD40. 6 hits.
[Graphical view]
SUPFAMiSSF50978. SSF50978. 1 hit.
PROSITEiPS50082. WD_REPEATS_2. 2 hits.
PS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Phosphorylation of human MAD1 by the BUB1 kinase in vitro."
    Seeley T.W., Wang L., Zhen J.Y.
    Biochem. Biophys. Res. Commun. 257:589-595(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, INTERACTION WITH BUB1 AND MAD1L1.
    Tissue: Spleen and Testis.
  2. "The human homologue of Bub3 is required for kinetochore localization of Bub1 and a Mad3/Bub1-related protein kinase."
    Taylor S.S., Ha E., McKeon F.
    J. Cell Biol. 142:1-11(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  3. "Human BUB3 is a kinetochore protein that interacts with hBUB1 and hBUBR1."
    Chan G.K.T., Yen T.J.
    Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  4. "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] (ISOFORM 1).
    Tissue: Tongue.
  5. "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].
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "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: Brain and Placenta.
  8. "Phosphorylation of Cdc20 by Bub1 provides a catalytic mechanism for APC/C inhibition by the spindle checkpoint."
    Tang Z., Shu H., Oncel D., Chen S., Yu H.
    Mol. Cell 16:387-397(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH BUB1.
  9. "The human spindle assembly checkpoint protein Bub3 is required for the establishment of efficient kinetochore-microtubule attachments."
    Logarinho E., Resende T., Torres C., Bousbaa H.
    Mol. Biol. Cell 19:1798-1813(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-211, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. "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-179, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "A microtubule-associated zinc finger protein, BuGZ, regulates mitotic chromosome alignment by ensuring Bub3 stability and kinetochore targeting."
    Jiang H., He X., Wang S., Jia J., Wan Y., Wang Y., Zeng R., Yates J. III, Zhu X., Zheng Y.
    Dev. Cell 28:268-281(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ZNF207.
  14. "BuGZ is required for Bub3 stability, Bub1 kinetochore function, and chromosome alignment."
    Toledo C.M., Herman J.A., Olsen J.B., Ding Y., Corrin P., Girard E.J., Olson J.M., Emili A., Deluca J.G., Paddison P.J.
    Dev. Cell 28:282-294(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ZNF207.

Entry informationi

Entry nameiBUB3_HUMAN
AccessioniPrimary (citable) accession number: O43684
Secondary accession number(s): A6NJ42
, B2R6E7, D3DRE9, O43685
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: June 1, 1998
Last modified: February 4, 2015
This is version 140 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

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. 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.