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Protein

Cyclin-A1

Gene

CCNA1

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

Functioni

May be involved in the control of the cell cycle at the G1/S (start) and G2/M (mitosis) transitions. May primarily function in the control of the germline meiotic cell cycle and additionally in the control of mitotic cell cycle in some somatic cells.1 Publication

GO - Biological processi

  1. cell division Source: UniProtKB-KW
  2. G1/S transition of mitotic cell cycle Source: Reactome
  3. G2/M transition of mitotic cell cycle Source: Reactome
  4. male meiosis I Source: ProtInc
  5. mitotic cell cycle Source: Reactome
  6. mitotic nuclear division Source: UniProtKB-KW
  7. regulation of cyclin-dependent protein serine/threonine kinase activity Source: InterPro
  8. regulation of G2/M transition of mitotic cell cycle Source: InterPro
  9. regulation of transcription involved in G1/S transition of mitotic cell cycle Source: Reactome
  10. spermatogenesis Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

Cyclin

Keywords - Biological processi

Cell cycle, Cell division, Mitosis

Enzyme and pathway databases

ReactomeiREACT_111214. G0 and Early G1.
REACT_1156. Orc1 removal from chromatin.
REACT_169168. Senescence-Associated Secretory Phenotype (SASP).
REACT_169185. DNA Damage/Telomere Stress Induced Senescence.
REACT_1857. Cyclin A/B1 associated events during G2/M transition.
REACT_1915. G2 Phase.
REACT_471. E2F mediated regulation of DNA replication.
REACT_6362. Phosphorylation of proteins involved in the G2/M transition by Cyclin A:Cdc2 complexes.
REACT_683. G1/S-Specific Transcription.
REACT_6837. Regulation of APC/C activators between G1/S and early anaphase.
REACT_6850. Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
REACT_9003. SCF(Skp2)-mediated degradation of p27/p21.
REACT_9029. Cyclin A:Cdk2-associated events at S phase entry.
SignaLinkiP78396.

Names & Taxonomyi

Protein namesi
Recommended name:
Cyclin-A1
Gene namesi
Name:CCNA1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 13

Organism-specific databases

HGNCiHGNC:1577. CCNA1.

Subcellular locationi

  1. Nucleus By similarity

GO - Cellular componenti

  1. cytosol Source: ProtInc
  2. microtubule cytoskeleton Source: LIFEdb
  3. nucleoplasm Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA26147.

Polymorphism and mutation databases

BioMutaiCCNA1.
DMDMi8134359.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 465465Cyclin-A1PRO_0000080333Add
BLAST

Post-translational modificationi

Polyubiquitinated via 'Lys-11'-linked ubiquitin by the anaphase-promoting complex (APC/C), leading to its degradation by the proteasome. Deubiquitinated and stabilized by USP37 enables entry into S phase.1 Publication

Keywords - PTMi

Ubl conjugation

Proteomic databases

MaxQBiP78396.
PaxDbiP78396.
PRIDEiP78396.

Expressioni

Tissue specificityi

Very high levels in testis and very low levels in brain. Also found in myeloid leukemia cell lines.

Developmental stagei

Expression increases in early G1 phase and reaches highest levels during the S and G2/M phases.

Gene expression databases

BgeeiP78396.
CleanExiHS_CCNA1.
ExpressionAtlasiP78396. baseline and differential.
GenevestigatoriP78396.

Interactioni

Subunit structurei

Interacts with the CDK2 and the CDC2 protein kinases to form a serine/threonine kinase holoenzyme complex. The cyclin subunit imparts substrate specificity to the complex. Does not bind CDK4 and CDK5 (in vitro). The cyclin A1-CDK2 complex interacts with transcription factor E2F-1 and RB proteins. Found in a complex with CDK2, CABLES1 and CCNE1 (By similarity). Interacts with INCA1 and KLHDC9.By similarity1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
CDKN1AP389363EBI-375065,EBI-375077

Protein-protein interaction databases

BioGridi114417. 55 interactions.
IntActiP78396. 10 interactions.
MINTiMINT-104479.
STRINGi9606.ENSP00000255465.

Structurei

3D structure databases

ProteinModelPortaliP78396.
SMRiP78396. Positions 210-462.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi388 – 3914Poly-Ala

Sequence similaritiesi

Belongs to the cyclin family. Cyclin AB subfamily.Curated

Phylogenomic databases

eggNOGiCOG5024.
GeneTreeiENSGT00760000118939.
HOGENOMiHOG000167672.
HOVERGENiHBG106244.
InParanoidiP78396.
KOiK06627.
OMAiAEIRHRP.
OrthoDBiEOG7G7KQ0.
PhylomeDBiP78396.
TreeFamiTF101002.

Family and domain databases

Gene3Di1.10.472.10. 2 hits.
InterProiIPR013763. Cyclin-like.
IPR015453. Cyclin_A_chordates.
IPR004367. Cyclin_C-dom.
IPR006671. Cyclin_N.
[Graphical view]
PANTHERiPTHR10177:SF68. PTHR10177:SF68. 1 hit.
PfamiPF02984. Cyclin_C. 1 hit.
PF00134. Cyclin_N. 1 hit.
[Graphical view]
SMARTiSM00385. CYCLIN. 2 hits.
[Graphical view]
SUPFAMiSSF47954. SSF47954. 2 hits.
PROSITEiPS00292. CYCLINS. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P78396-1) [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
METGFPAIMY PGSFIGGWGE EYLSWEGPGL PDFVFQQQPV ESEAMHCSNP
60 70 80 90 100
KSGVVLATVA RGPDACQILT RAPLGQDPPQ RTVLGLLTAN GQYRRTCGQG
110 120 130 140 150
ITRIRCYSGS ENAFPPAGKK ALPDCGVQEP PKQGFDIYMD ELEQGDRDSC
160 170 180 190 200
SVREGMAFED VYEVDTGTLK SDLHFLLDFN TVSPMLVDSS LLSQSEDISS
210 220 230 240 250
LGTDVINVTE YAEEIYQYLR EAEIRHRPKA HYMKKQPDIT EGMRTILVDW
260 270 280 290 300
LVEVGEEYKL RAETLYLAVN FLDRFLSCMS VLRGKLQLVG TAAMLLASKY
310 320 330 340 350
EEIYPPEVDE FVYITDDTYT KRQLLKMEHL LLKVLAFDLT VPTTNQFLLQ
360 370 380 390 400
YLRRQGVCVR TENLAKYVAE LSLLEADPFL KYLPSLIAAA AFCLANYTVN
410 420 430 440 450
KHFWPETLAA FTGYSLSEIV PCLSELHKAY LDIPHRPQQA IREKYKASKY
460
LCVSLMEPPA VLLLQ
Length:465
Mass (Da):52,358
Last modified:May 1, 1997 - v1
Checksum:iC9C023EEA1CF036D
GO
Isoform 2 (identifier: P78396-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     38-38: Missing.

Show »
Length:464
Mass (Da):52,230
Checksum:iE67C6E6D741B7D73
GO
Isoform 3 (identifier: P78396-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-44: Missing.

Show »
Length:421
Mass (Da):47,494
Checksum:i33F2BA565699105C
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti43 – 475EAMHC → SS in AAV38384 (Ref. 2) Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 4444Missing in isoform 3. 1 PublicationVSP_044257Add
BLAST
Alternative sequencei38 – 381Missing in isoform 2. 1 PublicationVSP_034392

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U66838 mRNA. Translation: AAB49754.1.
BT019577 mRNA. Translation: AAV38384.1.
AK301897 mRNA. Translation: BAH13579.1.
AK316392 mRNA. Translation: BAH14763.1.
AL359767 Genomic DNA. Translation: CAI12728.1.
CH471075 Genomic DNA. Translation: EAX08565.1.
CH471075 Genomic DNA. Translation: EAX08566.1.
BC036346 mRNA. Translation: AAH36346.1.
U97680 mRNA. Translation: AAB60863.1.
CCDSiCCDS45031.1. [P78396-3]
CCDS9357.1. [P78396-1]
RefSeqiNP_001104515.1. NM_001111045.1. [P78396-2]
NP_001104516.1. NM_001111046.1. [P78396-3]
NP_001104517.1. NM_001111047.1. [P78396-3]
NP_003905.1. NM_003914.3. [P78396-1]
UniGeneiHs.417050.

Genome annotation databases

EnsembliENST00000255465; ENSP00000255465; ENSG00000133101. [P78396-1]
ENST00000440264; ENSP00000400666; ENSG00000133101. [P78396-3]
GeneIDi8900.
KEGGihsa:8900.
UCSCiuc001uvr.4. human. [P78396-1]
uc001uvs.4. human. [P78396-2]

Polymorphism and mutation databases

BioMutaiCCNA1.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U66838 mRNA. Translation: AAB49754.1.
BT019577 mRNA. Translation: AAV38384.1.
AK301897 mRNA. Translation: BAH13579.1.
AK316392 mRNA. Translation: BAH14763.1.
AL359767 Genomic DNA. Translation: CAI12728.1.
CH471075 Genomic DNA. Translation: EAX08565.1.
CH471075 Genomic DNA. Translation: EAX08566.1.
BC036346 mRNA. Translation: AAH36346.1.
U97680 mRNA. Translation: AAB60863.1.
CCDSiCCDS45031.1. [P78396-3]
CCDS9357.1. [P78396-1]
RefSeqiNP_001104515.1. NM_001111045.1. [P78396-2]
NP_001104516.1. NM_001111046.1. [P78396-3]
NP_001104517.1. NM_001111047.1. [P78396-3]
NP_003905.1. NM_003914.3. [P78396-1]
UniGeneiHs.417050.

3D structure databases

ProteinModelPortaliP78396.
SMRiP78396. Positions 210-462.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi114417. 55 interactions.
IntActiP78396. 10 interactions.
MINTiMINT-104479.
STRINGi9606.ENSP00000255465.

Chemistry

BindingDBiP78396.
ChEMBLiCHEMBL2094128.

Polymorphism and mutation databases

BioMutaiCCNA1.
DMDMi8134359.

Proteomic databases

MaxQBiP78396.
PaxDbiP78396.
PRIDEiP78396.

Protocols and materials databases

DNASUi8900.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000255465; ENSP00000255465; ENSG00000133101. [P78396-1]
ENST00000440264; ENSP00000400666; ENSG00000133101. [P78396-3]
GeneIDi8900.
KEGGihsa:8900.
UCSCiuc001uvr.4. human. [P78396-1]
uc001uvs.4. human. [P78396-2]

Organism-specific databases

CTDi8900.
GeneCardsiGC13P037005.
HGNCiHGNC:1577. CCNA1.
MIMi604036. gene.
neXtProtiNX_P78396.
PharmGKBiPA26147.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG5024.
GeneTreeiENSGT00760000118939.
HOGENOMiHOG000167672.
HOVERGENiHBG106244.
InParanoidiP78396.
KOiK06627.
OMAiAEIRHRP.
OrthoDBiEOG7G7KQ0.
PhylomeDBiP78396.
TreeFamiTF101002.

Enzyme and pathway databases

ReactomeiREACT_111214. G0 and Early G1.
REACT_1156. Orc1 removal from chromatin.
REACT_169168. Senescence-Associated Secretory Phenotype (SASP).
REACT_169185. DNA Damage/Telomere Stress Induced Senescence.
REACT_1857. Cyclin A/B1 associated events during G2/M transition.
REACT_1915. G2 Phase.
REACT_471. E2F mediated regulation of DNA replication.
REACT_6362. Phosphorylation of proteins involved in the G2/M transition by Cyclin A:Cdc2 complexes.
REACT_683. G1/S-Specific Transcription.
REACT_6837. Regulation of APC/C activators between G1/S and early anaphase.
REACT_6850. Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
REACT_9003. SCF(Skp2)-mediated degradation of p27/p21.
REACT_9029. Cyclin A:Cdk2-associated events at S phase entry.
SignaLinkiP78396.

Miscellaneous databases

GeneWikiiCyclin_A1.
GenomeRNAii8900.
NextBioi33435.
PROiP78396.
SOURCEiSearch...

Gene expression databases

BgeeiP78396.
CleanExiHS_CCNA1.
ExpressionAtlasiP78396. baseline and differential.
GenevestigatoriP78396.

Family and domain databases

Gene3Di1.10.472.10. 2 hits.
InterProiIPR013763. Cyclin-like.
IPR015453. Cyclin_A_chordates.
IPR004367. Cyclin_C-dom.
IPR006671. Cyclin_N.
[Graphical view]
PANTHERiPTHR10177:SF68. PTHR10177:SF68. 1 hit.
PfamiPF02984. Cyclin_C. 1 hit.
PF00134. Cyclin_N. 1 hit.
[Graphical view]
SMARTiSM00385. CYCLIN. 2 hits.
[Graphical view]
SUPFAMiSSF47954. SSF47954. 2 hits.
PROSITEiPS00292. CYCLINS. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Characterization of a second human cyclin A that is highly expressed in testis and in several leukemic cell lines."
    Yang R., Morosetti R., Koeffler H.P.
    Cancer Res. 57:913-920(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Myeloid.
  2. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  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] (ISOFORM 3).
    Tissue: Testis.
  4. "The DNA sequence and analysis of human chromosome 13."
    Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L., Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T.
    , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P., Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L., Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S., Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R., Rogers J., Ross M.T.
    Nature 428:522-528(2004) [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] (ISOFORM 2).
    Tissue: Brain.
  7. "The human testes cyclin A1 disrupts growth and DNA damage response of a yeast replication mutant."
    Perkins E.L., Wood V.J., Sterling J.F., Hashem V.I., Resnick M.A.
    Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 55-465.
    Tissue: Testis.
  8. "Functions of cyclin A1 in the cell cycle and its interactions with transcription factor E2F-1 and the Rb family of proteins."
    Yang R., Mueller C., Huynh V., Fung Y.K., Yee A.S., Koeffler H.P.
    Mol. Cell. Biol. 19:2400-2407(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  9. Cited for: INTERACTION WITH INCA1 AND KLHDC9.
  10. "Deubiquitinase USP37 is activated by CDK2 to antagonize APC(CDH1) and promote S phase entry."
    Huang X., Summers M.K., Pham V., Lill J.R., Liu J., Lee G., Kirkpatrick D.S., Jackson P.K., Fang G., Dixit V.M.
    Mol. Cell 42:511-523(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: UBIQUITINATION, DEUBIQUITINATION BY USP37.

Entry informationi

Entry nameiCCNA1_HUMAN
AccessioniPrimary (citable) accession number: P78396
Secondary accession number(s): B7Z7E3
, Q5T3V0, Q5U0G2, Q8IY91
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: May 1, 1997
Last modified: April 29, 2015
This is version 138 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 13
    Human chromosome 13: 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.