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Protein

G2/mitotic-specific cyclin-B3

Gene

CCNB3

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

Functioni

Cyclins are positive regulatory subunits of the cyclin-dependent kinases (CDKs), and thereby play an essential role in the control of the cell cycle, notably via their destruction during cell division. Its tissue specificity suggest that it may be required during early meiotic prophase I.1 Publication

GO - Biological processi

  1. cell division Source: UniProtKB-KW
  2. meiotic cell cycle Source: UniProtKB-KW
  3. regulation of cyclin-dependent protein serine/threonine kinase activity Source: InterPro
  4. regulation of G2/M transition of mitotic cell cycle Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Cyclin

Keywords - Biological processi

Cell cycle, Cell division, Meiosis

Enzyme and pathway databases

SignaLinkiQ8WWL7.

Names & Taxonomyi

Protein namesi
Recommended name:
G2/mitotic-specific cyclin-B3
Gene namesi
Name:CCNB3
Synonyms:CYCB3
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome X

Organism-specific databases

HGNCiHGNC:18709. CCNB3.

Subcellular locationi

Nucleus 1 Publication

GO - Cellular componenti

  1. nucleoplasm Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi60 – 601R → A in cycB3XA; prevents its destruction after completion of anaphase; when associated with A-63 and A-68.
Mutagenesisi63 – 631F → A in cycB3XA; prevents its destruction after completion of anaphase; when associated with A-60 and A-68.
Mutagenesisi68 – 681N → A in cycB3XA; prevents its destruction after completion of anaphase; when associated with A-60 and A-63.

Organism-specific databases

PharmGKBiPA38653.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 13951395G2/mitotic-specific cyclin-B3PRO_0000080373Add
BLAST

Post-translational modificationi

Ubiquitinated (Probable). Ubiquitination leads to its degradation during anaphase entry, after degradation of CCNB1.Curated

Keywords - PTMi

Ubl conjugation

Proteomic databases

PaxDbiQ8WWL7.
PRIDEiQ8WWL7.

PTM databases

PhosphoSiteiQ8WWL7.

Expressioni

Tissue specificityi

Testis specific. In testis, it is expressed in developing germ cells, but not in Leydig cells. Weakly or not expressed in other tissues.2 Publications

Gene expression databases

BgeeiQ8WWL7.
CleanExiHS_CCNB3.
ExpressionAtlasiQ8WWL7. baseline and differential.
GenevestigatoriQ8WWL7.

Organism-specific databases

HPAiHPA000496.

Interactioni

Subunit structurei

Interacts with CDK2 kinase.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
CDK2A8UKE62EBI-767764,EBI-767796From a different organism.
Plk4Q647024EBI-767764,EBI-2552433From a different organism.

Protein-protein interaction databases

BioGridi124523. 2 interactions.
IntActiQ8WWL7. 3 interactions.
MINTiMINT-4054013.
STRINGi9606.ENSP00000276014.

Structurei

3D structure databases

ProteinModelPortaliQ8WWL7.
SMRiQ8WWL7. Positions 1127-1370.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi60 – 689D-box

Domaini

The N-terminal destruction box (D-box) probably acts as a recognition signal for degradation via the ubiquitin-proteasome pathway.By similarity

Sequence similaritiesi

Belongs to the cyclin family. Cyclin AB subfamily.Curated

Phylogenomic databases

eggNOGiCOG5024.
GeneTreeiENSGT00760000118939.
HOGENOMiHOG000231355.
HOVERGENiHBG050835.
InParanoidiQ8WWL7.
KOiK05868.
OMAiCKSIMEL.
OrthoDBiEOG7P2XST.
PhylomeDBiQ8WWL7.
TreeFamiTF101001.

Family and domain databases

Gene3Di1.10.472.10. 2 hits.
InterProiIPR013763. Cyclin-like.
IPR015452. Cyclin_B3.
IPR004367. Cyclin_C-dom.
IPR006671. Cyclin_N.
[Graphical view]
PANTHERiPTHR10177:SF22. PTHR10177:SF22. 1 hit.
PfamiPF02984. Cyclin_C. 1 hit.
PF00134. Cyclin_N. 1 hit.
[Graphical view]
SMARTiSM00385. CYCLIN. 2 hits.
[Graphical view]
SUPFAMiSSF47954. SSF47954. 2 hits.

Sequences (3)i

Sequence statusi: Complete.

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

Isoform 1 (identifier: Q8WWL7-1) [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
MLLPLPPQSS KPVPKKSQSS KIVPSHHDPS EKTGENCQTK ISPSSLQESP
60 70 80 90 100
SSLQGALKKR SAFEDLTNAS QCQPVQPKKE ANKEFVKVVS KKINRNTHAL
110 120 130 140 150
GLAKKNKRNL KWHKLEVTPV VASTTVVPNI MEKPLILDIS TTSKTPNTEE
160 170 180 190 200
ASLFRKPLVL KEEPTIEDET LINKSLSLKK CSNHEEVSLL EKLQPLQEES
210 220 230 240 250
DSDDAFVIEP MTFKKTHKTE EAAITKKTLS LKKKMCASQR KQSCQEESLA
260 270 280 290 300
VQDVNMEEDS FFMESMSFKK KPKTEESIPT HKLSSLKKKC TIYGKICHFR
310 320 330 340 350
KPPVLQTTIC GAMSSIKKPT TEKETLFQEL SVLQEKHTTE HEMSILKKSL
360 370 380 390 400
ALQKTNFKED SLVKESLAFK KKPSTEEAIM MPVILKEQCM TEGKRSRLKP
410 420 430 440 450
LVLQEITSGE KSLIMKPLSI KEKPSTEKES FSQEPSALQK KHTTQEEVSI
460 470 480 490 500
LKEPSSLLKS PTEESPFDEA LAFTKKCTIE EAPPTKKPLI LKRKHATQGT
510 520 530 540 550
MSHLKKPLIL QTTSGEKSLI KEPLPFKEEK VSLKKKCTTQ EMMSICPELL
560 570 580 590 600
DFQDMIGEDK NSFFMEPMSF RKNPTTEETV LTKTSLSLQE KKITQGKMSH
610 620 630 640 650
LKKPLVLQKI TSEEESFYKK LLPFKMKSTT EEKFLSQEPS ALKEKHTTLQ
660 670 680 690 700
EVSLSKESLA IQEKATTEEE FSQELFSLHV KHTNKSGSLF QEALVLQEKT
710 720 730 740 750
DAEEDSLKNL LALQEKSTME EESLINKLLA LKEELSAEAA TNIQTQLSLK
760 770 780 790 800
KKSTSHGKVF FLKKQLALNE TINEEEFLNK QPLALEGYPS IAEGETLFKK
810 820 830 840 850
LLAMQEEPSI EKEAVLKEPT IDTEAHFKEP LALQEEPSTE KEAVLKEPSV
860 870 880 890 900
DTEAHFKETL ALQEKPSIEQ EALFKRHSAL WEKPSTEKET IFKESLDLQE
910 920 930 940 950
KPSIKKETLL KKPLALKMST INEAVLFEDM IALNEKPTTG KELSFKEPLA
960 970 980 990 1000
LQESPTYKED TFLKTLLVPQ VGTSPNVSST APESITSKSS IATMTSVGKS
1010 1020 1030 1040 1050
GTINEAFLFE DMITLNEKPT TGKELSFKEP LALQESPTCK EDTFLETFLI
1060 1070 1080 1090 1100
PQIGTSPYVF STTPESITEK SSIATMTSVG KSRTTTESSA CESASDKPVS
1110 1120 1130 1140 1150
PQAKGTPKEI TPREDIDEDS SDPSFNPMYA KEIFSYMKER EEQFILTDYM
1160 1170 1180 1190 1200
NRQIEITSDM RAILVDWLVE VQVSFEMTHE TLYLAVKLVD LYLMKAVCKK
1210 1220 1230 1240 1250
DKLQLLGATA FMIAAKFEEH NSPRVDDFVY ICDDNYQRSE VLSMEINILN
1260 1270 1280 1290 1300
VLKCDINIPI AYHFLRRYAR CIHTNMKTLT LSRYICEMTL QEYHYVQEKA
1310 1320 1330 1340 1350
SKLAAASLLL ALYMKKLGYW VPFLEHYSGY SISELHPLVR QLNKLLTFSS
1360 1370 1380 1390
YDSLKAVYYK YSHPVFFEVA KIPALDMLKL EEILNCDCEA QGLVL
Length:1,395
Mass (Da):157,916
Last modified:October 14, 2008 - v2
Checksum:i454552BC5A67E34E
GO
Isoform 2 (identifier: Q8WWL7-2) [UniParc]FASTAAdd to basket

Also known as: Variant 1

The sequence of this isoform differs from the canonical sequence as follows:
     69-1172: Missing.

Show »
Length:291
Mass (Da):33,275
Checksum:iCC00FC3079181B7E
GO
Isoform 3 (identifier: Q8WWL7-3) [UniParc]FASTAAdd to basket

Also known as: Variant 2

The sequence of this isoform differs from the canonical sequence as follows:
     112-1395: Missing.

Show »
Length:111
Mass (Da):12,195
Checksum:i0D8F2ACB1016D226
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti295 – 2951K → R in CAC40024 (PubMed:11846420).Curated
Sequence conflicti331 – 3311S → F in CAC94915 (PubMed:12185076).Curated
Sequence conflicti396 – 3961S → P in CAC40024 (PubMed:11846420).Curated
Sequence conflicti493 – 4931R → K in CAC40024 (PubMed:11846420).Curated
Sequence conflicti573 – 5731N → S in CAC40024 (PubMed:11846420).Curated
Sequence conflicti597 – 5971K → E in CAC40024 (PubMed:11846420).Curated
Sequence conflicti774 – 7741E → K in CAC94915 (PubMed:12185076).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti597 – 5971K → T in a colorectal cancer sample; somatic mutation. 1 Publication
VAR_036580
Natural varianti1001 – 10011G → R.
Corresponds to variant rs6614336 [ dbSNP | Ensembl ].
VAR_047027

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei69 – 11721104Missing in isoform 2. 1 PublicationVSP_010514Add
BLAST
Alternative sequencei112 – 13951284Missing in isoform 3. 1 PublicationVSP_010515Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ416458 mRNA. Translation: CAC94915.1.
AJ314764 mRNA. Translation: CAC40024.1.
AJ314765 mRNA. Translation: CAC40025.1.
AJ314766 mRNA. Translation: CAC40026.1.
AL591367, BX323840 Genomic DNA. Translation: CAI41320.1.
AL591367, BX323840 Genomic DNA. Translation: CAI41321.1.
BX323840, AL591367 Genomic DNA. Translation: CAI43220.1.
BX323840, AL591367 Genomic DNA. Translation: CAI43221.1.
CH471180 Genomic DNA. Translation: EAW89922.1.
CH471180 Genomic DNA. Translation: EAW89923.1.
AL137550 mRNA. Translation: CAB70806.1.
CCDSiCCDS14331.1. [Q8WWL7-1]
CCDS14332.1. [Q8WWL7-2]
PIRiT46391.
RefSeqiNP_149020.2. NM_033031.2. [Q8WWL7-1]
NP_391990.1. NM_033670.2. [Q8WWL7-2]
UniGeneiHs.130310.
Hs.722420.
Hs.722421.
Hs.740165.

Genome annotation databases

EnsembliENST00000276014; ENSP00000276014; ENSG00000147082. [Q8WWL7-1]
ENST00000348603; ENSP00000338682; ENSG00000147082. [Q8WWL7-2]
ENST00000376038; ENSP00000365206; ENSG00000147082. [Q8WWL7-2]
ENST00000376042; ENSP00000365210; ENSG00000147082. [Q8WWL7-1]
ENST00000476167; ENSP00000431645; ENSG00000147082. [Q8WWL7-3]
GeneIDi85417.
KEGGihsa:85417.
UCSCiuc004dox.4. human. [Q8WWL7-1]
uc004doz.3. human. [Q8WWL7-2]

Polymorphism databases

DMDMi209572596.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ416458 mRNA. Translation: CAC94915.1.
AJ314764 mRNA. Translation: CAC40024.1.
AJ314765 mRNA. Translation: CAC40025.1.
AJ314766 mRNA. Translation: CAC40026.1.
AL591367, BX323840 Genomic DNA. Translation: CAI41320.1.
AL591367, BX323840 Genomic DNA. Translation: CAI41321.1.
BX323840, AL591367 Genomic DNA. Translation: CAI43220.1.
BX323840, AL591367 Genomic DNA. Translation: CAI43221.1.
CH471180 Genomic DNA. Translation: EAW89922.1.
CH471180 Genomic DNA. Translation: EAW89923.1.
AL137550 mRNA. Translation: CAB70806.1.
CCDSiCCDS14331.1. [Q8WWL7-1]
CCDS14332.1. [Q8WWL7-2]
PIRiT46391.
RefSeqiNP_149020.2. NM_033031.2. [Q8WWL7-1]
NP_391990.1. NM_033670.2. [Q8WWL7-2]
UniGeneiHs.130310.
Hs.722420.
Hs.722421.
Hs.740165.

3D structure databases

ProteinModelPortaliQ8WWL7.
SMRiQ8WWL7. Positions 1127-1370.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi124523. 2 interactions.
IntActiQ8WWL7. 3 interactions.
MINTiMINT-4054013.
STRINGi9606.ENSP00000276014.

Chemistry

BindingDBiQ8WWL7.
ChEMBLiCHEMBL2094127.

PTM databases

PhosphoSiteiQ8WWL7.

Polymorphism databases

DMDMi209572596.

Proteomic databases

PaxDbiQ8WWL7.
PRIDEiQ8WWL7.

Protocols and materials databases

DNASUi85417.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000276014; ENSP00000276014; ENSG00000147082. [Q8WWL7-1]
ENST00000348603; ENSP00000338682; ENSG00000147082. [Q8WWL7-2]
ENST00000376038; ENSP00000365206; ENSG00000147082. [Q8WWL7-2]
ENST00000376042; ENSP00000365210; ENSG00000147082. [Q8WWL7-1]
ENST00000476167; ENSP00000431645; ENSG00000147082. [Q8WWL7-3]
GeneIDi85417.
KEGGihsa:85417.
UCSCiuc004dox.4. human. [Q8WWL7-1]
uc004doz.3. human. [Q8WWL7-2]

Organism-specific databases

CTDi85417.
GeneCardsiGC0XP049967.
HGNCiHGNC:18709. CCNB3.
HPAiHPA000496.
MIMi300456. gene.
neXtProtiNX_Q8WWL7.
PharmGKBiPA38653.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG5024.
GeneTreeiENSGT00760000118939.
HOGENOMiHOG000231355.
HOVERGENiHBG050835.
InParanoidiQ8WWL7.
KOiK05868.
OMAiCKSIMEL.
OrthoDBiEOG7P2XST.
PhylomeDBiQ8WWL7.
TreeFamiTF101001.

Enzyme and pathway databases

SignaLinkiQ8WWL7.

Miscellaneous databases

ChiTaRSiCCNB3. human.
GenomeRNAii85417.
NextBioi75998.
PROiQ8WWL7.
SOURCEiSearch...

Gene expression databases

BgeeiQ8WWL7.
CleanExiHS_CCNB3.
ExpressionAtlasiQ8WWL7. baseline and differential.
GenevestigatoriQ8WWL7.

Family and domain databases

Gene3Di1.10.472.10. 2 hits.
InterProiIPR013763. Cyclin-like.
IPR015452. Cyclin_B3.
IPR004367. Cyclin_C-dom.
IPR006671. Cyclin_N.
[Graphical view]
PANTHERiPTHR10177:SF22. PTHR10177:SF22. 1 hit.
PfamiPF02984. Cyclin_C. 1 hit.
PF00134. Cyclin_N. 1 hit.
[Graphical view]
SMARTiSM00385. CYCLIN. 2 hits.
[Graphical view]
SUPFAMiSSF47954. SSF47954. 2 hits.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Characterization and expression of mammalian cyclin b3, a prepachytene meiotic cyclin."
    Nguyen T.B., Manova K., Capodieci P., Lindon C., Bottega S., Wang X.-Y., Refik-Rogers J., Pines J., Wolgemuth D.J., Koff A.
    J. Biol. Chem. 277:41960-41969(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, DOMAIN, TISSUE SPECIFICITY, MUTANT CYCB3XA, INTERACTION WITH CDK2.
    Tissue: Testis.
  2. "Molecular cloning, gene localization, and structure of human cyclin B3."
    Lozano J.-C., Perret E., Schatt P., Arnould C., Peaucellier G., Picard A.
    Biochem. Biophys. Res. Commun. 291:406-413(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3), ALTERNATIVE SPLICING, TISSUE SPECIFICITY.
    Tissue: Placenta.
  3. "The DNA sequence of the human X chromosome."
    Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.
    , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
    Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1249-1395 (ISOFORM 1).
    Tissue: Testis.
  6. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  7. Cited for: VARIANT [LARGE SCALE ANALYSIS] THR-597.

Entry informationi

Entry nameiCCNB3_HUMAN
AccessioniPrimary (citable) accession number: Q8WWL7
Secondary accession number(s): B1AQI5
, B1AQI6, Q96SB5, Q96SB6, Q96SB7, Q9NT38
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 7, 2004
Last sequence update: October 14, 2008
Last modified: February 4, 2015
This is version 116 of the entry and version 2 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 X
    Human chromosome X: 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. 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.