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O43303

- CP110_HUMAN

UniProt

O43303 - CP110_HUMAN

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Protein

Centriolar coiled-coil protein of 110 kDa

Gene

CCP110

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

Functioni

Necessary for centrosome duplication at different stages of procentriole formation. Acts as a key negative regulator of ciliogenesis in collaboration with CEP97 by capping the mother centriole thereby preventing cilia formation. Required for correct spindle formation and has a role in regulating cytokinesis and genome stability via cooperation with CALM1 and CETN2.5 Publications

GO - Biological processi

  1. cell projection organization Source: UniProtKB-KW
  2. centriole replication Source: UniProtKB
  3. centrosome duplication Source: UniProtKB
  4. G2/M transition of mitotic cell cycle Source: Reactome
  5. mitotic cell cycle Source: Reactome
  6. regulation of cytokinesis Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Cilium biogenesis/degradation

Enzyme and pathway databases

ReactomeiREACT_15296. Recruitment of mitotic centrosome proteins and complexes.
REACT_15364. Loss of Nlp from mitotic centrosomes.
REACT_15451. Loss of proteins required for interphase microtubule organization from the centrosome.
REACT_160315. Regulation of PLK1 Activity at G2/M Transition.

Names & Taxonomyi

Protein namesi
Recommended name:
Centriolar coiled-coil protein of 110 kDa
Alternative name(s):
Centrosomal protein of 110 kDa
Short name:
CP110
Short name:
Cep110
Gene namesi
Name:CCP110
Synonyms:CEP110, CP110, KIAA0419
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 16

Organism-specific databases

HGNCiHGNC:24342. CCP110.

Subcellular locationi

Cytoplasmcytoskeletonmicrotubule organizing centercentrosomecentriole 7 Publications
Note: Recruited early and then associates with the growing distal tips. Recruited to the mother centriole by KIF24. Removed from centrioles by TTBK2, leading to initiation of ciliogenesis.

GO - Cellular componenti

  1. centriole Source: UniProtKB
  2. centrosome Source: UniProtKB
  3. cytosol Source: Reactome
  4. protein complex Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi586 – 5883RRL → ARA: Abolishes interaction with CCNF. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 10121012Centriolar coiled-coil protein of 110 kDaPRO_0000089460Add
BLAST

Post-translational modificationi

Phosphorylated by CDKs.1 Publication
Ubiquitinated by the SCF(CCNF) during G2 phase, leading to its degradation by the proteasome and preventing centrosome reduplication. Deubiquitinated by USP33 in S and G2/M phase, leading to stabilize CCP110 during the period which centrioles duplicate and elongate.2 Publications

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiO43303.
PaxDbiO43303.
PRIDEiO43303.

PTM databases

PhosphoSiteiO43303.

Expressioni

Tissue specificityi

Highly expressed in testis. Detected at intermediate levels in spleen, thymus, prostate, small intestine, colon and peripheral blood leukocytes.1 Publication

Inductioni

Up-regulated during the transition from G1 to S phase of the cell cycle. The highest levels are observed in S phase, after which the levels decrease markedly.1 Publication

Gene expression databases

BgeeiO43303.
CleanExiHS_CEP110.
ExpressionAtlasiO43303. baseline and differential.
GenevestigatoriO43303.

Organism-specific databases

HPAiHPA039402.

Interactioni

Subunit structurei

Interacts with CALM1, CETN2, CEP76 and CEP97. Interacts with NEURL4 and CCNF; these interactions are not mutually exclusive and both lead to CCP110 ubiquitination and proteasome-dependent degradation. Via its interaction with NEURL4, may indirectly interact with HERC2. Interacts with KIF24, leading to its recruitment to centrioles. Interacts with USP20 and USP33.8 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CALM3P621589EBI-1566217,EBI-397435
CCNFP410023EBI-1566217,EBI-1207574
CEP97Q8IW3518EBI-1566217,EBI-1566210
CETN2P412083EBI-1566217,EBI-1789926
KIF24Q5T7B89EBI-1566217,EBI-2556811
NEURL4Q96JN89EBI-1566217,EBI-1053406

Protein-protein interaction databases

BioGridi115087. 30 interactions.
DIPiDIP-39892N.
IntActiO43303. 19 interactions.
MINTiMINT-7994609.

Structurei

3D structure databases

ProteinModelPortaliO43303.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 223223CEP97 bindingAdd
BLAST
Regioni64 – 8219Calmodulin-bindingAdd
BLAST
Regioni350 – 565216Interaction with CEP76Add
BLAST
Regioni781 – 82141Calmodulin-bindingAdd
BLAST
Regioni909 – 92416Calmodulin-bindingAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili49 – 9042Sequence AnalysisAdd
BLAST
Coiled coili640 – 70970Sequence AnalysisAdd
BLAST

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiNOG82086.
GeneTreeiENSGT00390000004090.
HOVERGENiHBG050873.
InParanoidiO43303.
KOiK16453.
OMAiFYLWGSS.
OrthoDBiEOG7SV0XP.
PhylomeDBiO43303.
TreeFamiTF332788.

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: O43303-1) [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
MEEYEKFCEK SLARIQEASL STESFLPAQS ESISLIRFHG VAILSPLLNI
60 70 80 90 100
EKRKEMQQEK QKALDVEARK QVNRKKALLT RVQEILDNVQ VRKAPNASDF
110 120 130 140 150
DQWEMETVYS NSEVRNLNVP ATFPNSFPSH TEHSTAAKLD KIAGILPLDN
160 170 180 190 200
EDQCKTDGID LARDSEGFNS PKQCDSSNIS HVENEAFPKT SSATPQETLI
210 220 230 240 250
SDGPFSVNEQ QDLPLLAEVI PDPYVMSLQN LMKKSKEYIE REQSRRSLRG
260 270 280 290 300
SINRIVNESH LDKEHDAVEV ADCVKEKGQL TGKHCVSVIP DKPSLNKSNV
310 320 330 340 350
LLQGASTQAS SMSMPVLASF SKVDIPIRTG HPTVLESNSD FKVIPTFVTE
360 370 380 390 400
NNVIKSLTGS YAKLPSPEPS MSPKMHRRRS RTSSACHILI NNPINACELS
410 420 430 440 450
PKGKEQAMDL IIQDTDENTN VPEIMPKLPT DLAGVCSSKV YVGKNTSEVK
460 470 480 490 500
EDVVLGKSNQ VCQSSGNHLE NKVTHGLVTV EGQLTSDERG AHIMNSTCAA
510 520 530 540 550
MPKLHEPYAS SQCIASPNFG TVSGLKPASM LEKNCSLQTE LNKSYDVKNP
560 570 580 590 600
SPLLMQNQNT RQQMDTPMVS CGNEQFLDNS FEKVKRRLDL DIDGLQKENC
610 620 630 640 650
PYVITSGITE QERQHLPEKR YPKGSGFVNK NKMLGTSSKE SEELLKSKML
660 670 680 690 700
AFEEMRKRLE EQHAQQLSLL IAEQEREQER LQKEIEEQEK MLKEKKAMTA
710 720 730 740 750
EASELDINNA VELEWRKISD SSLLETMLSQ ADSLHTSNSN SSGFTNSAMQ
760 770 780 790 800
YSFVSANEAP FYLWGSSTSG LTKLSVTRPF GRAKTRWSQV FSLEIQAKFN
810 820 830 840 850
KITAVAKGFL TRRLMQTDKL KQLRQTVKDT MEFIRSFQSE APLKRGIVSA
860 870 880 890 900
QDASLQERVL AQLRAALYGI HDIFFVMDAA ERMSILHHDR EVRKEKMLRQ
910 920 930 940 950
MDKMKSPRVA LSAATQKSLD RKKYMKAAEM GMPNKKFLVK QNPSETRVLQ
960 970 980 990 1000
PNQGQNAPVH RLLSRQGTPK TSVKGVVQNR QKPSQSRVPN RVPVSGVYAG
1010
KIQRKRPNVA TI
Length:1,012
Mass (Da):113,424
Last modified:October 23, 2007 - v3
Checksum:i5459F655CFB9DFD0
GO
Isoform 2 (identifier: O43303-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     968-1012: TPKTSVKGVVQNRQKPSQSRVPNRVPVSGVYAGKIQRKRPNVATI → SICRKNPKKAAKCCDNLRRQHSLG

Show »
Length:991
Mass (Da):111,224
Checksum:iCDEA157BFDBC92EA
GO

Sequence cautioni

The sequence BAA24849.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti628 – 6281V → F in AAH36654. (PubMed:15489334)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti69 – 691R → S.
Corresponds to variant rs16972129 [ dbSNP | Ensembl ].
VAR_056788
Natural varianti171 – 1711P → L.
Corresponds to variant rs3751821 [ dbSNP | Ensembl ].
VAR_056789
Natural varianti252 – 2521I → M.4 Publications
Corresponds to variant rs226891 [ dbSNP | Ensembl ].
VAR_019823
Natural varianti347 – 3471F → I.1 Publication
Corresponds to variant rs11645625 [ dbSNP | Ensembl ].
VAR_056790
Natural varianti375 – 3751M → I.
Corresponds to variant rs7190666 [ dbSNP | Ensembl ].
VAR_019824

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei968 – 101245TPKTS…NVATI → SICRKNPKKAAKCCDNLRRQ HSLG in isoform 2. 2 PublicationsVSP_011897Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB007879 mRNA. Translation: BAA24849.2. Different initiation.
CR749255 mRNA. Translation: CAH18111.1.
AC003108 Genomic DNA. Translation: AAC05804.1.
AC012621 Genomic DNA. No translation available.
BC036654 mRNA. Translation: AAH36654.1.
CCDSiCCDS10579.1. [O43303-2]
CCDS55992.1. [O43303-1]
PIRiT01372.
RefSeqiNP_001185951.1. NM_001199022.1.
NP_055526.3. NM_014711.4.
XP_005255776.1. XM_005255719.1. [O43303-1]
XP_005255778.1. XM_005255721.1. [O43303-2]
UniGeneiHs.279912.

Genome annotation databases

EnsembliENST00000381396; ENSP00000370803; ENSG00000103540. [O43303-1]
ENST00000396208; ENSP00000379511; ENSG00000103540. [O43303-2]
ENST00000396212; ENSP00000379515; ENSG00000103540. [O43303-2]
GeneIDi9738.
KEGGihsa:9738.
UCSCiuc002dgk.4. human. [O43303-2]
uc002dgl.4. human. [O43303-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB007879 mRNA. Translation: BAA24849.2 . Different initiation.
CR749255 mRNA. Translation: CAH18111.1 .
AC003108 Genomic DNA. Translation: AAC05804.1 .
AC012621 Genomic DNA. No translation available.
BC036654 mRNA. Translation: AAH36654.1 .
CCDSi CCDS10579.1. [O43303-2 ]
CCDS55992.1. [O43303-1 ]
PIRi T01372.
RefSeqi NP_001185951.1. NM_001199022.1.
NP_055526.3. NM_014711.4.
XP_005255776.1. XM_005255719.1. [O43303-1 ]
XP_005255778.1. XM_005255721.1. [O43303-2 ]
UniGenei Hs.279912.

3D structure databases

ProteinModelPortali O43303.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 115087. 30 interactions.
DIPi DIP-39892N.
IntActi O43303. 19 interactions.
MINTi MINT-7994609.

PTM databases

PhosphoSitei O43303.

Proteomic databases

MaxQBi O43303.
PaxDbi O43303.
PRIDEi O43303.

Protocols and materials databases

DNASUi 9738.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000381396 ; ENSP00000370803 ; ENSG00000103540 . [O43303-1 ]
ENST00000396208 ; ENSP00000379511 ; ENSG00000103540 . [O43303-2 ]
ENST00000396212 ; ENSP00000379515 ; ENSG00000103540 . [O43303-2 ]
GeneIDi 9738.
KEGGi hsa:9738.
UCSCi uc002dgk.4. human. [O43303-2 ]
uc002dgl.4. human. [O43303-1 ]

Organism-specific databases

CTDi 9738.
GeneCardsi GC16P019536.
HGNCi HGNC:24342. CCP110.
HPAi HPA039402.
MIMi 609544. gene.
neXtProti NX_O43303.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG82086.
GeneTreei ENSGT00390000004090.
HOVERGENi HBG050873.
InParanoidi O43303.
KOi K16453.
OMAi FYLWGSS.
OrthoDBi EOG7SV0XP.
PhylomeDBi O43303.
TreeFami TF332788.

Enzyme and pathway databases

Reactomei REACT_15296. Recruitment of mitotic centrosome proteins and complexes.
REACT_15364. Loss of Nlp from mitotic centrosomes.
REACT_15451. Loss of proteins required for interphase microtubule organization from the centrosome.
REACT_160315. Regulation of PLK1 Activity at G2/M Transition.

Miscellaneous databases

GeneWikii CCP110.
GenomeRNAii 9738.
NextBioi 36648.
PROi O43303.
SOURCEi Search...

Gene expression databases

Bgeei O43303.
CleanExi HS_CEP110.
ExpressionAtlasi O43303. baseline and differential.
Genevestigatori O43303.

Family and domain databases

ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Prediction of the coding sequences of unidentified human genes. VIII. 78 new cDNA clones from brain which code for large proteins in vitro."
    Ishikawa K., Nagase T., Nakajima D., Seki N., Ohira M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
    DNA Res. 4:307-313(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), VARIANTS MET-252 AND ILE-347.
    Tissue: Brain.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT MET-252.
    Tissue: Fetal kidney.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT MET-252.
  4. "The sequence and analysis of duplication-rich human chromosome 16."
    Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.
    , Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A.
    Nature 432:988-994(2004) [PubMed] [Europe PMC] [Abstract]
    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] (ISOFORM 2), VARIANT MET-252.
    Tissue: Testis.
  6. "CP110, a cell cycle-dependent CDK substrate, regulates centrosome duplication in human cells."
    Chen Z., Indjeian V.B., McManus M., Wang L., Dynlacht B.D.
    Dev. Cell 3:339-350(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INDUCTION, PHOSPHORYLATION.
  7. "Proteomic characterization of the human centrosome by protein correlation profiling."
    Andersen J.S., Wilkinson C.J., Mayor T., Mortensen P., Nigg E.A., Mann M.
    Nature 426:570-574(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    Tissue: Lymphoblast.
  8. "CP110 cooperates with two calcium-binding proteins to regulate cytokinesis and genome stability."
    Tsang W.Y., Spektor A., Luciano D.J., Indjeian V.B., Chen Z., Salisbury J.L., Sanchez I., Dynlacht B.D.
    Mol. Biol. Cell 17:3423-3434(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH CALM1 AND CETN2, SUBCELLULAR LOCATION.
  9. "Cep97 and CP110 suppress a cilia assembly program."
    Spektor A., Tsang W.Y., Khoo D., Dynlacht B.D.
    Cell 130:678-690(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH CALM1 AND CEP97, SUBCELLULAR LOCATION.
  10. Cited for: FUNCTION, SUBCELLULAR LOCATION.
  11. "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].
  12. "Cep76, a centrosomal protein that specifically restrains centriole reduplication."
    Tsang W.Y., Spektor A., Vijayakumar S., Bista B.R., Li J., Sanchez I., Duensing S., Dynlacht B.D.
    Dev. Cell 16:649-660(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CEP76.
  13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "SCF(Cyclin F) controls centrosome homeostasis and mitotic fidelity through CP110 degradation."
    D'Angiolella V., Donato V., Vijayakumar S., Saraf A., Florens L., Washburn M.P., Dynlacht B., Pagano M.
    Nature 466:138-142(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: UBIQUITINATION, SUBCELLULAR LOCATION, MUTAGENESIS OF 586-ARG--LEU-588, INTERACTION WITH CCNF.
  15. "Centriolar kinesin Kif24 interacts with CP110 to remodel microtubules and regulate ciliogenesis."
    Kobayashi T., Tsang W.Y., Li J., Lane W., Dynlacht B.D.
    Cell 145:914-925(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, INTERACTION WITH KIF24.
  16. "Neurl4, a novel daughter centriole protein, prevents formation of ectopic microtubule organizing centres."
    Li J., Kim S., Kobayashi T., Liang F.X., Korzeniewski N., Duensing S., Dynlacht B.D.
    EMBO Rep. 13:547-553(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NEURL4 AND CCNF.
  17. "Interaction proteomics identify NEURL4 and the HECT E3 ligase HERC2 as novel modulators of centrosome architecture."
    Al-Hakim A.K., Bashkurov M., Gingras A.C., Durocher D., Pelletier L.
    Mol. Cell. Proteomics 11:M111.014233.01-M111.014233.14(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CEP97; HERC2 AND NEURL4.
  18. "USP33 regulates centrosome biogenesis via deubiquitination of the centriolar protein CP110."
    Li J., D'Angiolella V., Seeley E.S., Kim S., Kobayashi T., Fu W., Campos E.I., Pagano M., Dynlacht B.D.
    Nature 495:255-259(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DEUBIQUITINATION, INTERACTION WITH USP20 AND USP33.

Entry informationi

Entry nameiCP110_HUMAN
AccessioniPrimary (citable) accession number: O43303
Secondary accession number(s): B7WP23
, O43335, Q68DV9, Q8NE13
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 21, 2001
Last sequence update: October 23, 2007
Last modified: October 29, 2014
This is version 122 of the entry and version 3 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 16
    Human chromosome 16: 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

External Data

Dasty 3