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Q7Z7A1 (CNTRL_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 92. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Centriolin
Alternative name(s):
Centrosomal protein 1
Centrosomal protein of 110 kDa
Short name=Cep110
Gene names
Name:CNTRL
Synonyms:CEP1, CEP110
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length2325 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved in cell cycle progression and cytokinesis. During the late steps of cytokinesis, anchors exocyst and SNARE complexes at the midbody, thereby allowing secretory vesicle-mediated abscission. Ref.2 Ref.9

Subunit structure

Interacts with HOOK2. Interacts with EXOC6 and SNAPIN. Associates with the exocyst complex. Ref.9 Ref.10

Subcellular location

Cytoplasmcytoskeletonmicrotubule organizing centercentrosome. Note: During cytokinesis, localizes to a ring-like structure at the central midbody. Ref.1 Ref.2 Ref.8

Tissue specificity

Highly expressed in testis and trachea. Ref.1

Involvement in disease

A chromosomal aberration involving CEP110 may be a cause of stem cell myeloproliferative disorder (MPD). Translocation t(8;9)(p12;q33) with FGFR1. MPD is characterized by myeloid hyperplasia, eosinophilia and T-cell or B-cell lymphoblastic lymphoma. In general it progresses to acute myeloid leukemia. The fusion protein CEP110-FGFR1 is found in the cytoplasm, exhibits constitutive kinase activity and may be responsible for the transforming activity.

Sequence similarities

Contains 4 LRR (leucine-rich) repeats.

Contains 1 LRRCT domain.

Sequence caution

The sequence AAH02932.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence AAH02932.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.

The sequence AAH89415.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q7Z7A1-1)

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.
Isoform 2 (identifier: Q7Z7A1-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-552: Missing.
Isoform 3 (identifier: Q7Z7A1-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-1331: Missing.
Isoform 4 (identifier: Q7Z7A1-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-1818: Missing.
     1962-1986: Missing.
Note: No experimental confirmation available.
Isoform 5 (identifier: Q7Z7A1-5)

The sequence of this isoform differs from the canonical sequence as follows:
     1291-1296: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 23252325Centriolin
PRO_0000323675

Regions

Repeat126 – 14722LRR 1
Repeat148 – 16922LRR 2
Repeat170 – 19122LRR 3
Repeat194 – 21522LRR 4
Domain228 – 26639LRRCT
Region1948 – 2118171Required for centrosome localization
Region1985 – 2325341Sufficient for interaction with HOOK2
Coiled coil267 – 34377 Potential
Coiled coil435 – 799365 Potential
Coiled coil851 – 1101251 Potential
Coiled coil1317 – 2255939 Potential
Compositional bias956 – 9594Poly-Lys
Compositional bias1147 – 11504Poly-Pro
Compositional bias1236 – 130772Pro-rich

Sites

Site2139 – 21402Breakpoint for translocation to form CEP110-FGFR1

Natural variations

Alternative sequence1 – 18181818Missing in isoform 4.
VSP_032046
Alternative sequence1 – 13311331Missing in isoform 3.
VSP_032047
Alternative sequence1 – 552552Missing in isoform 2.
VSP_032048
Alternative sequence1291 – 12966Missing in isoform 5.
VSP_032049
Alternative sequence1962 – 198625Missing in isoform 4.
VSP_032050
Natural variant561V → I. Ref.2
Corresponds to variant rs10818503 [ dbSNP | Ensembl ].
VAR_039559
Natural variant2161P → L.
Corresponds to variant rs10818504 [ dbSNP | Ensembl ].
VAR_039560
Natural variant8891A → T.
Corresponds to variant rs17292952 [ dbSNP | Ensembl ].
VAR_039561
Natural variant11461M → V.
Corresponds to variant rs35342437 [ dbSNP | Ensembl ].
VAR_061622

Experimental info

Sequence conflict13891Q → R in AAC32373. Ref.1
Sequence conflict16991K → Q in AAC32373. Ref.1
Sequence conflict18281E → D in AAC32373. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified March 18, 2008. Version 2.
Checksum: 93DD4CA08B5BD4AF

FASTA2,325268,886
        10         20         30         40         50         60 
MKKGSQQKIF SKAKIPSSSH SPIPSSMSNM RSRSLSPLIG SETLPFHSGG QWCEQVEIAD 

        70         80         90        100        110        120 
ENNMLLDYQD HKGADSHAGV RYITEALIKK LTKQDNLALI KSLNLSLSKD GGKKFKYIEN 

       130        140        150        160        170        180 
LEKCVKLEVL NLSYNLIGKI EKLDKLLKLR ELNLSYNKIS KIEGIENMCN LQKLNLAGNE 

       190        200        210        220        230        240 
IEHIPVWLGK KLKSLRVLNL KGNKISSLQD ISKLKPLQDL ISLILVENPV VTLPHYLQFT 

       250        260        270        280        290        300 
IFHLRSLESL EGQPVTTQDR QEAFERFSLE EVERLERDLE KKMIETEELK SKQTRFLEEI 

       310        320        330        340        350        360 
KNQDKLNKSL KEEAMLQKQS CEELKSDLNT KNELLKQKTI ELTRACQKQY ELEQELAFYK 

       370        380        390        400        410        420 
IDAKFEPLNY YPSEYAEIDK APDESPYIGK SRYKRNMFAT ESYIIDSAQA VQIKKMEPDE 

       430        440        450        460        470        480 
QLRNDHMNLR GHTPLDTQLE DKEKKISAAQ TRLSELHDEI EKAEQQILRA TEEFKQLEEA 

       490        500        510        520        530        540 
IQLKKISEAG KDLLYKQLSG RLQLVNKLRQ EALDLELQME KQKQEIAGKQ KEIKDLQIAI 

       550        560        570        580        590        600 
DSLDSKDPKH SHMKAQKSGK EQQLDIMNKQ YQQLESRLDE ILSRIAKETE EIKDLEEQLT 

       610        620        630        640        650        660 
EGQIAANEAL KKDLEGVISG LQEYLGTIKG QATQAQNECR KLRDEKETLL QRLTEVEQER 

       670        680        690        700        710        720 
DQLEIVAMDA ENMRKELAEL ESALQEQHEV NASLQQTQGD LSAYEAELEA RLNLRDAEAN 

       730        740        750        760        770        780 
QLKEELEKVT RLTQLEQSAL QAELEKERQA LKNALGKAQF SEEKEQENSE LHAKLKHLQD 

       790        800        810        820        830        840 
DNNLLKQQLK DFQNHLNHVV DGLVRPEEVA ARVDELRRKL KLGTGEMNIH SPSDVLGKSL 

       850        860        870        880        890        900 
ADLQKQFSEI LARSKWERDE AQVRERKLQE EMALQQEKLA TGQEEFRQAC ERALEARMNF 

       910        920        930        940        950        960 
DKRQHEARIQ QMENEIHYLQ ENLKSMEEIQ GLTDLQLQEA DEEKERILAQ LRELEKKKKL 

       970        980        990       1000       1010       1020 
EDAKSQEQVF GLDKELKKLK KAVATSDKLA TAELTIAKDQ LKSLHGTVMK INQERAEELQ 

      1030       1040       1050       1060       1070       1080 
EAERFSRKAA QAARDLTRAE AEIELLQNLL RQKGEQFRLE MEKTGVGTGA NSQVLEIEKL 

      1090       1100       1110       1120       1130       1140 
NETMERQRTE IARLQNVLDL TGSDNKGGFE NVLEEIAELR REVSYQNDYI SSMADPFKRR 

      1150       1160       1170       1180       1190       1200 
GYWYFMPPPP SSKVSSHSSQ ATKDSGVGLK YSASTPVRKP RPGQQDGKEG SQPPPASGYW 

      1210       1220       1230       1240       1250       1260 
VYSPIRSGLH KLFPSRDADS GGDSQEESEL DDQEEPPFVP PPGYMMYTVL PDGSPVPQGM 

      1270       1280       1290       1300       1310       1320 
ALYAPPPPLP NNSRPLTPGT VVYGPPPAGA PMVYGPPPPN FSIPFIPMGV LHCNVPEHHN 

      1330       1340       1350       1360       1370       1380 
LENEVSRLED IMQHLKSKKR EERWMRASKR QSEKEMEELH HNIDDLLQEK KSLECEVEEL 

      1390       1400       1410       1420       1430       1440 
HRTVQKRQQQ KDFIDGNVES LMTELEIEKS LKHHEDIVDE IECIEKTLLK RRSELREADR 

      1450       1460       1470       1480       1490       1500 
LLAEAESELS CTKEKTKNAV EKFTDAKRSL LQTESDAEEL ERRAQETAVN LVKADQQLRS 

      1510       1520       1530       1540       1550       1560 
LQADAKDLEQ HKIKQEEILK EINKIVAAKD SDFQCLSKKK EKLTEELQKL QKDIEMAERN 

      1570       1580       1590       1600       1610       1620 
EDHHLQVLKE SEVLLQAKRA ELEKLKSQVT SQQQEMAVLD RQLGHKKEEL HLLQGSMVQA 

      1630       1640       1650       1660       1670       1680 
KADLQEALRL GETEVTEKCN HIREVKSLLE ELSFQKGELN VQISERKTQL TLIKQEIEKE 

      1690       1700       1710       1720       1730       1740 
EENLQVVLRQ MSKHKTELKN ILDMLQLENH ELQGLKLQHD QRVSELEKTQ VAVLEEKLEL 

      1750       1760       1770       1780       1790       1800 
ENLQQISQQQ KGEIEWQKQL LERDKREIER MTAESRALQS CVECLSKEKE DLQEKCDIWE 

      1810       1820       1830       1840       1850       1860 
KKLAQTKRVL AAAEENSKME QSNLEKLELN VRKLQQELDQ LNRDKLSLHN DISAMQQQLQ 

      1870       1880       1890       1900       1910       1920 
EKREAVNSLQ EELANVQDHL NLAKQDLLHT TKHQDVLLSE QTRLQKDISE WANRFEDCQK 

      1930       1940       1950       1960       1970       1980 
EEETKQQQLQ VLQNEIEENK LKLVQQEMMF QRLQKERESE ESKLETSKVT LKEQQHQLEK 

      1990       2000       2010       2020       2030       2040 
ELTDQKSKLD QVLSKVLAAE ERVRTLQEEE RWCESLEKTL SQTKRQLSER EQQLVEKSGE 

      2050       2060       2070       2080       2090       2100 
LLALQKEADS MRADFSLLRN QFLTERKKAE KQVASLKEAL KIQRSQLEKN LLEQKQENSC 

      2110       2120       2130       2140       2150       2160 
IQKEMATIEL VAQDNHERAR RLMKELNQMQ YEYTELKKQM ANQKDLERRQ MEISDAMRTL 

      2170       2180       2190       2200       2210       2220 
KSEVKDEIRT SLKNLNQFLP ELPADLEAIL ERNENLEGEL ESLKENLPFT MNEGPFEEKL 

      2230       2240       2250       2260       2270       2280 
NFSQVHIMDE HWRGEALREK LRHREDRLKA QLRHCMSKQA EVLIKGKRQT EGTLHSLRRQ 

      2290       2300       2310       2320 
VDALGELVTS TSADSASSPS LSQLESSLTE DSQLGQNQEK NASAR 

« Hide

Isoform 2 [UniParc].

Checksum: F430B910E219D5E2
Show »

FASTA1,773205,172
Isoform 3 [UniParc].

Checksum: BFE7F893259BA73D
Show »

FASTA994116,799
Isoform 4 [UniParc].

Checksum: 1B4867D4FEAFE023
Show »

FASTA48256,587
Isoform 5 [UniParc].

Checksum: 5C9924F8D58B852A
Show »

FASTA2,319268,241

References

« Hide 'large scale' references
[1]"FGFR1 is fused to the centrosome-associated protein CEP110 in the 8p12 stem cell myeloproliferative disorder with t(8;9)(p12;q33)."
Guasch G., Mack G.J., Popovici C., Dastugue N., Birnbaum D., Rattner J.B., Pebusque M.-J.
Blood 95:1788-1796(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), TISSUE SPECIFICITY, CHROMOSOMAL TRANSLOCATION WITH FGFR1, SUBCELLULAR LOCATION.
[2]"A novel human protein of the maternal centriole is required for the final stages of cytokinesis and entry into S phase."
Gromley A., Jurczyk A., Sillibourne J., Halilovic E., Mogensen M., Groisman I., Blomberg M., Doxsey S.J.
J. Cell Biol. 161:535-545(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT ILE-56, SUBCELLULAR LOCATION, FUNCTION.
[3]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
Tissue: Liver.
[4]"DNA sequence and analysis of human chromosome 9."
Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L. expand/collapse author list , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
Nature 429:369-374(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] OF 1-1513 (ISOFORM 2).
Tissue: Lymph and Placenta.
[6]"Humoral detection of leukaemia-associated antigens in presentation acute myeloid leukaemia."
Guinn B.-A., Bland E.A., Lodi U., Liggins A.P., Tobal K., Petters S., Wells J.W., Banham A.H., Mufti G.J.
Biochem. Biophys. Res. Commun. 335:1293-1304(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 434-1677 (ISOFORM 1).
[7]"Characterization of long cDNA clones from human adult spleen. II. The complete sequences of 81 cDNA clones."
Jikuya H., Takano J., Kikuno R., Hirosawa M., Nagase T., Nomura N., Ohara O.
DNA Res. 10:49-57(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 527-2325 (ISOFORM 5).
Tissue: Spleen.
[8]"CEP110 and ninein are located in a specific domain of the centrosome associated with centrosome maturation."
Ou Y.Y., Mack G.J., Zhang M., Rattner J.B.
J. Cell Sci. 115:1825-1835(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[9]"Centriolin anchoring of exocyst and SNARE complexes at the midbody is required for secretory-vesicle-mediated abscission."
Gromley A., Yeaman C., Rosa J., Redick S., Chen C.-T., Mirabelle S., Guha M., Sillibourne J., Doxsey S.J.
Cell 123:75-87(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH EXOC6 AND SNAPIN.
[10]"Hook2 localizes to the centrosome, binds directly to centriolin/CEP110 and contributes to centrosomal function."
Szebenyi G., Hall B., Yu R., Hashim A.I., Kraemer H.
Traffic 8:32-46(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HOOK2.
[11]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF083322 mRNA. Translation: AAC32373.1.
AF513978 mRNA. Translation: AAP43846.1.
BX640927 mRNA. Translation: CAE45965.1.
AL137068 Genomic DNA. Translation: CAI12358.1.
AL137068 Genomic DNA. Translation: CAM13285.1.
BC002932 mRNA. Translation: AAH02932.1. Sequence problems.
BC089415 mRNA. Translation: AAH89415.1. Sequence problems.
BC137286 mRNA. Translation: AAI37287.1.
AY651261 mRNA. Translation: AAX35689.1.
AK074079 mRNA. Translation: BAB84905.1.
RefSeqNP_008949.4. NM_007018.4.
XP_005251736.1. XM_005251679.2.
UniGeneHs.653263.

3D structure databases

ProteinModelPortalQ7Z7A1.
SMRQ7Z7A1. Positions 47-279.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid116248. 4 interactions.
DIPDIP-47280N.
IntActQ7Z7A1. 17 interactions.
MINTMINT-4988988.

PTM databases

PhosphoSiteQ7Z7A1.

Polymorphism databases

DMDM172045911.

Proteomic databases

PaxDbQ7Z7A1.
PRIDEQ7Z7A1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000238341; ENSP00000238341; ENSG00000119397. [Q7Z7A1-1]
ENST00000373850; ENSP00000362956; ENSG00000119397. [Q7Z7A1-2]
ENST00000373855; ENSP00000362962; ENSG00000119397. [Q7Z7A1-1]
GeneID11064.
KEGGhsa:11064.
UCSCuc004bkx.1. human. [Q7Z7A1-1]
uc004blb.1. human. [Q7Z7A1-3]
uc010mvp.1. human. [Q7Z7A1-4]

Organism-specific databases

CTD11064.
GeneCardsGC09P123839.
H-InvDBHIX0008344.
HGNCHGNC:1858. CNTRL.
HPAHPA020468.
HPA020480.
HPA051583.
MIM605496. gene.
neXtProtNX_Q7Z7A1.
PharmGKBPA26414.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG145909.
HOVERGENHBG101203.
InParanoidQ7Z7A1.
KOK16770.
OMADESPYIG.
OrthoDBEOG7NSB1F.
PhylomeDBQ7Z7A1.
TreeFamTF101135.

Enzyme and pathway databases

ReactomeREACT_115566. Cell Cycle.
REACT_116125. Disease.

Gene expression databases

ArrayExpressQ7Z7A1.
BgeeQ7Z7A1.
CleanExHS_CEP110.
GenevestigatorQ7Z7A1.

Family and domain databases

InterProIPR028640. CEP110.
IPR001611. Leu-rich_rpt.
[Graphical view]
PANTHERPTHR18877. PTHR18877. 1 hit.
PROSITEPS51450. LRR. 5 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSCNTRL. human.
GeneWikiCNTRL.
GenomeRNAi11064.
NextBio42047.
PROQ7Z7A1.
SOURCESearch...

Entry information

Entry nameCNTRL_HUMAN
AccessionPrimary (citable) accession number: Q7Z7A1
Secondary accession number(s): A2A2Y1 expand/collapse secondary AC list , B2RP67, Q3MN79, Q5FWF8, Q5JVD0, Q6MZR3, Q6PKC1, Q8TEP3, Q9Y489
Entry history
Integrated into UniProtKB/Swiss-Prot: March 18, 2008
Last sequence update: March 18, 2008
Last modified: April 16, 2014
This is version 92 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 9

Human chromosome 9: entries, gene names and cross-references to MIM