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Q5VT06 (CE350_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 101. 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·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Centrosome-associated protein 350

Short name=Cep350
Alternative name(s):
Centrosome-associated protein of 350 kDa
Gene names
Name:CEP350
Synonyms:CAP350, KIAA0480
ORF Names:GM133
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length3117 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Plays an essential role in centriole growth by stabilizing a procentriolar seed composed of at least, SASS6 and CENPJ. Required for anchoring microtubules to the centrosomes and for the integrity of the microtubule network. Recruits PPARA to discrete subcellular compartments and thereby modulates PPARA activity. Ref.5 Ref.7 Ref.8 Ref.9 Ref.10

Subunit structure

Part of a ternary complex composed of SASS6, CENPJ and CEP350. Part of a ternary complex that contains CEP350, FGFR1OP and MAPRE1. Interacts directly with FGFR1OP via its C-terminus. Interacts with NR1H3, PPARA, PPARD and PPARG. Interacts directly with microtubules. Interacts with the fusion protein FGFR1OP-FGFR1, and by doing so recruits and activates PI3K and PLC-gamma. Ref.5 Ref.7 Ref.8 Ref.9 Ref.10

Subcellular location

Cytoplasmcytoskeletonmicrotubule organizing centercentrosome. Cytoplasmcytoskeletonspindle. Nucleus. Note: Associated with mitotic spindles. Nuclear, in discrete foci. Associated with intermediate filaments. Also present in the pericentrosomal area. Ref.4 Ref.5 Ref.7 Ref.8 Ref.10

Tissue specificity

Detected in heart, brain, skeletal muscle, testis, placenta, lung, liver, kidney and pancreas. Ref.3 Ref.5

Post-translational modification

Phosphorylated during mitosis. Ref.7

Sequence similarities

Contains 1 CAP-Gly domain.

Ontologies

Keywords
   Cellular componentCytoplasm
Cytoskeleton
Nucleus
   Coding sequence diversityPolymorphism
   DomainCoiled coil
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Cellular_componentcentrosome

Inferred from direct assay PubMed 21399614. Source: UniProtKB

cytoplasm

Inferred from direct assay. Source: HPA

nucleus

Inferred from direct assay. Source: HPA

spindle

Inferred from electronic annotation. Source: UniProtKB-SubCell

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 31173117Centrosome-associated protein 350
PRO_0000233291

Regions

Domain2517 – 255943CAP-Gly
Coiled coil598 – 64548 Potential
Coiled coil1369 – 141143 Potential
Coiled coil1707 – 180094 Potential
Coiled coil1856 – 189944 Potential
Coiled coil2051 – 211060 Potential
Coiled coil2719 – 275234 Potential
Compositional bias1112 – 1281170Ser-rich
Compositional bias1502 – 155655Ser-rich

Amino acid modifications

Modified residue8781Phosphothreonine Ref.11
Modified residue10611Phosphoserine Ref.13
Modified residue12531Phosphothreonine Ref.11
Modified residue12561Phosphoserine Ref.11
Modified residue12591Phosphoserine Ref.11
Modified residue22041Phosphothreonine Ref.11
Modified residue22061Phosphoserine Ref.11
Modified residue24601Phosphoserine Ref.11
Modified residue28391Phosphoserine Ref.6

Natural variations

Natural variant8921R → T.
Corresponds to variant rs6692219 [ dbSNP | Ensembl ].
VAR_059202
Natural variant9451E → Q. Ref.1
Corresponds to variant rs2477120 [ dbSNP | Ensembl ].
VAR_026126
Natural variant12131G → V.
Corresponds to variant rs12125245 [ dbSNP | Ensembl ].
VAR_059203
Natural variant14451T → A.
Corresponds to variant rs16855164 [ dbSNP | Ensembl ].
VAR_048671
Natural variant14461T → A.
Corresponds to variant rs16855164 [ dbSNP | Ensembl ].
VAR_059204
Natural variant15171S → A.
Corresponds to variant rs12124336 [ dbSNP | Ensembl ].
VAR_059205
Natural variant20441T → P.
Corresponds to variant rs56173179 [ dbSNP | Ensembl ].
VAR_061092

Experimental info

Mutagenesis762 – 7632LL → AA: Abolishes recruitment of PPARA to specific nuclear foci. No effect on interaction with PPARA (in vitro). Ref.5
Sequence conflict251Missing in AAL91355. Ref.3
Sequence conflict1141S → G in AAL55733. Ref.1
Sequence conflict4591E → R in AAL55733. Ref.1
Sequence conflict21641S → P in AAL55733. Ref.1

Secondary structure

................. 3117
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q5VT06 [UniParc].

Last modified December 7, 2004. Version 1.
Checksum: DD0E03EA96DA319E

FASTA3,117350,930
        10         20         30         40         50         60 
MRSSKSKEVP LPNPRNSQSK DTVQADITTS WDALSQTKAA LRHIENKLEV APTSTAVCDS 

        70         80         90        100        110        120 
VMDTKKSSTS ATRKISRKDG RYLDDSWVNA PISKSTKSRK EKSRSPLRAT TLESNVKKNN 

       130        140        150        160        170        180 
RVEFREPLVS YREIHGAPSN FSSSHLESKH VYCVDVNEEK TESGNWMIGS REERNIRSCD 

       190        200        210        220        230        240 
FESSQSSVIN DTVVRFLNDR PAIDALQNSE CLIRMGASMR TEEEMPNRTK GSENNLKLSV 

       250        260        270        280        290        300 
NNMAHDTDPK ALRLTDSSPS STSTSNSQRL DILKRRQHDV KLEKLKERIR KQWEHSEETN 

       310        320        330        340        350        360 
GRGQKLGHID HPVMVVNVDN SVTAKVRKVA TAPPAPAYKG FNPSETKIRT PDGKVWQEAE 

       370        380        390        400        410        420 
FQNMSRELYR DLALHFADDI SIKEKPAEKS KEKKVVKPVR KVQKVAQLSS TECRTGSSHL 

       430        440        450        460        470        480 
ISTSSWRDGQ KLVKKILGPA PRMEPKEQRT ASSDRGGRER TAKSGGHIGR AESDPRLDVL 

       490        500        510        520        530        540 
HRHLQRNSER SRSKSRSENN IKKLASSLPD NKQEENTALN KDFLPIEIRG ILDDLQLDST 

       550        560        570        580        590        600 
AHTAKQDTVE LQNQKSSAPV HAPRSHSPVK RKPDKITANE DPPVISKRRH YDTDEVRQYI 

       610        620        630        640        650        660 
VRQQEERKRK QNEEKKAQKE ATEQKNKRLQ ELYRKQKEAF TKVKNVPPSE PSATRRLQET 

       670        680        690        700        710        720 
YSKLLLEKTL LEEPSHQHVT QETQAKPGYQ PSGESDKENK VQERPPSASS SSDMSLSEPP 

       730        740        750        760        770        780 
QPLARKDLME STWMQPERLS PQVHHSQPQP FAGTAGSLLS HLLSLEHVGI LHKDFESILP 

       790        800        810        820        830        840 
TRKNHNMASR PLTFTPQPYV TSPAAYTDAL LKPSASQYKS KLDRIEALKA TAASLSSRIE 

       850        860        870        880        890        900 
SEAKKLAGAS INYGSAWNTE YDVQQAPQED GPWTKAVTPP VKDDNEDVFS ARIQKMLGSC 

       910        920        930        940        950        960 
VSHATFDDDL PGVGNLSEFK KLPEMIRPQS AISSFRVRSP GPKPEGLLAQ LCKRQTDSSS 

       970        980        990       1000       1010       1020 
SDMQACSQDK AKISLGSSID SVSEGPLLSE GSLSEEEGDQ DGQPLLKVAE ILKEKEFCPG 

      1030       1040       1050       1060       1070       1080 
ERNSYEPIKE FQKEAEKFLP LFGHIGGTQS KGPWEELAKG SPHSVINIFT KSYQLYGKGF 

      1090       1100       1110       1120       1130       1140 
EDKLDRGTST SRPLNATATP LSGVSYEDDF VSSPGTGTST EKKSTLEPHS TLSPQEDHSN 

      1150       1160       1170       1180       1190       1200 
RKSAYDPSSV DVTSQHSSGA QSAASSRSST SSKGKKGKKE KTEWLDSFTG NVQNSLLDEE 

      1210       1220       1230       1240       1250       1260 
KAERGSHQGK KSGTSSKLSV KDFEQTLDTD STLEDLSGHS VSVSSDKGRS QKTPTSPLSP 

      1270       1280       1290       1300       1310       1320 
SSQKSLQFDV AGTSSERSKS SVMPPTITGF KPNAPLTDLN PAASRTTTEN MAPIPGSKRF 

      1330       1340       1350       1360       1370       1380 
SPAGLHHRMA AELSYLNAIE ESVRQLSDVE RVRGISLAQQ ESVSLAQIIK AQQQRHERDL 

      1390       1400       1410       1420       1430       1440 
ALLKLKAEQE ALESQRQLEE TRNKAAQVHA ESLQQVVQSQ REVTEVLQEA TCKIAAQQSE 

      1450       1460       1470       1480       1490       1500 
TARLTTDAAR QICEMAELTR THISDAVVAS GAPLAILYDH QRQHLPDFVK QLRTRTETDR 

      1510       1520       1530       1540       1550       1560 
KSPSVSLSQS KEGTLDSKHQ KYSASYDSYS ESSGYKNHDR RSSSGSSRQE SPSVPSCKEN 

      1570       1580       1590       1600       1610       1620 
EKKLNGEKIE SSIDEQVQTA ADDSLRSDSV PSLPDEKDST SIATEYSLKF DESMTEDEIE 

      1630       1640       1650       1660       1670       1680 
EQSFRSLLPS ESHRRFNMEK RRGHHDDSDE EASPEKTTLS TAKELNMPFS GGQDSFSKFT 

      1690       1700       1710       1720       1730       1740 
MEMVRQYMKE EEMRAAHQSS LLRLREKALK EKTKAELAWL EHQKKHLRDK GEDDKMPPLR 

      1750       1760       1770       1780       1790       1800 
KKQRGLLLRL QQEKAEIKRL QEANKAARKE RQLILKQQEE IEKIRQTTIK LQEKLKSAGE 

      1810       1820       1830       1840       1850       1860 
SKLDSHSDDD TKDNKATSPG PTDLETRSPS PISISSSETS SIMQKLKKMR SRMDEKFLTK 

      1870       1880       1890       1900       1910       1920 
REQKLMQRRQ HAEELLEWKR RLDAEEAEIR QMEKQALAAW DKELIKPKTP KKELEDQRTE 

      1930       1940       1950       1960       1970       1980 
QKEIASEEES PVPLYSHLNS ESSIPEELGS PAVEYVPSES IGQEQPGSPD HSILTEEMIC 

      1990       2000       2010       2020       2030       2040 
SQELESSTSP SKHSLPKSCT SVSKQESSKG SHRTGGQCHL PIKSHQHCYS WSDESLSMTQ 

      2050       2060       2070       2080       2090       2100 
SETTSDQSDI EGRIRALKDE LRKRKSVVNQ LKKEQKKRQK ERLKAQEASL IKQLESYDEF 

      2110       2120       2130       2140       2150       2160 
IKKTEAELSQ DLETSPTAKP QIKTLSSASE KPKIKPLTPL HRSETAKNWK SLTESERSRG 

      2170       2180       2190       2200       2210       2220 
SLESIAEHVD ASLSGSERSV SERSLSAYAK RVNEWDSRTE DFQTPSPVLR SSRKIREESG 

      2230       2240       2250       2260       2270       2280 
DSLENVPALH LLKELNATSR ILDMSDGKVG ESSKKSEIKE IEYTKLKKSK IEDAFSKEGK 

      2290       2300       2310       2320       2330       2340 
SDVLLKLVLE QGDSSEILSK KDLPLDSENV QKDLVGLAIE NLHKSEEMLK ERQSDQDMNH 

      2350       2360       2370       2380       2390       2400 
SPNIQSGKDI HEQKNTKEKD LSWSEHLFAP KEIPYSEDFE VSSFKKEISA ELYKDDFEVS 

      2410       2420       2430       2440       2450       2460 
SLLSLRKDSQ SCRDKPQPMR SSTSGATSFG SNEEISECLS EKSLSIHSNV HSDRLLELKS 

      2470       2480       2490       2500       2510       2520 
PTELMKSKER SDVEHEQQVT ESPSLASVPT ADELFDFHIG DRVLIGNVQP GILRFKGETS 

      2530       2540       2550       2560       2570       2580 
FAKGFWAGVE LDKPEGNNNG TYDGIAYFEC KEKHGIFAPP QKISHIPENF DDYVDINEDE 

      2590       2600       2610       2620       2630       2640 
DCYSDERYQC YNQEQNDTEG PKDREKDVSE YFYEKSLPSV NDIEASVNRS RSLKIETDNV 

      2650       2660       2670       2680       2690       2700 
QDISGVLEAH VHQQSSVDSQ ISSKENKDLI SDATEKVSIA AEDDTLDNTF SEELEKQQQF 

      2710       2720       2730       2740       2750       2760 
TEEEDNLYAE ASEKLCTPLL DLLTREKNQL EAQLKSSLNE EKKSKQQLEK ISLLTDSLLK 

      2770       2780       2790       2800       2810       2820 
VFVKDTVNQL QQIKKTRDEK IQLSNQELLG DDQKKVTPQD LSQNVEEQSP SISGCFLSSE 

      2830       2840       2850       2860       2870       2880 
LEDEKEEISS PDMCPRPESP VFGASGQEEL AKRLAELELS REFLSALGDD QDWFDEDFGL 

      2890       2900       2910       2920       2930       2940 
SSSHKIQKNK AEETIVPLMA EPKRVTQQPC ETLLAVPHTA EEVEILVHNA AEELWKWKEL 

      2950       2960       2970       2980       2990       3000 
GHDLHSISIP TKLLGCASKG LDIESTSKRV YKQAVFDLTK EIFEEIFAED PNLNQPVWMK 

      3010       3020       3030       3040       3050       3060 
PCRINSSYFR RVKNPNNLDE IKSFIASEVL KLFSLKKEPN HKTDWQKMMK FGRKKRDRVD 

      3070       3080       3090       3100       3110 
HILVQELHEE EAQWVNYDED ELCVKMQLAD GIFETLIKDT IDVLNQISEK QGRMLLV 

« Hide

References

« Hide 'large scale' references
[1]"Cloning and characterization of a cDNA encoding a protein of 350 kDa (CAP350) associated with centrosomes."
Klein-Hitpass L., Esser F., Michels D., Schwerk C., Vassen L.
Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT GLN-945.
[2]"The DNA sequence and biological annotation of human chromosome 1."
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. expand/collapse author list , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]"Identification of six novel genes by experimental validation of GeneMachine predicted genes."
Makalowska I., Sood R., Faruque M.U., Hu P., Robbins C.M., Eddings E.M., Mestre J.D., Baxevanis A.D., Carpten J.D.
Gene 284:203-213(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-131, IDENTIFICATION, TISSUE SPECIFICITY.
[4]"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.
[5]"Activity and subcellular compartmentalization of peroxisome proliferator-activated receptor alpha are altered by the centrosome-associated protein CAP350."
Patel H., Truant R., Rachubinski R.A., Capone J.P.
J. Cell Sci. 118:175-186(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, MUTAGENESIS OF 762-LEU-LEU-763, INTERACTION WITH NR1H3; PPARA; PPARD AND PPARG.
[6]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2839, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[7]"A complex of two centrosomal proteins, CAP350 and FOP, cooperates with EB1 in microtubule anchoring."
Yan X., Habedanck R., Nigg E.A.
Mol. Biol. Cell 17:634-644(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION, INTERACTION WITH FGFR1OP.
[8]"Centrosomal CAP350 protein stabilises microtubules associated with the Golgi complex."
Hoppeler-Lebel A., Celati C., Bellett G., Mogensen M.M., Klein-Hitpass L., Bornens M., Tassin A.-M.
J. Cell Sci. 120:3299-3308(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH MICROTUBULE.
[9]"Myeloproliferative disorder FOP-FGFR1 fusion kinase recruits phosphoinositide-3 kinase and phospholipase Cgamma at the centrosome."
Lelievre H., Chevrier V., Tassin A.-M., Birnbaum D.
Mol. Cancer 7:30-30(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH FGFR1OP-FGFR1 FUSION PROTEIN.
[10]"Role of CAP350 in centriolar tubule stability and centriole assembly."
Le Clech M.
PLoS ONE 3:E3855-E3855(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, IDENTIFICATION IN A COMPLEX WITH SASS6 AND CENPJ.
[11]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-878; THR-1253; SER-1256; SER-1259; THR-2204; SER-2206 AND SER-2460, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[12]"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].
[13]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1061, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[14]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[15]"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].
[16]"Solution structure of the CAP-Gly domain in human centrosome-associated protein CAP350."
RIKEN structural genomics initiative (RSGI)
Submitted (NOV-2005) to the PDB data bank
Cited for: STRUCTURE BY NMR OF 2473-2581.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF287356 mRNA. Translation: AAL55733.1.
AL645487, AL390718, AL590632 Genomic DNA. Translation: CAH72345.1.
AL590632, AL390718, AL645487 Genomic DNA. Translation: CAI15177.1.
AL390718, AL590632, AL645487 Genomic DNA. Translation: CAI14833.1.
AF387614 mRNA. Translation: AAL91355.1.
CCDSCCDS1336.1.
PIRT00263.
RefSeqNP_055625.4. NM_014810.4.
UniGeneHs.413045.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2COZNMR-A2473-2581[»]
ProteinModelPortalQ5VT06.
SMRQ5VT06. Positions 2467-2581.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115191. 12 interactions.
IntActQ5VT06. 4 interactions.
MINTMINT-2867672.
STRING9606.ENSP00000356579.

PTM databases

PhosphoSiteQ5VT06.

Polymorphism databases

DMDM74746869.

Proteomic databases

MaxQBQ5VT06.
PaxDbQ5VT06.
PRIDEQ5VT06.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000367607; ENSP00000356579; ENSG00000135837.
GeneID9857.
KEGGhsa:9857.
UCSCuc001gnt.3. human.

Organism-specific databases

CTD9857.
GeneCardsGC01P179923.
H-InvDBHIX0001384.
HGNCHGNC:24238. CEP350.
HPAHPA028355.
HPA028357.
HPA030845.
neXtProtNX_Q5VT06.
PharmGKBPA143485434.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5244.
HOGENOMHOG000111528.
HOVERGENHBG095435.
InParanoidQ5VT06.
KOK16768.
OMAQWEHSEE.
OrthoDBEOG7G4QD6.
PhylomeDBQ5VT06.
TreeFamTF329845.

Gene expression databases

ArrayExpressQ5VT06.
BgeeQ5VT06.
CleanExHS_CEP350.
GenevestigatorQ5VT06.

Family and domain databases

Gene3D2.30.30.190. 1 hit.
InterProIPR000938. CAP-Gly_domain.
IPR028750. CEP350.
[Graphical view]
PANTHERPTHR13958. PTHR13958. 1 hit.
PfamPF01302. CAP_GLY. 1 hit.
[Graphical view]
SMARTSM01052. CAP_GLY. 1 hit.
[Graphical view]
SUPFAMSSF74924. SSF74924. 1 hit.
PROSITEPS00845. CAP_GLY_1. 1 hit.
PS50245. CAP_GLY_2. 1 hit.
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Other

ChiTaRSCEP350. human.
EvolutionaryTraceQ5VT06.
GeneWikiCEP350.
GenomeRNAi9857.
NextBio37150.
PROQ5VT06.

Entry information

Entry nameCE350_HUMAN
AccessionPrimary (citable) accession number: Q5VT06
Secondary accession number(s): O75068, Q8TDK3, Q8WY20
Entry history
Integrated into UniProtKB/Swiss-Prot: May 2, 2006
Last sequence update: December 7, 2004
Last modified: July 9, 2014
This is version 101 of the entry and version 1 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

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 1

Human chromosome 1: entries, gene names and cross-references to MIM