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Q5VT06

- CE350_HUMAN

UniProt

Q5VT06 - CE350_HUMAN

Protein

Centrosome-associated protein 350

Gene

CEP350

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 103 (01 Oct 2014)
      Sequence version 1 (07 Dec 2004)
      Previous versions | rss
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    Functioni

    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.5 Publications

    GO - Biological processi

    1. microtubule anchoring Source: InterPro

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Centrosome-associated protein 350
    Short name:
    Cep350
    Alternative name(s):
    Centrosome-associated protein of 350 kDa
    Gene namesi
    Name:CEP350
    Synonyms:CAP350, KIAA0480
    ORF Names:GM133
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:24238. CEP350.

    Subcellular locationi

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

    GO - Cellular componenti

    1. centrosome Source: UniProtKB
    2. cytoplasm Source: HPA
    3. membrane Source: UniProtKB
    4. nucleus Source: HPA
    5. spindle Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi762 – 7632LL → AA: Abolishes recruitment of PPARA to specific nuclear foci. No effect on interaction with PPARA (in vitro). 1 Publication

    Organism-specific databases

    PharmGKBiPA143485434.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 31173117Centrosome-associated protein 350PRO_0000233291Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei878 – 8781Phosphothreonine2 Publications
    Modified residuei1061 – 10611Phosphoserine2 Publications
    Modified residuei1253 – 12531Phosphothreonine2 Publications
    Modified residuei1256 – 12561Phosphoserine2 Publications
    Modified residuei1259 – 12591Phosphoserine2 Publications
    Modified residuei2204 – 22041Phosphothreonine2 Publications
    Modified residuei2206 – 22061Phosphoserine2 Publications
    Modified residuei2460 – 24601Phosphoserine2 Publications
    Modified residuei2839 – 28391Phosphoserine2 Publications

    Post-translational modificationi

    Phosphorylated during mitosis.4 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ5VT06.
    PaxDbiQ5VT06.
    PRIDEiQ5VT06.

    PTM databases

    PhosphoSiteiQ5VT06.

    Expressioni

    Tissue specificityi

    Detected in heart, brain, skeletal muscle, testis, placenta, lung, liver, kidney and pancreas.2 Publications

    Gene expression databases

    ArrayExpressiQ5VT06.
    BgeeiQ5VT06.
    CleanExiHS_CEP350.
    GenevestigatoriQ5VT06.

    Organism-specific databases

    HPAiHPA028355.
    HPA028357.
    HPA030845.

    Interactioni

    Subunit structurei

    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.5 Publications

    Protein-protein interaction databases

    BioGridi115191. 12 interactions.
    IntActiQ5VT06. 4 interactions.
    MINTiMINT-2867672.
    STRINGi9606.ENSP00000356579.

    Structurei

    Secondary structure

    1
    3117
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi2483 – 24864
    Beta strandi2501 – 25055
    Turni2506 – 25083
    Beta strandi2509 – 251810
    Beta strandi2520 – 253314
    Beta strandi2536 – 25383
    Beta strandi2540 – 25423
    Beta strandi2555 – 25584
    Helixi2560 – 25623

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2COZNMR-A2473-2581[»]
    ProteinModelPortaliQ5VT06.
    SMRiQ5VT06. Positions 2467-2581.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ5VT06.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini2517 – 255943CAP-GlyPROSITE-ProRule annotationAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili598 – 64548Sequence AnalysisAdd
    BLAST
    Coiled coili1369 – 141143Sequence AnalysisAdd
    BLAST
    Coiled coili1707 – 180094Sequence AnalysisAdd
    BLAST
    Coiled coili1856 – 189944Sequence AnalysisAdd
    BLAST
    Coiled coili2051 – 211060Sequence AnalysisAdd
    BLAST
    Coiled coili2719 – 275234Sequence AnalysisAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi1112 – 1281170Ser-richAdd
    BLAST
    Compositional biasi1502 – 155655Ser-richAdd
    BLAST

    Sequence similaritiesi

    Contains 1 CAP-Gly domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Coiled coil

    Phylogenomic databases

    eggNOGiCOG5244.
    HOGENOMiHOG000111528.
    HOVERGENiHBG095435.
    InParanoidiQ5VT06.
    KOiK16768.
    OMAiQWEHSEE.
    OrthoDBiEOG7G4QD6.
    PhylomeDBiQ5VT06.
    TreeFamiTF329845.

    Family and domain databases

    Gene3Di2.30.30.190. 1 hit.
    InterProiIPR000938. CAP-Gly_domain.
    IPR028750. CEP350.
    [Graphical view]
    PANTHERiPTHR13958. PTHR13958. 1 hit.
    PfamiPF01302. CAP_GLY. 1 hit.
    [Graphical view]
    SMARTiSM01052. CAP_GLY. 1 hit.
    [Graphical view]
    SUPFAMiSSF74924. SSF74924. 1 hit.
    PROSITEiPS00845. CAP_GLY_1. 1 hit.
    PS50245. CAP_GLY_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q5VT06-1 [UniParc]FASTAAdd to Basket

    « Hide

    MRSSKSKEVP LPNPRNSQSK DTVQADITTS WDALSQTKAA LRHIENKLEV     50
    APTSTAVCDS VMDTKKSSTS ATRKISRKDG RYLDDSWVNA PISKSTKSRK 100
    EKSRSPLRAT TLESNVKKNN RVEFREPLVS YREIHGAPSN FSSSHLESKH 150
    VYCVDVNEEK TESGNWMIGS REERNIRSCD FESSQSSVIN DTVVRFLNDR 200
    PAIDALQNSE CLIRMGASMR TEEEMPNRTK GSENNLKLSV NNMAHDTDPK 250
    ALRLTDSSPS STSTSNSQRL DILKRRQHDV KLEKLKERIR KQWEHSEETN 300
    GRGQKLGHID HPVMVVNVDN SVTAKVRKVA TAPPAPAYKG FNPSETKIRT 350
    PDGKVWQEAE FQNMSRELYR DLALHFADDI SIKEKPAEKS KEKKVVKPVR 400
    KVQKVAQLSS TECRTGSSHL ISTSSWRDGQ KLVKKILGPA PRMEPKEQRT 450
    ASSDRGGRER TAKSGGHIGR AESDPRLDVL HRHLQRNSER SRSKSRSENN 500
    IKKLASSLPD NKQEENTALN KDFLPIEIRG ILDDLQLDST AHTAKQDTVE 550
    LQNQKSSAPV HAPRSHSPVK RKPDKITANE DPPVISKRRH YDTDEVRQYI 600
    VRQQEERKRK QNEEKKAQKE ATEQKNKRLQ ELYRKQKEAF TKVKNVPPSE 650
    PSATRRLQET YSKLLLEKTL LEEPSHQHVT QETQAKPGYQ PSGESDKENK 700
    VQERPPSASS SSDMSLSEPP QPLARKDLME STWMQPERLS PQVHHSQPQP 750
    FAGTAGSLLS HLLSLEHVGI LHKDFESILP TRKNHNMASR PLTFTPQPYV 800
    TSPAAYTDAL LKPSASQYKS KLDRIEALKA TAASLSSRIE SEAKKLAGAS 850
    INYGSAWNTE YDVQQAPQED GPWTKAVTPP VKDDNEDVFS ARIQKMLGSC 900
    VSHATFDDDL PGVGNLSEFK KLPEMIRPQS AISSFRVRSP GPKPEGLLAQ 950
    LCKRQTDSSS SDMQACSQDK AKISLGSSID SVSEGPLLSE GSLSEEEGDQ 1000
    DGQPLLKVAE ILKEKEFCPG ERNSYEPIKE FQKEAEKFLP LFGHIGGTQS 1050
    KGPWEELAKG SPHSVINIFT KSYQLYGKGF EDKLDRGTST SRPLNATATP 1100
    LSGVSYEDDF VSSPGTGTST EKKSTLEPHS TLSPQEDHSN RKSAYDPSSV 1150
    DVTSQHSSGA QSAASSRSST SSKGKKGKKE KTEWLDSFTG NVQNSLLDEE 1200
    KAERGSHQGK KSGTSSKLSV KDFEQTLDTD STLEDLSGHS VSVSSDKGRS 1250
    QKTPTSPLSP SSQKSLQFDV AGTSSERSKS SVMPPTITGF KPNAPLTDLN 1300
    PAASRTTTEN MAPIPGSKRF SPAGLHHRMA AELSYLNAIE ESVRQLSDVE 1350
    RVRGISLAQQ ESVSLAQIIK AQQQRHERDL ALLKLKAEQE ALESQRQLEE 1400
    TRNKAAQVHA ESLQQVVQSQ REVTEVLQEA TCKIAAQQSE TARLTTDAAR 1450
    QICEMAELTR THISDAVVAS GAPLAILYDH QRQHLPDFVK QLRTRTETDR 1500
    KSPSVSLSQS KEGTLDSKHQ KYSASYDSYS ESSGYKNHDR RSSSGSSRQE 1550
    SPSVPSCKEN EKKLNGEKIE SSIDEQVQTA ADDSLRSDSV PSLPDEKDST 1600
    SIATEYSLKF DESMTEDEIE EQSFRSLLPS ESHRRFNMEK RRGHHDDSDE 1650
    EASPEKTTLS TAKELNMPFS GGQDSFSKFT MEMVRQYMKE EEMRAAHQSS 1700
    LLRLREKALK EKTKAELAWL EHQKKHLRDK GEDDKMPPLR KKQRGLLLRL 1750
    QQEKAEIKRL QEANKAARKE RQLILKQQEE IEKIRQTTIK LQEKLKSAGE 1800
    SKLDSHSDDD TKDNKATSPG PTDLETRSPS PISISSSETS SIMQKLKKMR 1850
    SRMDEKFLTK REQKLMQRRQ HAEELLEWKR RLDAEEAEIR QMEKQALAAW 1900
    DKELIKPKTP KKELEDQRTE QKEIASEEES PVPLYSHLNS ESSIPEELGS 1950
    PAVEYVPSES IGQEQPGSPD HSILTEEMIC SQELESSTSP SKHSLPKSCT 2000
    SVSKQESSKG SHRTGGQCHL PIKSHQHCYS WSDESLSMTQ SETTSDQSDI 2050
    EGRIRALKDE LRKRKSVVNQ LKKEQKKRQK ERLKAQEASL IKQLESYDEF 2100
    IKKTEAELSQ DLETSPTAKP QIKTLSSASE KPKIKPLTPL HRSETAKNWK 2150
    SLTESERSRG SLESIAEHVD ASLSGSERSV SERSLSAYAK RVNEWDSRTE 2200
    DFQTPSPVLR SSRKIREESG DSLENVPALH LLKELNATSR ILDMSDGKVG 2250
    ESSKKSEIKE IEYTKLKKSK IEDAFSKEGK SDVLLKLVLE QGDSSEILSK 2300
    KDLPLDSENV QKDLVGLAIE NLHKSEEMLK ERQSDQDMNH SPNIQSGKDI 2350
    HEQKNTKEKD LSWSEHLFAP KEIPYSEDFE VSSFKKEISA ELYKDDFEVS 2400
    SLLSLRKDSQ SCRDKPQPMR SSTSGATSFG SNEEISECLS EKSLSIHSNV 2450
    HSDRLLELKS PTELMKSKER SDVEHEQQVT ESPSLASVPT ADELFDFHIG 2500
    DRVLIGNVQP GILRFKGETS FAKGFWAGVE LDKPEGNNNG TYDGIAYFEC 2550
    KEKHGIFAPP QKISHIPENF DDYVDINEDE DCYSDERYQC YNQEQNDTEG 2600
    PKDREKDVSE YFYEKSLPSV NDIEASVNRS RSLKIETDNV QDISGVLEAH 2650
    VHQQSSVDSQ ISSKENKDLI SDATEKVSIA AEDDTLDNTF SEELEKQQQF 2700
    TEEEDNLYAE ASEKLCTPLL DLLTREKNQL EAQLKSSLNE EKKSKQQLEK 2750
    ISLLTDSLLK VFVKDTVNQL QQIKKTRDEK IQLSNQELLG DDQKKVTPQD 2800
    LSQNVEEQSP SISGCFLSSE LEDEKEEISS PDMCPRPESP VFGASGQEEL 2850
    AKRLAELELS REFLSALGDD QDWFDEDFGL SSSHKIQKNK AEETIVPLMA 2900
    EPKRVTQQPC ETLLAVPHTA EEVEILVHNA AEELWKWKEL GHDLHSISIP 2950
    TKLLGCASKG LDIESTSKRV YKQAVFDLTK EIFEEIFAED PNLNQPVWMK 3000
    PCRINSSYFR RVKNPNNLDE IKSFIASEVL KLFSLKKEPN HKTDWQKMMK 3050
    FGRKKRDRVD HILVQELHEE EAQWVNYDED ELCVKMQLAD GIFETLIKDT 3100
    IDVLNQISEK QGRMLLV 3117
    Length:3,117
    Mass (Da):350,930
    Last modified:December 7, 2004 - v1
    Checksum:iDD0E03EA96DA319E
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti25 – 251Missing in AAL91355. (PubMed:11891061)Curated
    Sequence conflicti114 – 1141S → G in AAL55733. 1 PublicationCurated
    Sequence conflicti459 – 4591E → R in AAL55733. 1 PublicationCurated
    Sequence conflicti2164 – 21641S → P in AAL55733. 1 PublicationCurated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti892 – 8921R → T.
    Corresponds to variant rs6692219 [ dbSNP | Ensembl ].
    VAR_059202
    Natural varianti945 – 9451E → Q.1 Publication
    Corresponds to variant rs2477120 [ dbSNP | Ensembl ].
    VAR_026126
    Natural varianti1213 – 12131G → V.
    Corresponds to variant rs12125245 [ dbSNP | Ensembl ].
    VAR_059203
    Natural varianti1445 – 14451T → A.
    Corresponds to variant rs16855164 [ dbSNP | Ensembl ].
    VAR_048671
    Natural varianti1446 – 14461T → A.
    Corresponds to variant rs16855164 [ dbSNP | Ensembl ].
    VAR_059204
    Natural varianti1517 – 15171S → A.
    Corresponds to variant rs12124336 [ dbSNP | Ensembl ].
    VAR_059205
    Natural varianti2044 – 20441T → P.
    Corresponds to variant rs56173179 [ dbSNP | Ensembl ].
    VAR_061092

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS1336.1.
    PIRiT00263.
    RefSeqiNP_055625.4. NM_014810.4.
    UniGeneiHs.413045.

    Genome annotation databases

    EnsembliENST00000367607; ENSP00000356579; ENSG00000135837.
    GeneIDi9857.
    KEGGihsa:9857.
    UCSCiuc001gnt.3. human.

    Polymorphism databases

    DMDMi74746869.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    CCDSi CCDS1336.1.
    PIRi T00263.
    RefSeqi NP_055625.4. NM_014810.4.
    UniGenei Hs.413045.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2COZ NMR - A 2473-2581 [» ]
    ProteinModelPortali Q5VT06.
    SMRi Q5VT06. Positions 2467-2581.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 115191. 12 interactions.
    IntActi Q5VT06. 4 interactions.
    MINTi MINT-2867672.
    STRINGi 9606.ENSP00000356579.

    PTM databases

    PhosphoSitei Q5VT06.

    Polymorphism databases

    DMDMi 74746869.

    Proteomic databases

    MaxQBi Q5VT06.
    PaxDbi Q5VT06.
    PRIDEi Q5VT06.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000367607 ; ENSP00000356579 ; ENSG00000135837 .
    GeneIDi 9857.
    KEGGi hsa:9857.
    UCSCi uc001gnt.3. human.

    Organism-specific databases

    CTDi 9857.
    GeneCardsi GC01P179923.
    H-InvDB HIX0001384.
    HGNCi HGNC:24238. CEP350.
    HPAi HPA028355.
    HPA028357.
    HPA030845.
    neXtProti NX_Q5VT06.
    PharmGKBi PA143485434.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5244.
    HOGENOMi HOG000111528.
    HOVERGENi HBG095435.
    InParanoidi Q5VT06.
    KOi K16768.
    OMAi QWEHSEE.
    OrthoDBi EOG7G4QD6.
    PhylomeDBi Q5VT06.
    TreeFami TF329845.

    Miscellaneous databases

    ChiTaRSi CEP350. human.
    EvolutionaryTracei Q5VT06.
    GeneWikii CEP350.
    GenomeRNAii 9857.
    NextBioi 37150.
    PROi Q5VT06.

    Gene expression databases

    ArrayExpressi Q5VT06.
    Bgeei Q5VT06.
    CleanExi HS_CEP350.
    Genevestigatori Q5VT06.

    Family and domain databases

    Gene3Di 2.30.30.190. 1 hit.
    InterProi IPR000938. CAP-Gly_domain.
    IPR028750. CEP350.
    [Graphical view ]
    PANTHERi PTHR13958. PTHR13958. 1 hit.
    Pfami PF01302. CAP_GLY. 1 hit.
    [Graphical view ]
    SMARTi SM01052. CAP_GLY. 1 hit.
    [Graphical view ]
    SUPFAMi SSF74924. SSF74924. 1 hit.
    PROSITEi PS00845. CAP_GLY_1. 1 hit.
    PS50245. CAP_GLY_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.
      , 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. 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. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. 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.

    Entry informationi

    Entry nameiCE350_HUMAN
    AccessioniPrimary (citable) accession number: Q5VT06
    Secondary accession number(s): O75068, Q8TDK3, Q8WY20
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 2, 2006
    Last sequence update: December 7, 2004
    Last modified: October 1, 2014
    This is version 103 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

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 1
      Human chromosome 1: 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3