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Q5SW79

- CE170_HUMAN

UniProt

Q5SW79 - CE170_HUMAN

Protein

Centrosomal protein of 170 kDa

Gene

CEP170

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 95 (01 Oct 2014)
      Sequence version 1 (21 Dec 2004)
      Previous versions | rss
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    Functioni

    Plays a role in microtubule organization.1 Publication

    GO - Molecular functioni

    1. protein binding Source: IntAct

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Centrosomal protein of 170 kDa
    Short name:
    Cep170
    Alternative name(s):
    KARP-1-binding protein
    Short name:
    KARP1-binding protein
    Gene namesi
    Name:CEP170
    Synonyms:FAM68A, KAB, KIAA0470
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:28920. CEP170.

    Subcellular locationi

    Cytoplasmcytoskeletonmicrotubule organizing centercentrosomecentriole 1 Publication. Cytoplasmcytoskeletonspindle 1 Publication
    Note: Associated with the mature mother centriole. Associated with spindle microtubules during mitosis.

    GO - Cellular componenti

    1. centriole Source: MGI
    2. centrosome Source: UniProtKB
    3. cytoplasm Source: HPA
    4. microtubule Source: UniProtKB-KW
    5. nuclear membrane Source: HPA
    6. spindle Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton, Microtubule

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA128395757.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 15841584Centrosomal protein of 170 kDaPRO_0000282887Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei356 – 3561Phosphoserine5 Publications
    Modified residuei359 – 3591Phosphoserine5 Publications
    Modified residuei364 – 3641Phosphotyrosine2 Publications
    Modified residuei446 – 4461Phosphoserine2 Publications
    Modified residuei497 – 4971Phosphoserine2 Publications
    Modified residuei501 – 5011Phosphothreonine2 Publications
    Modified residuei633 – 6331Phosphoserine3 Publications
    Modified residuei636 – 6361Phosphoserine4 Publications
    Modified residuei838 – 8381Phosphoserine3 Publications
    Modified residuei930 – 9301Phosphoserine2 Publications
    Modified residuei933 – 9331Phosphoserine2 Publications
    Modified residuei958 – 9581Phosphoserine2 Publications
    Modified residuei1112 – 11121Phosphoserine4 Publications
    Modified residuei1114 – 11141Phosphoserine2 Publications
    Modified residuei1160 – 11601Phosphoserine2 Publications
    Modified residuei1165 – 11651Phosphoserine2 Publications
    Modified residuei1251 – 12511Phosphoserine2 Publications

    Post-translational modificationi

    Phosphorylated; probably by PLK1.8 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ5SW79.
    PaxDbiQ5SW79.
    PRIDEiQ5SW79.

    PTM databases

    PhosphoSiteiQ5SW79.

    Miscellaneous databases

    PMAP-CutDBQ5SW79.

    Expressioni

    Gene expression databases

    ArrayExpressiQ5SW79.
    BgeeiQ5SW79.
    CleanExiHS_CEP170.
    GenevestigatoriQ5SW79.

    Organism-specific databases

    HPAiHPA042151.
    HPA045787.

    Interactioni

    Subunit structurei

    Interacts with PLK1.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    vprP125204EBI-1104799,EBI-6164519From a different organism.

    Protein-protein interaction databases

    BioGridi115193. 19 interactions.
    DIPiDIP-37594N.
    IntActiQ5SW79. 15 interactions.
    MINTiMINT-1790395.
    STRINGi9606.ENSP00000415575.

    Structurei

    Secondary structure

    1
    1584
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi2 – 109
    Beta strandi15 – 173
    Beta strandi23 – 297
    Beta strandi31 – 333
    Beta strandi44 – 496
    Turni50 – 534
    Beta strandi54 – 596
    Beta strandi66 – 683
    Beta strandi86 – 894
    Beta strandi96 – 1049
    Helixi107 – 1115
    Helixi113 – 1208

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4JONX-ray2.15A/B/C/D/E1-126[»]
    ProteinModelPortaliQ5SW79.
    SMRiQ5SW79. Positions 1-123.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini23 – 7351FHAPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni853 – 1584732Targeting to microtubulesAdd
    BLAST
    Regioni1113 – 1584472Targeting to centrosomesAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili1467 – 149529Sequence AnalysisAdd
    BLAST

    Sequence similaritiesi

    Belongs to the CEP170 family.Curated
    Contains 1 FHA domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Coiled coil

    Phylogenomic databases

    eggNOGiNOG18196.
    HOVERGENiHBG058059.
    KOiK16463.
    OMAiQSSGRMR.
    OrthoDBiEOG741Z19.
    PhylomeDBiQ5SW79.
    TreeFamiTF328469.

    Family and domain databases

    Gene3Di2.60.200.20. 1 hit.
    InterProiIPR026644. CEP170.
    IPR029300. CEP170_C.
    IPR000253. FHA_dom.
    IPR008984. SMAD_FHA_domain.
    [Graphical view]
    PANTHERiPTHR15715:SF17. PTHR15715:SF17. 1 hit.
    PfamiPF15308. CEP170_C. 1 hit.
    PF00498. FHA. 1 hit.
    [Graphical view]
    SMARTiSM00240. FHA. 1 hit.
    [Graphical view]
    SUPFAMiSSF49879. SSF49879. 1 hit.
    PROSITEiPS50006. FHA_DOMAIN. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q5SW79-1) [UniParc]FASTAAdd to Basket

    Also known as: Alpha

    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

    MSLTSWFLVS SGGTRHRLPR EMIFVGRDDC ELMLQSRSVD KQHAVINYDA     50
    STDEHLVKDL GSLNGTFVND VRIPEQTYIT LKLEDKLRFG YDTNLFTVVQ 100
    GEMRVPEEAL KHEKFTIQLQ LSQKSSESEL SKSASAKSID SKVADAATEV 150
    QHKTTEALKS EEKAMDISAM PRGTPLYGQP SWWGDDEVDE KRAFKTNGKP 200
    EEKNHEAGTS GCGIDAKQVE EQSAAANEEV LFPFCREPSY FEIPTKEFQQ 250
    PSQITESTIH EIPTKDTPSS HITGAGHASF TIEFDDSTPG KVTIRDHVTK 300
    FTSDQRHKSK KSSPGTQDLL GIQTGMMAPE NKVADWLAQN NPPQMLWERT 350
    EEDSKSIKSD VPVYLKRLKG NKHDDGTQSD SENAGAHRRC SKRATLEEHL 400
    RRHHSEHKKL QKVQATEKHQ DQAVTSSAHH RGGHGVPHGK LLKQKSEEPS 450
    VSIPFLQTAL LRSSGSLGHR PSQEMDKMLK NQATSATSEK DNDDDQSDKG 500
    TYTIELENPN SEEVEARKMI DKVFGVDDNQ DYNRPVINEK HKDLIKDWAL 550
    SSAAAVMEER KPLTTSGFHH SEEGTSSSGS KRWVSQWASL AANHTRHDQE 600
    ERIMEFSAPL PLENETEISE SGMTVRSTGS ATSLASQGER RRRTLPQLPN 650
    EEKSLESHRA KVVTQRSEIG EKQDTELQEK ETPTQVYQKD KQDADRPLSK 700
    MNRAVNGETL KTGGDNKTLL HLGSSAPGKE KSETDKETSL VKQTLAKLQQ 750
    QEQREEAQWT PTKLSSKNVS GQTDKCREET FKQESQPPEK NSGHSTSKGD 800
    RVAQSESKRR KAEEILKSQT PKGGDKKESS KSLVRQGSFT IEKPSPNIPI 850
    ELIPHINKQT SSTPSSLALT SASRIRERSE SLDPDSSMDT TLILKDTEAV 900
    MAFLEAKLRE DNKTDEGPDT PSYNRDNSIS PESDVDTAST ISLVTGETER 950
    KSTQKRKSFT SLYKDRCSTG SPSKDVTKSS SSGAREKMEK KTKSRSTDVG 1000
    SRADGRKFVQ SSGRIRQPSV DLTDDDQTSS VPHSAISDIM SSDQETYSCK 1050
    PHGRTPLTSA DEHVHSKLEG SKVTKSKTSP VVSGSSSKST TLPRPRPTRT 1100
    SLLRRARLGE ASDSELADAD KASVASEVST TSSTSKPPTG RRNISRIDLL 1150
    AQPRRTRLGS LSARSDSEAT ISRSSASSRT AEAIIRSGAR LVPSDKFSPR 1200
    IRANSISRLS DSKVKSMTSA HGSASVNSRW RRFPTDYAST SEDEFGSNRN 1250
    SPKHTRLRTS PALKTTRLQS AGSAMPTSSS FKHRIKEQED YIRDWTAHRE 1300
    EIARISQDLA LIAREINDVA GEIDSVTSSG TAPSTTVSTA ATTPGSAIDT 1350
    REELVDRVFD ESLNFRKIPP LVHSKTPEGN NGRSGDPRPQ AAEPPDHLTI 1400
    TRRRTWSRDE VMGDNLLLSS VFQFSKKIRQ SIDKTAGKIR ILFKDKDRNW 1450
    DDIESKLRAE SEVPIVKTSS MEISSILQEL KRVEKQLQAI NAMIDPDGTL 1500
    EALNNMGFPS AMLPSPPKQK SSPVNNHHSP GQTPTLGQPE ARALHPAAVS 1550
    AAAEFENAES EADFSIHFNR FNPDGEEEDV TVQE 1584
    Length:1,584
    Mass (Da):175,293
    Last modified:December 21, 2004 - v1
    Checksum:i50E981650D21B2E6
    GO
    Isoform 2 (identifier: Q5SW79-2) [UniParc]FASTAAdd to Basket

    Also known as: Gamma, 3

    The sequence of this isoform differs from the canonical sequence as follows:
         425-522: Missing.
         1226-1261: Missing.
         1353-1353: E → EVGDLHGEMHK

    Show »
    Length:1,460
    Mass (Da):161,408
    Checksum:i4EEECA047C7B0EFA
    GO
    Isoform 3 (identifier: Q5SW79-3) [UniParc]FASTAAdd to Basket

    Also known as: Beta, KAB2

    The sequence of this isoform differs from the canonical sequence as follows:
         425-522: Missing.

    Show »
    Length:1,486
    Mass (Da):164,539
    Checksum:i376DEE4949EC24D1
    GO

    Sequence cautioni

    The sequence BAA32315.2 differs from that shown. Reason: Erroneous initiation.

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti213 – 2131G → S.3 Publications
    Corresponds to variant rs2631092 [ dbSNP | Ensembl ].
    VAR_031437

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei425 – 52298Missing in isoform 2 and isoform 3. 3 PublicationsVSP_024240Add
    BLAST
    Alternative sequencei1226 – 126136Missing in isoform 2. 3 PublicationsVSP_024241Add
    BLAST
    Alternative sequencei1353 – 13531E → EVGDLHGEMHK in isoform 2. 3 PublicationsVSP_024242

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB022657 mRNA. Translation: BAA83378.1.
    AB022658 mRNA. Translation: BAA83379.1.
    AB022659 mRNA. Translation: BAA83380.1.
    AB007939 mRNA. Translation: BAA32315.2. Different initiation.
    AL606534, AC092782 Genomic DNA. Translation: CAI12943.1.
    AL606534, AC092782 Genomic DNA. Translation: CAI12944.1.
    AL606534, AC092782 Genomic DNA. Translation: CAI12945.1.
    BC050722 mRNA. Translation: AAH50722.1. Different termination.
    CCDSiCCDS44337.1. [Q5SW79-3]
    CCDS44338.1. [Q5SW79-2]
    CCDS44339.1. [Q5SW79-1]
    PIRiT00095.
    RefSeqiNP_001035863.1. NM_001042404.1. [Q5SW79-3]
    NP_001035864.1. NM_001042405.1. [Q5SW79-2]
    NP_055627.2. NM_014812.2. [Q5SW79-1]
    XP_006711912.1. XM_006711849.1. [Q5SW79-1]
    XP_006711914.1. XM_006711851.1. [Q5SW79-3]
    XP_006711915.1. XM_006711852.1. [Q5SW79-2]
    XP_006725044.1. XM_006724981.1. [Q5SW79-1]
    XP_006725046.1. XM_006724983.1. [Q5SW79-3]
    XP_006725047.1. XM_006724984.1. [Q5SW79-2]
    UniGeneiHs.533635.

    Genome annotation databases

    EnsembliENST00000366542; ENSP00000355500; ENSG00000143702. [Q5SW79-1]
    ENST00000366543; ENSP00000355501; ENSG00000143702. [Q5SW79-2]
    ENST00000366544; ENSP00000355502; ENSG00000143702. [Q5SW79-3]
    GeneIDi9859.
    KEGGihsa:9859.
    UCSCiuc021plo.1. human. [Q5SW79-1]
    uc021plp.1. human. [Q5SW79-2]
    uc021plq.1. human. [Q5SW79-3]

    Polymorphism databases

    DMDMi74743919.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB022657 mRNA. Translation: BAA83378.1 .
    AB022658 mRNA. Translation: BAA83379.1 .
    AB022659 mRNA. Translation: BAA83380.1 .
    AB007939 mRNA. Translation: BAA32315.2 . Different initiation.
    AL606534 , AC092782 Genomic DNA. Translation: CAI12943.1 .
    AL606534 , AC092782 Genomic DNA. Translation: CAI12944.1 .
    AL606534 , AC092782 Genomic DNA. Translation: CAI12945.1 .
    BC050722 mRNA. Translation: AAH50722.1 . Different termination.
    CCDSi CCDS44337.1. [Q5SW79-3 ]
    CCDS44338.1. [Q5SW79-2 ]
    CCDS44339.1. [Q5SW79-1 ]
    PIRi T00095.
    RefSeqi NP_001035863.1. NM_001042404.1. [Q5SW79-3 ]
    NP_001035864.1. NM_001042405.1. [Q5SW79-2 ]
    NP_055627.2. NM_014812.2. [Q5SW79-1 ]
    XP_006711912.1. XM_006711849.1. [Q5SW79-1 ]
    XP_006711914.1. XM_006711851.1. [Q5SW79-3 ]
    XP_006711915.1. XM_006711852.1. [Q5SW79-2 ]
    XP_006725044.1. XM_006724981.1. [Q5SW79-1 ]
    XP_006725046.1. XM_006724983.1. [Q5SW79-3 ]
    XP_006725047.1. XM_006724984.1. [Q5SW79-2 ]
    UniGenei Hs.533635.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    4JON X-ray 2.15 A/B/C/D/E 1-126 [» ]
    ProteinModelPortali Q5SW79.
    SMRi Q5SW79. Positions 1-123.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 115193. 19 interactions.
    DIPi DIP-37594N.
    IntActi Q5SW79. 15 interactions.
    MINTi MINT-1790395.
    STRINGi 9606.ENSP00000415575.

    PTM databases

    PhosphoSitei Q5SW79.

    Polymorphism databases

    DMDMi 74743919.

    Proteomic databases

    MaxQBi Q5SW79.
    PaxDbi Q5SW79.
    PRIDEi Q5SW79.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000366542 ; ENSP00000355500 ; ENSG00000143702 . [Q5SW79-1 ]
    ENST00000366543 ; ENSP00000355501 ; ENSG00000143702 . [Q5SW79-2 ]
    ENST00000366544 ; ENSP00000355502 ; ENSG00000143702 . [Q5SW79-3 ]
    GeneIDi 9859.
    KEGGi hsa:9859.
    UCSCi uc021plo.1. human. [Q5SW79-1 ]
    uc021plp.1. human. [Q5SW79-2 ]
    uc021plq.1. human. [Q5SW79-3 ]

    Organism-specific databases

    CTDi 9859.
    GeneCardsi GC01M243287.
    H-InvDB HIX0004456.
    HGNCi HGNC:28920. CEP170.
    HPAi HPA042151.
    HPA045787.
    MIMi 613023. gene.
    neXtProti NX_Q5SW79.
    PharmGKBi PA128395757.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG18196.
    HOVERGENi HBG058059.
    KOi K16463.
    OMAi QSSGRMR.
    OrthoDBi EOG741Z19.
    PhylomeDBi Q5SW79.
    TreeFami TF328469.

    Miscellaneous databases

    GeneWikii CEP170.
    GenomeRNAii 9859.
    NextBioi 37158.
    PMAP-CutDB Q5SW79.
    PROi Q5SW79.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q5SW79.
    Bgeei Q5SW79.
    CleanExi HS_CEP170.
    Genevestigatori Q5SW79.

    Family and domain databases

    Gene3Di 2.60.200.20. 1 hit.
    InterProi IPR026644. CEP170.
    IPR029300. CEP170_C.
    IPR000253. FHA_dom.
    IPR008984. SMAD_FHA_domain.
    [Graphical view ]
    PANTHERi PTHR15715:SF17. PTHR15715:SF17. 1 hit.
    Pfami PF15308. CEP170_C. 1 hit.
    PF00498. FHA. 1 hit.
    [Graphical view ]
    SMARTi SM00240. FHA. 1 hit.
    [Graphical view ]
    SUPFAMi SSF49879. SSF49879. 1 hit.
    PROSITEi PS50006. FHA_DOMAIN. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Molecular cloning and initial characterization of KAB."
      Hara Y., Adachi Y.
      Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3), VARIANT SER-213.
      Tissue: Brain and Cervix carcinoma.
    2. "Characterization of cDNA clones in size-fractionated cDNA libraries from human brain."
      Seki N., Ohira M., Nagase T., Ishikawa K., Miyajima N., Nakajima D., Nomura N., Ohara O.
      DNA Res. 4:345-349(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), VARIANT SER-213.
      Tissue: Brain.
    3. Ohara O.
      Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: SEQUENCE REVISION.
    4. "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].
    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 1-543 (ISOFORM 2), VARIANT SER-213.
      Tissue: Testis.
    6. "The forkhead-associated domain protein Cep170 interacts with Polo-like kinase 1 and serves as a marker for mature centrioles."
      Guarguaglini G., Duncan P.I., Stierhof Y.D., Holmstroem T., Duensing S., Nigg E.A.
      Mol. Biol. Cell 16:1095-1107(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH PLK1, SUBCELLULAR LOCATION, PHOSPHORYLATION.
    7. "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-356; SER-359 AND SER-933, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    8. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
      Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
      Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-636, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-633 AND SER-636, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic kidney.
    10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-356; SER-359; THR-501; SER-633; SER-636; SER-838; SER-930; SER-958; SER-1112; SER-1165 AND SER-1251, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    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. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1112 AND SER-1160, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    14. "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-356; SER-359; TYR-364; SER-1112 AND SER-1114, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    15. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    16. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-356; SER-359; SER-446; SER-497 AND SER-838, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    17. "Crystal structure of a centrosomal protein 170kDA, transcript variant beta (CEP170) from Homo sapiens at 2.15 A resolution (PSI community target, Sundstrom)."
      Joint center for structural genomics (JCSG)
      Submitted (APR-2013) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 1-126.

    Entry informationi

    Entry nameiCE170_HUMAN
    AccessioniPrimary (citable) accession number: Q5SW79
    Secondary accession number(s): O75058
    , Q5SW77, Q5SW78, Q7LGA9, Q86W31, Q9UQ08, Q9UQ09
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 3, 2007
    Last sequence update: December 21, 2004
    Last modified: October 1, 2014
    This is version 95 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. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3