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Q53EZ4

- CEP55_HUMAN

UniProt

Q53EZ4 - CEP55_HUMAN

Protein

Centrosomal protein of 55 kDa

Gene

CEP55

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 97 (01 Oct 2014)
      Sequence version 3 (18 May 2010)
      Previous versions | rss
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    Functioni

    Plays a role in mitotic exit and cytokinesis. Not required for microtubule nucleation. Recruits PDCD6IP and TSG101 to midbody during cytokinesis.2 Publications

    GO - Molecular functioni

    1. protein binding Source: IntAct

    GO - Biological processi

    1. establishment of protein localization Source: UniProt
    2. mitotic cytokinesis Source: MGI
    3. mitotic nuclear division Source: UniProtKB-KW

    Keywords - Biological processi

    Cell cycle, Cell division, Mitosis

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Centrosomal protein of 55 kDa
    Short name:
    Cep55
    Alternative name(s):
    Up-regulated in colon cancer 6
    Gene namesi
    Name:CEP55
    Synonyms:C10orf3, URCC6
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 10

    Organism-specific databases

    HGNCiHGNC:1161. CEP55.

    Subcellular locationi

    Cytoplasmcytoskeletonmicrotubule organizing centercentrosomecentriole. Cytoplasmcytoskeletonmicrotubule organizing centercentrosome. Cleavage furrow. Midbody
    Note: Present at the centrosomes at interphase. A small portion is associated preferentially with the mother centriole, whereas the majority localizes to the pericentriolar material. During mitosis, loss of affinity for the centrosome at the onset of prophase and diffusion throughout the cell. This dissociation from the centrosome is phosphorylation-dependent. May remain localized at the centrosome during mitosis in certain cell types. Appears at the cleavage furrow in late anaphase and in the midbody in cytokinesis.

    GO - Cellular componenti

    1. centriole Source: UniProtKB-SubCell
    2. centrosome Source: UniProtKB
    3. cleavage furrow Source: UniProtKB-SubCell
    4. intercellular bridge Source: Ensembl
    5. membrane Source: UniProtKB
    6. midbody Source: MGI

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi184 – 1841W → A: Abolishes interaction with PDCD6IP. 1 Publication
    Mutagenesisi187 – 1871Y → A: Abolishes interaction with PDCD6IP. 1 Publication
    Mutagenesisi188 – 1881D → A: Diminishes interaction with PDCD6IP. 1 Publication
    Mutagenesisi191 – 1911R → A: Abolishes interaction with PDCD6IP. 1 Publication
    Mutagenesisi192 – 1921E → A: Abolishes interaction with PDCD6IP. 1 Publication
    Mutagenesisi396 – 3961S → A: No effect on phosphorylation in mitotic cells. 1 Publication
    Mutagenesisi425 – 4251S → A: Partial loss of phosphorylation in mitotic cells. Complete loss of phosphorylation in mitotic cells; when associated with A-428. Remains associated with the centrosome throughout mitosis; when associated with A-428. Arrests mitotic cells at the midbody stage; when associated with A-428 and A-436. 1 Publication
    Mutagenesisi428 – 4281S → A: Partial loss of phosphorylation in mitotic cells. Complete loss of phosphorylation in mitotic cells; when associated with A-425. Remains associated with the centrosome throughout mitosis; when associated with A-425. Arrests mitotic cells at the midbody stage; when associated with A-425 and A-436. 1 Publication
    Mutagenesisi436 – 4361S → A: No effect on phosphorylation in mitotic cells. Arrests mitotic cells at the midbody stage; when associated with A-425 and A-428. 1 Publication

    Organism-specific databases

    PharmGKBiPA25475.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 464464Centrosomal protein of 55 kDaPRO_0000089777Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei425 – 4251Phosphoserine; by CDK1 and MAPK14 Publications
    Modified residuei428 – 4281Phosphoserine; by CDK1 and MAPK12 Publications
    Modified residuei430 – 4301Phosphothreonine1 Publication
    Modified residuei436 – 4361Phosphoserine; by PLK12 Publications

    Post-translational modificationi

    There is a hierachy of phosphorylation, where both Ser-425 and Ser-428 are phosphorylated at the onset of mitosis, prior to Ser-436. Phosphorylation at Ser-425 and Ser-428 is required for dissociation from the centrosome at the G2/M boundary. Phosphorylation at the 3 sites, Ser-425, Ser-428 and Ser-436, is required for protein function at the final stages of cell division to complete cytokinesis successfully.4 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ53EZ4.
    PaxDbiQ53EZ4.
    PRIDEiQ53EZ4.

    PTM databases

    PhosphoSiteiQ53EZ4.

    Expressioni

    Tissue specificityi

    Widely expressed, mostly in proliferative tissues. Highly expressed in testis. Intermediate levels in adult and fetal thymus, as well as in various cancer cell lines. Low levels in different parts of the digestive tract, bone marrow, lymph nodes, placenta, fetal heart and fetal spleen. Hardly detected in brain.2 Publications

    Gene expression databases

    BgeeiQ53EZ4.
    CleanExiHS_CEP55.
    GenevestigatoriQ53EZ4.

    Organism-specific databases

    HPAiHPA023430.

    Interactioni

    Subunit structurei

    Homodimer. Interacts (phosphorylated on Ser-425 and Ser-428) with PLK1. Interacts with AKAP9; the interaction occurs in interphase and is lost upon mitotic entry. Interacts with PCNT; the interaction occurs in interphase and is lost upon mitotic entry. Interacts with PDCD6IP; the interaction is direct; CEP55 binds PDCD6IP in a 2:1 stoechiometry; PDCD6IP competes with TSG101 for the same binding site. Interacts with TSG101; TSG101 competes with PDCD6IP for the same binding site; interaction is required for cytokinesis but not for viral budding. Interacts with MVB12A, VPS37B, VPS37C and VPS28.4 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    PDCD6IPQ8WUM49EBI-747776,EBI-7603917
    TEX14Q8IWB63EBI-747776,EBI-6674697
    TSG101Q9981612EBI-747776,EBI-346882

    Protein-protein interaction databases

    BioGridi120465. 22 interactions.
    DIPiDIP-44581N.
    IntActiQ53EZ4. 18 interactions.
    MINTiMINT-4994059.
    STRINGi9606.ENSP00000360540.

    Structurei

    Secondary structure

    1
    464
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi166 – 20944

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3E1RX-ray2.00A/B160-217[»]
    ProteinModelPortaliQ53EZ4.
    SMRiQ53EZ4. Positions 165-210.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ53EZ4.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni157 – 23680Interaction with TSG101Add
    BLAST
    Regioni160 – 21455Interaction with PDCD6IPAdd
    BLAST
    Regioni355 – 464110Required for localization to the interphase centrosome and to the midbody during cytokinesisAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili22 – 186165Sequence AnalysisAdd
    BLAST
    Coiled coili238 – 337100Sequence AnalysisAdd
    BLAST
    Coiled coili374 – 40330Sequence AnalysisAdd
    BLAST

    Keywords - Domaini

    Coiled coil

    Phylogenomic databases

    eggNOGiNOG135886.
    HOVERGENiHBG081092.
    InParanoidiQ53EZ4.
    KOiK16456.
    OMAiSQVQFLY.
    OrthoDBiEOG7H4DTJ.
    PhylomeDBiQ53EZ4.
    TreeFamiTF331107.

    Family and domain databases

    InterProiIPR022008. EABR.
    [Graphical view]
    PfamiPF12180. EABR. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q53EZ4-1) [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

    MSSRSTKDLI KSKWGSKPSN SKSETTLEKL KGEIAHLKTS VDEITSGKGK    50
    LTDKERHRLL EKIRVLEAEK EKNAYQLTEK DKEIQRLRDQ LKARYSTTTL 100
    LEQLEETTRE GERREQVLKA LSEEKDVLKQ QLSAATSRIA ELESKTNTLR 150
    LSQTVAPNCF NSSINNIHEM EIQLKDALEK NQQWLVYDQQ REVYVKGLLA 200
    KIFELEKKTE TAAHSLPQQT KKPESEGYLQ EEKQKCYNDL LASAKKDLEV 250
    ERQTITQLSF ELSEFRRKYE ETQKEVHNLN QLLYSQRRAD VQHLEDDRHK 300
    TEKIQKLREE NDIARGKLEE EKKRSEELLS QVQFLYTSLL KQQEEQTRVA 350
    LLEQQMQACT LDFENEKLDR QHVQHQLHVI LKELRKARNQ ITQLESLKQL 400
    HEFAITEPLV TFQGETENRE KVAASPKSPT AALNESLVEC PKCNIQYPAT 450
    EHRDLLVHVE YCSK 464
    Length:464
    Mass (Da):54,178
    Last modified:May 18, 2010 - v3
    Checksum:iA652F86EBCE46A51
    GO
    Isoform 2 (identifier: Q53EZ4-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         389-400: NQITQLESLKQL → KNNTVGILETAS
         401-464: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:400
    Mass (Da):46,857
    Checksum:i61FCFE0A0965559F
    GO

    Sequence cautioni

    The sequence BAA91670.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti155 – 1551V → A in BAD97215. 1 PublicationCurated
    Sequence conflicti204 – 2041E → G in BAD97215. 1 PublicationCurated
    Sequence conflicti298 – 2981R → G in CAE45837. (PubMed:17974005)Curated
    Sequence conflicti334 – 3341F → S in AAX14687. (PubMed:16406728)Curated
    Sequence conflicti334 – 3341F → S in BAA91670. (PubMed:14702039)Curated
    Sequence conflicti435 – 4351E → G in AAX14687. (PubMed:16406728)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti57 – 571H → Q.2 Publications
    Corresponds to variant rs3740370 [ dbSNP | Ensembl ].
    VAR_026559
    Natural varianti99 – 991T → A.9 Publications
    Corresponds to variant rs7080916 [ dbSNP | Ensembl ].
    VAR_022996
    Natural varianti236 – 2361C → R.
    Corresponds to variant rs7072484 [ dbSNP | Ensembl ].
    VAR_056791
    Natural varianti378 – 3781H → L.4 Publications
    Corresponds to variant rs2293277 [ dbSNP | Ensembl ].
    VAR_022997

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei389 – 40012NQITQ…SLKQL → KNNTVGILETAS in isoform 2. 1 PublicationVSP_014750Add
    BLAST
    Alternative sequencei401 – 46464Missing in isoform 2. 1 PublicationVSP_014751Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY788918 mRNA. Translation: AAX14687.1.
    AB091343 mRNA. Translation: BAE45243.1.
    AK001402 mRNA. Translation: BAA91670.1. Different initiation.
    AK315536 mRNA. Translation: BAG37915.1.
    AK223495 mRNA. Translation: BAD97215.1.
    BX640718 mRNA. Translation: CAE45837.1.
    AL356214 Genomic DNA. Translation: CAH72324.1.
    CH471066 Genomic DNA. Translation: EAW50071.1.
    BC008947 mRNA. Translation: AAH08947.1.
    CCDSiCCDS7428.1. [Q53EZ4-1]
    RefSeqiNP_001120654.1. NM_001127182.1.
    NP_060601.3. NM_018131.4.
    UniGeneiHs.14559.

    Genome annotation databases

    EnsembliENST00000371485; ENSP00000360540; ENSG00000138180. [Q53EZ4-1]
    GeneIDi55165.
    KEGGihsa:55165.
    UCSCiuc001kiq.4. human. [Q53EZ4-1]

    Polymorphism databases

    DMDMi296439403.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY788918 mRNA. Translation: AAX14687.1 .
    AB091343 mRNA. Translation: BAE45243.1 .
    AK001402 mRNA. Translation: BAA91670.1 . Different initiation.
    AK315536 mRNA. Translation: BAG37915.1 .
    AK223495 mRNA. Translation: BAD97215.1 .
    BX640718 mRNA. Translation: CAE45837.1 .
    AL356214 Genomic DNA. Translation: CAH72324.1 .
    CH471066 Genomic DNA. Translation: EAW50071.1 .
    BC008947 mRNA. Translation: AAH08947.1 .
    CCDSi CCDS7428.1. [Q53EZ4-1 ]
    RefSeqi NP_001120654.1. NM_001127182.1.
    NP_060601.3. NM_018131.4.
    UniGenei Hs.14559.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3E1R X-ray 2.00 A/B 160-217 [» ]
    ProteinModelPortali Q53EZ4.
    SMRi Q53EZ4. Positions 165-210.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 120465. 22 interactions.
    DIPi DIP-44581N.
    IntActi Q53EZ4. 18 interactions.
    MINTi MINT-4994059.
    STRINGi 9606.ENSP00000360540.

    PTM databases

    PhosphoSitei Q53EZ4.

    Polymorphism databases

    DMDMi 296439403.

    Proteomic databases

    MaxQBi Q53EZ4.
    PaxDbi Q53EZ4.
    PRIDEi Q53EZ4.

    Protocols and materials databases

    DNASUi 55165.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000371485 ; ENSP00000360540 ; ENSG00000138180 . [Q53EZ4-1 ]
    GeneIDi 55165.
    KEGGi hsa:55165.
    UCSCi uc001kiq.4. human. [Q53EZ4-1 ]

    Organism-specific databases

    CTDi 55165.
    GeneCardsi GC10P095247.
    HGNCi HGNC:1161. CEP55.
    HPAi HPA023430.
    MIMi 610000. gene.
    neXtProti NX_Q53EZ4.
    PharmGKBi PA25475.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG135886.
    HOVERGENi HBG081092.
    InParanoidi Q53EZ4.
    KOi K16456.
    OMAi SQVQFLY.
    OrthoDBi EOG7H4DTJ.
    PhylomeDBi Q53EZ4.
    TreeFami TF331107.

    Miscellaneous databases

    EvolutionaryTracei Q53EZ4.
    GeneWikii CEP55.
    GenomeRNAii 55165.
    NextBioi 58933.
    PROi Q53EZ4.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q53EZ4.
    CleanExi HS_CEP55.
    Genevestigatori Q53EZ4.

    Family and domain databases

    InterProi IPR022008. EABR.
    [Graphical view ]
    Pfami PF12180. EABR. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The novel centrosomal associated protein CEP55 is present in the spindle midzone and the midbody."
      Martinez-Garay I., Rustom A., Gerdes H.-H., Kutsche K.
      Genomics 87:243-253(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, TISSUE SPECIFICITY, HOMODIMERIZATION, VARIANTS GLN-57 AND ALA-99.
    2. "Cloning and characterization of URCC6, a novel gene up-regulated in colon cancer."
      Shimokawa T., Furukawa Y., Sakai M., Nakamura Y.
      Submitted (SEP-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT ALA-99.
    3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 33-464 (ISOFORM 2), VARIANTS GLN-57; ALA-99 AND LEU-378.
    4. Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
      Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANTS ALA-99 AND LEU-378.
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT ALA-99.
      Tissue: Esophageal carcinoma.
    6. "The DNA sequence and comparative analysis of human chromosome 10."
      Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J.
      , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
      Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANTS ALA-99 AND LEU-378.
    8. "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 1), VARIANTS ALA-99 AND LEU-378.
      Tissue: Muscle.
    9. "Cdk1/Erk2- and Plk1-dependent phosphorylation of a centrosome protein, Cep55, is required for its recruitment to midbody and cytokinesis."
      Fabbro M., Zhou B.-B., Takahashi M., Sarcevic B., Lal P., Graham M.E., Gabrielli B.G., Robinson P.J., Nigg E.A., Ono Y., Khanna K.K.
      Dev. Cell 9:477-488(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INTERACTION WITH PLK1; AKAP9 AND PCNT, PHOSPHORYLATION AT SER-425; SER-428 AND SER-436, MUTAGENESIS OF SER-396; SER-425; SER-428 AND SER-436, IDENTIFICATION BY MASS SPECTROMETRY.
    10. "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-425, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. "Human ESCRT and ALIX proteins interact with proteins of the midbody and function in cytokinesis."
      Morita E., Sandrin V., Chung H.Y., Morham S.G., Gygi S.P., Rodesch C.K., Sundquist W.I.
      EMBO J. 26:4215-4227(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, SELF-ASSOCIATION, INTERACTION WITH PDCD6IP; TSG101; MVB12A; VPS37B; VPS37C AND VPS28.
    12. "Parallels between cytokinesis and retroviral budding: a role for the ESCRT machinery."
      Carlton J.G., Martin-Serrano J.
      Science 316:1908-1912(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: SELF-ASSOCIATION, INTERACTION WITH PDCD6IP AND TSG101, SUBCELLULAR LOCATION.
    13. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
      Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
      Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-425, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    14. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-425; SER-428; THR-430 AND SER-436, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    15. "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].
    16. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    17. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    18. "Midbody targeting of the ESCRT machinery by a noncanonical coiled coil in CEP55."
      Lee H.H., Elia N., Ghirlando R., Lippincott-Schwartz J., Hurley J.H.
      Science 322:576-580(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 160-217 IN COMPLEX WITH PDCD6IP, INTERACTION WITH TSG101, MUTAGENESIS OF TRP-184; TYR-187; ASP-188; ARG-191 AND GLU-192.
    19. "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: VARIANT [LARGE SCALE ANALYSIS] ALA-99, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    20. Cited for: VARIANT [LARGE SCALE ANALYSIS] ALA-99, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiCEP55_HUMAN
    AccessioniPrimary (citable) accession number: Q53EZ4
    Secondary accession number(s): B2RDG8
    , Q32WF5, Q3MV20, Q5VY28, Q6N034, Q96H32, Q9NVS7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 19, 2005
    Last sequence update: May 18, 2010
    Last modified: October 1, 2014
    This is version 97 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

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 10
      Human chromosome 10: 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

    External Data

    Dasty 3