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Protein

Centrosomal protein of 55 kDa

Gene

CEP55

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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 - Biological processi

  • cell separation after cytokinesis Source: UniProtKB
  • establishment of protein localization Source: UniProtKB
  • mitotic cytokinesis Source: MGI
  • mitotic nuclear division Source: UniProtKB-KW
Complete GO annotation...

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 Componenti: Chromosome 10

Organism-specific databases

HGNCiHGNC:1161. CEP55.

Subcellular locationi

GO - Cellular componenti

  • centriole Source: UniProtKB-SubCell
  • centrosome Source: UniProtKB
  • cleavage furrow Source: UniProtKB-SubCell
  • intercellular bridge Source: Ensembl
  • membrane Source: UniProtKB
  • midbody Source: MGI
Complete GO annotation...

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.

Polymorphism and mutation databases

BioMutaiCEP55.
DMDMi296439403.

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.1 Publication

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.
ExpressionAtlasiQ53EZ4. baseline and differential.
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-310624
TEX14Q8IWB63EBI-747776,EBI-6674697
TSG101Q9981612EBI-747776,EBI-346882

Protein-protein interaction databases

BioGridi120465. 68 interactions.
DIPiDIP-44581N.
IntActiQ53EZ4. 19 interactions.
MINTiMINT-4994059.
STRINGi9606.ENSP00000360540.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
GeneTreeiENSGT00510000047961.
HOVERGENiHBG081092.
InParanoidiQ53EZ4.
KOiK16456.
OMAiKQLHEFA.
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. AlignAdd to basket

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

        10         20         30         40         50
MSSRSTKDLI KSKWGSKPSN SKSETTLEKL KGEIAHLKTS VDEITSGKGK
60 70 80 90 100
LTDKERHRLL EKIRVLEAEK EKNAYQLTEK DKEIQRLRDQ LKARYSTTTL
110 120 130 140 150
LEQLEETTRE GERREQVLKA LSEEKDVLKQ QLSAATSRIA ELESKTNTLR
160 170 180 190 200
LSQTVAPNCF NSSINNIHEM EIQLKDALEK NQQWLVYDQQ REVYVKGLLA
210 220 230 240 250
KIFELEKKTE TAAHSLPQQT KKPESEGYLQ EEKQKCYNDL LASAKKDLEV
260 270 280 290 300
ERQTITQLSF ELSEFRRKYE ETQKEVHNLN QLLYSQRRAD VQHLEDDRHK
310 320 330 340 350
TEKIQKLREE NDIARGKLEE EKKRSEELLS QVQFLYTSLL KQQEEQTRVA
360 370 380 390 400
LLEQQMQACT LDFENEKLDR QHVQHQLHVI LKELRKARNQ ITQLESLKQL
410 420 430 440 450
HEFAITEPLV TFQGETENRE KVAASPKSPT AALNESLVEC PKCNIQYPAT
460
EHRDLLVHVE YCSK
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.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti155 – 1551V → A in BAD97215 (Ref. 4) Curated
Sequence conflicti204 – 2041E → G in BAD97215 (Ref. 4) Curated
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:
EMBLi
GenBanki
DDBJi
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]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

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

Protein-protein interaction databases

BioGridi120465. 68 interactions.
DIPiDIP-44581N.
IntActiQ53EZ4. 19 interactions.
MINTiMINT-4994059.
STRINGi9606.ENSP00000360540.

PTM databases

PhosphoSiteiQ53EZ4.

Polymorphism and mutation databases

BioMutaiCEP55.
DMDMi296439403.

Proteomic databases

MaxQBiQ53EZ4.
PaxDbiQ53EZ4.
PRIDEiQ53EZ4.

Protocols and materials databases

DNASUi55165.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi55165.
GeneCardsiGC10P095247.
HGNCiHGNC:1161. CEP55.
HPAiHPA023430.
MIMi610000. gene.
neXtProtiNX_Q53EZ4.
PharmGKBiPA25475.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG135886.
GeneTreeiENSGT00510000047961.
HOVERGENiHBG081092.
InParanoidiQ53EZ4.
KOiK16456.
OMAiKQLHEFA.
OrthoDBiEOG7H4DTJ.
PhylomeDBiQ53EZ4.
TreeFamiTF331107.

Miscellaneous databases

EvolutionaryTraceiQ53EZ4.
GeneWikiiCEP55.
GenomeRNAii55165.
NextBioi58933.
PROiQ53EZ4.
SOURCEiSearch...

Gene expression databases

BgeeiQ53EZ4.
CleanExiHS_CEP55.
ExpressionAtlasiQ53EZ4. baseline and differential.
GenevestigatoriQ53EZ4.

Family and domain databases

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

Publicationsi

« Hide 'large scale' publications
  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: May 27, 2015
This is version 105 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.