Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q53EZ4 (CEP55_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 95. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Centrosomal protein of 55 kDa

Short name=Cep55
Alternative name(s):
Up-regulated in colon cancer 6
Gene names
Name:CEP55
Synonyms:C10orf3, URCC6
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length464 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Plays a role in mitotic exit and cytokinesis. Not required for microtubule nucleation. Recruits PDCD6IP and TSG101 to midbody during cytokinesis. Ref.9 Ref.11

Subunit structure

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. Ref.1 Ref.9 Ref.11 Ref.12 Ref.18

Subcellular location

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. Ref.1 Ref.9 Ref.11 Ref.12

Tissue specificity

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. Ref.1 Ref.9

Post-translational modification

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. Ref.9

Sequence caution

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

Binary interactions

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q53EZ4-1)

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.
Isoform 2 (identifier: Q53EZ4-2)

The sequence of this isoform differs from the canonical sequence as follows:
     389-400: NQITQLESLKQL → KNNTVGILETAS
     401-464: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 464464Centrosomal protein of 55 kDa
PRO_0000089777

Regions

Region157 – 23680Interaction with TSG101
Region160 – 21455Interaction with PDCD6IP
Region355 – 464110Required for localization to the interphase centrosome and to the midbody during cytokinesis
Coiled coil22 – 186165 Potential
Coiled coil238 – 337100 Potential
Coiled coil374 – 40330 Potential

Amino acid modifications

Modified residue4251Phosphoserine; by CDK1 and MAPK1 Ref.9 Ref.10 Ref.13 Ref.14
Modified residue4281Phosphoserine; by CDK1 and MAPK1 Ref.9 Ref.14
Modified residue4301Phosphothreonine Ref.14
Modified residue4361Phosphoserine; by PLK1 Ref.9 Ref.14

Natural variations

Alternative sequence389 – 40012NQITQ…SLKQL → KNNTVGILETAS in isoform 2.
VSP_014750
Alternative sequence401 – 46464Missing in isoform 2.
VSP_014751
Natural variant571H → Q. Ref.1 Ref.3
Corresponds to variant rs3740370 [ dbSNP | Ensembl ].
VAR_026559
Natural variant991T → A. Ref.1 Ref.2 Ref.3 Ref.4 Ref.5 Ref.7 Ref.8 Ref.19 Ref.20
Corresponds to variant rs7080916 [ dbSNP | Ensembl ].
VAR_022996
Natural variant2361C → R.
Corresponds to variant rs7072484 [ dbSNP | Ensembl ].
VAR_056791
Natural variant3781H → L. Ref.3 Ref.4 Ref.7 Ref.8
Corresponds to variant rs2293277 [ dbSNP | Ensembl ].
VAR_022997

Experimental info

Mutagenesis1841W → A: Abolishes interaction with PDCD6IP. Ref.18
Mutagenesis1871Y → A: Abolishes interaction with PDCD6IP. Ref.18
Mutagenesis1881D → A: Diminishes interaction with PDCD6IP. Ref.18
Mutagenesis1911R → A: Abolishes interaction with PDCD6IP. Ref.18
Mutagenesis1921E → A: Abolishes interaction with PDCD6IP. Ref.18
Mutagenesis3961S → A: No effect on phosphorylation in mitotic cells. Ref.9
Mutagenesis4251S → 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. Ref.9
Mutagenesis4281S → 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. Ref.9
Mutagenesis4361S → A: No effect on phosphorylation in mitotic cells. Arrests mitotic cells at the midbody stage; when associated with A-425 and A-428. Ref.9
Sequence conflict1551V → A in BAD97215. Ref.4
Sequence conflict2041E → G in BAD97215. Ref.4
Sequence conflict2981R → G in CAE45837. Ref.5
Sequence conflict3341F → S in AAX14687. Ref.1
Sequence conflict3341F → S in BAA91670. Ref.3
Sequence conflict4351E → G in AAX14687. Ref.1

Secondary structure

... 464
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified May 18, 2010. Version 3.
Checksum: A652F86EBCE46A51

FASTA46454,178
        10         20         30         40         50         60 
MSSRSTKDLI KSKWGSKPSN SKSETTLEKL KGEIAHLKTS VDEITSGKGK LTDKERHRLL 

        70         80         90        100        110        120 
EKIRVLEAEK EKNAYQLTEK DKEIQRLRDQ LKARYSTTTL LEQLEETTRE GERREQVLKA 

       130        140        150        160        170        180 
LSEEKDVLKQ QLSAATSRIA ELESKTNTLR LSQTVAPNCF NSSINNIHEM EIQLKDALEK 

       190        200        210        220        230        240 
NQQWLVYDQQ REVYVKGLLA KIFELEKKTE TAAHSLPQQT KKPESEGYLQ EEKQKCYNDL 

       250        260        270        280        290        300 
LASAKKDLEV ERQTITQLSF ELSEFRRKYE ETQKEVHNLN QLLYSQRRAD VQHLEDDRHK 

       310        320        330        340        350        360 
TEKIQKLREE NDIARGKLEE EKKRSEELLS QVQFLYTSLL KQQEEQTRVA LLEQQMQACT 

       370        380        390        400        410        420 
LDFENEKLDR QHVQHQLHVI LKELRKARNQ ITQLESLKQL HEFAITEPLV TFQGETENRE 

       430        440        450        460 
KVAASPKSPT AALNESLVEC PKCNIQYPAT EHRDLLVHVE YCSK 

« Hide

Isoform 2 [UniParc].

Checksum: 61FCFE0A0965559F
Show »

FASTA40046,857

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
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]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT 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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] ALA-99, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS7428.1. [Q53EZ4-1]
RefSeqNP_001120654.1. NM_001127182.1.
NP_060601.3. NM_018131.4.
UniGeneHs.14559.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3E1RX-ray2.00A/B160-217[»]
ProteinModelPortalQ53EZ4.
SMRQ53EZ4. Positions 165-210.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid120465. 22 interactions.
DIPDIP-44581N.
IntActQ53EZ4. 18 interactions.
MINTMINT-4994059.
STRING9606.ENSP00000360540.

PTM databases

PhosphoSiteQ53EZ4.

Polymorphism databases

DMDM296439403.

Proteomic databases

MaxQBQ53EZ4.
PaxDbQ53EZ4.
PRIDEQ53EZ4.

Protocols and materials databases

DNASU55165.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000371485; ENSP00000360540; ENSG00000138180. [Q53EZ4-1]
GeneID55165.
KEGGhsa:55165.
UCSCuc001kiq.4. human. [Q53EZ4-1]

Organism-specific databases

CTD55165.
GeneCardsGC10P095247.
HGNCHGNC:1161. CEP55.
HPAHPA023430.
MIM610000. gene.
neXtProtNX_Q53EZ4.
PharmGKBPA25475.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG135886.
HOVERGENHBG081092.
InParanoidQ53EZ4.
KOK16456.
OMASQVQFLY.
OrthoDBEOG7H4DTJ.
PhylomeDBQ53EZ4.
TreeFamTF331107.

Gene expression databases

BgeeQ53EZ4.
CleanExHS_CEP55.
GenevestigatorQ53EZ4.

Family and domain databases

InterProIPR022008. EABR.
[Graphical view]
PfamPF12180. EABR. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ53EZ4.
GeneWikiCEP55.
GenomeRNAi55165.
NextBio58933.
PROQ53EZ4.
SOURCESearch...

Entry information

Entry nameCEP55_HUMAN
AccessionPrimary (citable) accession number: Q53EZ4
Secondary accession number(s): B2RDG8 expand/collapse secondary AC list , Q32WF5, Q3MV20, Q5VY28, Q6N034, Q96H32, Q9NVS7
Entry history
Integrated into UniProtKB/Swiss-Prot: July 19, 2005
Last sequence update: May 18, 2010
Last modified: July 9, 2014
This is version 95 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 10

Human chromosome 10: entries, gene names and cross-references to MIM