Q53EZ4 (CEP55_HUMAN) Reviewed, UniProtKB/Swiss-Prot
Last modified
April 3, 2013.
Version 85.
History...
Names·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Centrosomal protein of 55 kDa Short name=Cep55 Alternative name(s): Up-regulated in colon cancer 6 | ||||
| Gene names |
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| Organism | Homo sapiens (Human) [Reference proteome] | ||||
| Taxonomic identifier | 9606 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo![]() |
Protein attributes
| Sequence length | 464 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence 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.17 |
| Subcellular location | Cytoplasm › cytoskeleton › centrosome › centriole. Cytoplasm › cytoskeleton › centrosome. 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. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Cell cycle Cell division Mitosis |
| Cellular component | Cytoplasm Cytoskeleton |
| Coding sequence diversity | Alternative splicing Polymorphism |
| Domain | Coiled coil |
| PTM | Phosphoprotein |
| Technical term | 3D-structure Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Biological_process | cytokinesis Inferred from genetic interaction PubMed 19638580. Source: MGI mitosisInferred from electronic annotation. Source: UniProtKB-KW |
| Cellular_component | centriole Inferred from electronic annotation. Source: UniProtKB-SubCell centrosomeInferred from direct assay PubMed 21399614. Source: UniProtKB cleavage furrowInferred from electronic annotation. Source: UniProtKB-SubCell intercellular bridgeInferred from electronic annotation. Source: Compara midbodyInferred from direct assay PubMed 20186884. Source: MGI |
| Complete GO annotation... | |
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 key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||
Molecule processing | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 464 | 464 | Centrosomal protein of 55 kDa | PRO_0000089777 | |||||||
Regions | |||||||||||
| Region | 157 – 236 | 80 | Interaction with TSG101 | ||||||||
| Region | 160 – 214 | 55 | Interaction with PDCD6IP | ||||||||
| Region | 355 – 464 | 110 | Required for localization to the interphase centrosome and to the midbody during cytokinesis | ||||||||
| Coiled coil | 22 – 186 | 165 | Potential | ||||||||
| Coiled coil | 238 – 337 | 100 | Potential | ||||||||
| Coiled coil | 374 – 403 | 30 | Potential | ||||||||
Amino acid modifications | |||||||||||
| Modified residue | 425 | 1 | Phosphoserine; by CDK1 and MAPK1 Ref.9 Ref.10 Ref.13 Ref.14 | ||||||||
| Modified residue | 428 | 1 | Phosphoserine; by CDK1 and MAPK1 Ref.9 Ref.14 | ||||||||
| Modified residue | 430 | 1 | Phosphothreonine Ref.14 | ||||||||
| Modified residue | 436 | 1 | Phosphoserine; by PLK1 Ref.9 Ref.14 | ||||||||
Natural variations | |||||||||||
| Alternative sequence | 389 – 400 | 12 | NQITQ…SLKQL → KNNTVGILETAS in isoform 2. | VSP_014750 | |||||||
| Alternative sequence | 401 – 464 | 64 | Missing in isoform 2. | VSP_014751 | |||||||
| Natural variant | 57 | 1 | H → Q. Ref.1 Ref.3 Corresponds to variant rs3740370 [ dbSNP | Ensembl ]. | VAR_026559 | |||||||
| Natural variant | 99 | 1 | T → A. Ref.1 Ref.2 Ref.3 Ref.4 Ref.5 Ref.7 Ref.8 Ref.18 Ref.19 Corresponds to variant rs7080916 [ dbSNP | Ensembl ]. | VAR_022996 | |||||||
| Natural variant | 236 | 1 | C → R. Corresponds to variant rs7072484 [ dbSNP | Ensembl ]. | VAR_056791 | |||||||
| Natural variant | 378 | 1 | H → L. Ref.3 Ref.4 Ref.7 Ref.8 Corresponds to variant rs2293277 [ dbSNP | Ensembl ]. | VAR_022997 | |||||||
Experimental info | |||||||||||
| Mutagenesis | 184 | 1 | W → A: Abolishes interaction with PDCD6IP. Ref.17 | ||||||||
| Mutagenesis | 187 | 1 | Y → A: Abolishes interaction with PDCD6IP. Ref.17 | ||||||||
| Mutagenesis | 188 | 1 | D → A: Diminishes interaction with PDCD6IP. Ref.17 | ||||||||
| Mutagenesis | 191 | 1 | R → A: Abolishes interaction with PDCD6IP. Ref.17 | ||||||||
| Mutagenesis | 192 | 1 | E → A: Abolishes interaction with PDCD6IP. Ref.17 | ||||||||
| Mutagenesis | 396 | 1 | S → A: No effect on phosphorylation in mitotic cells. Ref.9 | ||||||||
| Mutagenesis | 425 | 1 | S → 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 | ||||||||
| Mutagenesis | 428 | 1 | S → 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 | ||||||||
| Mutagenesis | 436 | 1 | S → 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 conflict | 155 | 1 | V → A in BAD97215. Ref.4 | ||||||||
| Sequence conflict | 204 | 1 | E → G in BAD97215. Ref.4 | ||||||||
| Sequence conflict | 298 | 1 | R → G in CAE45837. Ref.5 | ||||||||
| Sequence conflict | 334 | 1 | F → S in AAX14687. Ref.1 | ||||||||
| Sequence conflict | 334 | 1 | F → S in BAA91670. Ref.3 | ||||||||
| Sequence conflict | 435 | 1 | E → G in AAX14687. Ref.1 | ||||||||
Secondary structure | |||||||||||
Helix Strand Turn | |||||||||||
| Helix | 166 – 209 | 44 | |||||||||
Sequences
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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. 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. 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. 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, 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. Tissue: Cervix carcinoma. |
| [15] | "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. |
| [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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. |
| [17] | "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. |
| [18] | "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, MASS SPECTROMETRY. Tissue: Leukemic T-cell. |
| [19] | "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, MASS SPECTROMETRY. |
| + | 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. | ||||||||||||
| IPI | IPI00101532. IPI00478943. | ||||||||||||
| RefSeq | NP_001120654.1. NM_001127182.1. NP_060601.3. NM_018131.4. | ||||||||||||
| UniGene | Hs.14559. | ||||||||||||
3D structure databases | |||||||||||||
| PDBe RCSB PDB PDBj |
| ||||||||||||
| ProteinModelPortal | Q53EZ4. | ||||||||||||
| SMR | Q53EZ4. Positions 165-210. | ||||||||||||
| ModBase | Search... | ||||||||||||
Protein-protein interaction databases | |||||||||||||
| DIP | DIP-44581N. | ||||||||||||
| IntAct | Q53EZ4. 7 interactions. | ||||||||||||
| MINT | MINT-4994059. | ||||||||||||
| STRING | 9606.ENSP00000360540. | ||||||||||||
PTM databases | |||||||||||||
| PhosphoSite | Q53EZ4. | ||||||||||||
Polymorphism databases | |||||||||||||
| DMDM | 296439403. | ||||||||||||
Proteomic databases | |||||||||||||
| PaxDb | Q53EZ4. | ||||||||||||
| PRIDE | Q53EZ4. | ||||||||||||
Protocols and materials databases | |||||||||||||
| DNASU | 55165. | ||||||||||||
| StructuralBiologyKnowledgebase | Search... | ||||||||||||
Genome annotation databases | |||||||||||||
| Ensembl | ENST00000371485; ENSP00000360540; ENSG00000138180. | ||||||||||||
| GeneID | 55165. | ||||||||||||
| KEGG | hsa:55165. | ||||||||||||
| UCSC | uc001kiq.4. human. | ||||||||||||
Organism-specific databases | |||||||||||||
| CTD | 55165. | ||||||||||||
| GeneCards | GC10P095247. | ||||||||||||
| HGNC | HGNC:1161. CEP55. | ||||||||||||
| HPA | HPA023430. | ||||||||||||
| MIM | 610000. gene. | ||||||||||||
| neXtProt | NX_Q53EZ4. | ||||||||||||
| PharmGKB | PA25475. | ||||||||||||
| GenAtlas | Search... | ||||||||||||
Phylogenomic databases | |||||||||||||
| eggNOG | NOG135886. | ||||||||||||
| HOVERGEN | HBG081092. | ||||||||||||
| InParanoid | Q53EZ4. | ||||||||||||
| KO | K16456. | ||||||||||||
| OMA | KQLHEFA. | ||||||||||||
| OrthoDB | EOG4FN4JB. | ||||||||||||
| PhylomeDB | Q53EZ4. | ||||||||||||
Gene expression databases | |||||||||||||
| ArrayExpress | Q53EZ4. | ||||||||||||
| Bgee | Q53EZ4. | ||||||||||||
| CleanEx | HS_CEP55. | ||||||||||||
| Genevestigator | Q53EZ4. | ||||||||||||
| GermOnline | ENSG00000138180. Homo sapiens. | ||||||||||||
Family and domain databases | |||||||||||||
| InterPro | IPR022008. EABR. [Graphical view] | ||||||||||||
| Pfam | PF12180. EABR. 1 hit. [Graphical view] | ||||||||||||
| ProtoNet | Search... | ||||||||||||
Other | |||||||||||||
| EvolutionaryTrace | Q53EZ4. | ||||||||||||
| GenomeRNAi | 55165. | ||||||||||||
| NextBio | 58933. | ||||||||||||
| SOURCE | Search... | ||||||||||||
Entry information
| Entry name | CEP55_HUMAN | ||||||||
| Accession | Primary (citable) accession number: Q53EZ4 Secondary accession number(s): B2RDG8 Q9NVS7 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
| Disclaimer | Any 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
| Human chromosome 10 Human chromosome 10: entries, gene names and cross-references to MIM |
| Human entries with polymorphisms or disease mutations List of human entries with polymorphisms or disease mutations |
| Human polymorphisms and disease mutations Index of human polymorphisms and disease mutations |
| MIM cross-references Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot |
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |

Clusters with
