Q6UX04 (CWC27_HUMAN) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 91.
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: Peptidyl-prolyl cis-trans isomerase CWC27 homolog Short name=PPIase CWC27 EC=5.2.1.8 Alternative name(s): Antigen NY-CO-10 Serologically defined colon cancer antigen 10 | ||||||
| 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 | 472 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | PPIases accelerate the folding of proteins By similarity. |
| Catalytic activity | Peptidylproline (omega=180) = peptidylproline (omega=0). |
| Sequence similarities | Belongs to the cyclophilin-type PPIase family. Contains 1 PPIase cyclophilin-type domain. |
| Sequence caution | The sequence AAC18041.1 differs from that shown. Reason: Frameshift at position 41. The sequence AAC18042.1 differs from that shown. Reason: Frameshift at position 136. The sequence AAH12117.1 differs from that shown. Reason: Erroneous initiation. |
Ontologies
| Keywords | |
|---|---|
| Coding sequence diversity | Alternative splicing Polymorphism |
| Domain | Coiled coil |
| Molecular function | Isomerase Rotamase |
| PTM | Glycoprotein Phosphoprotein |
| Technical term | 3D-structure Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Biological_process | mRNA splicing, via spliceosome Inferred by curator PubMed 11991638. Source: UniProtKB protein foldingInferred from electronic annotation. Source: UniProtKB-KW protein peptidyl-prolyl isomerizationInferred from electronic annotation. Source: GOC |
| Cellular_component | catalytic step 2 spliceosome Inferred from direct assay PubMed 11991638. Source: UniProtKB |
| Molecular_function | peptidyl-prolyl cis-trans isomerase activity Inferred from electronic annotation. Source: UniProtKB-KW |
| Complete GO annotation... | |
Alternative products
| This entry describes 2 isoforms produced by alternative splicing. [Align] [Select] | ||||||
| Isoform 1 (identifier: Q6UX04-1) 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: Q6UX04-2) The sequence of this isoform differs from the canonical sequence as follows: 385-391: TLALLNQ → DVTCTS 392-472: Missing. |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||||||||||||||||||||||||||||||
Molecule processing | |||||||||||||||||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 472 | 472 | Peptidyl-prolyl cis-trans isomerase CWC27 homolog | PRO_0000313647 | |||||||||||||||||||||||||||||||||||
Regions | |||||||||||||||||||||||||||||||||||||||
| Domain | 11 – 166 | 156 | PPIase cyclophilin-type | ||||||||||||||||||||||||||||||||||||
| Coiled coil | 206 – 230 | 25 | Potential | ||||||||||||||||||||||||||||||||||||
| Coiled coil | 306 – 377 | 72 | Potential | ||||||||||||||||||||||||||||||||||||
Amino acid modifications | |||||||||||||||||||||||||||||||||||||||
| Modified residue | 250 | 1 | Phosphoserine By similarity | ||||||||||||||||||||||||||||||||||||
| Glycosylation | 109 | 1 | N-linked (GlcNAc...) Potential | ||||||||||||||||||||||||||||||||||||
| Glycosylation | 201 | 1 | N-linked (GlcNAc...) Ref.5 | ||||||||||||||||||||||||||||||||||||
Natural variations | |||||||||||||||||||||||||||||||||||||||
| Alternative sequence | 385 – 391 | 7 | TLALLNQ → DVTCTS in isoform 2. | VSP_030082 | |||||||||||||||||||||||||||||||||||
| Alternative sequence | 392 – 472 | 81 | Missing in isoform 2. | VSP_030083 | |||||||||||||||||||||||||||||||||||
| Natural variant | 256 | 1 | P → A. Ref.1 Corresponds to variant rs7735338 [ dbSNP | Ensembl ]. | VAR_037686 | |||||||||||||||||||||||||||||||||||
Experimental info | |||||||||||||||||||||||||||||||||||||||
| Sequence conflict | 111 – 112 | 2 | SQ → TH in AAC18041. Ref.1 | ||||||||||||||||||||||||||||||||||||
| Sequence conflict | 331 | 1 | K → E in AAC18042. Ref.1 | ||||||||||||||||||||||||||||||||||||
Secondary structure | |||||||||||||||||||||||||||||||||||||||
Helix Strand Turn | |||||||||||||||||||||||||||||||||||||||
| Beta strand | 14 – 19 | 6 | |||||||||||||||||||||||||||||||||||||
| Beta strand | 22 – 29 | 8 | |||||||||||||||||||||||||||||||||||||
| Turn | 30 – 32 | 3 | |||||||||||||||||||||||||||||||||||||
| Helix | 34 – 45 | 12 | |||||||||||||||||||||||||||||||||||||
| Turn | 46 – 51 | 6 | |||||||||||||||||||||||||||||||||||||
| Beta strand | 56 – 58 | 3 | |||||||||||||||||||||||||||||||||||||
| Turn | 59 – 61 | 3 | |||||||||||||||||||||||||||||||||||||
| Beta strand | 62 – 65 | 4 | |||||||||||||||||||||||||||||||||||||
| Beta strand | 70 – 73 | 4 | |||||||||||||||||||||||||||||||||||||
| Beta strand | 95 – 101 | 7 | |||||||||||||||||||||||||||||||||||||
| Beta strand | 113 – 118 | 6 | |||||||||||||||||||||||||||||||||||||
| Helix | 121 – 123 | 3 | |||||||||||||||||||||||||||||||||||||
| Turn | 124 – 126 | 3 | |||||||||||||||||||||||||||||||||||||
| Beta strand | 129 – 133 | 5 | |||||||||||||||||||||||||||||||||||||
| Helix | 135 – 137 | 3 | |||||||||||||||||||||||||||||||||||||
| Helix | 138 – 143 | 6 | |||||||||||||||||||||||||||||||||||||
| Beta strand | 155 – 157 | 3 | |||||||||||||||||||||||||||||||||||||
| Beta strand | 160 – 168 | 9 | |||||||||||||||||||||||||||||||||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Characterization of human colon cancer antigens recognized by autologous antibodies." Scanlan M.J., Chen Y.-T., Williamson B., Gure A.O., Stockert E., Gordan J.D., Tuereci O., Sahin U., Pfreundschuh M., Old L.J. Int. J. Cancer 76:652-658(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT ALA-256. Tissue: Colon carcinoma. |
| [2] | "The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment." Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J., Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P., Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E. Gray A.M.Genome Res. 13:2265-2270(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). |
| [3] | 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]. |
| [4] | "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 2). Tissue: Uterus. |
| [5] | "Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry." Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D. J. Proteome Res. 4:2070-2080(2005) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-201, MASS SPECTROMETRY. Tissue: Plasma. |
| [6] | "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| EMBL GenBank DDBJ | AY358569 mRNA. Translation: AAQ88932.1. CH471137 Genomic DNA. Translation: EAW51365.1. AF039692 mRNA. Translation: AAC18041.1. Frameshift. AF039693 mRNA. Translation: AAC18042.1. Frameshift. BC012117 mRNA. Translation: AAH12117.1. Different initiation. | ||||||||||||
| IPI | IPI00025174. IPI00879475. | ||||||||||||
| RefSeq | NP_005860.2. NM_005869.2. | ||||||||||||
| UniGene | Hs.371372. | ||||||||||||
3D structure databases | |||||||||||||
| PDBe RCSB PDB PDBj |
| ||||||||||||
| ProteinModelPortal | Q6UX04. | ||||||||||||
| ModBase | Search... | ||||||||||||
Protein-protein interaction databases | |||||||||||||
| IntAct | Q6UX04. 3 interactions. | ||||||||||||
| STRING | 9606.ENSP00000370460. | ||||||||||||
PTM databases | |||||||||||||
| PhosphoSite | Q6UX04. | ||||||||||||
Polymorphism databases | |||||||||||||
| DMDM | 74749411. | ||||||||||||
Proteomic databases | |||||||||||||
| PaxDb | Q6UX04. | ||||||||||||
| PRIDE | Q6UX04. | ||||||||||||
Protocols and materials databases | |||||||||||||
| StructuralBiologyKnowledgebase | Search... | ||||||||||||
Genome annotation databases | |||||||||||||
| Ensembl | ENST00000381070; ENSP00000370460; ENSG00000153015. | ||||||||||||
| GeneID | 10283. | ||||||||||||
| KEGG | hsa:10283. | ||||||||||||
| UCSC | uc003jtm.3. human. uc010iwt.1. human. | ||||||||||||
Organism-specific databases | |||||||||||||
| CTD | 10283. | ||||||||||||
| GeneCards | GC05P064064. | ||||||||||||
| HGNC | HGNC:10664. CWC27. | ||||||||||||
| HPA | HPA020344. HPA024149. | ||||||||||||
| neXtProt | NX_Q6UX04. | ||||||||||||
| PharmGKB | PA35594. | ||||||||||||
| GenAtlas | Search... | ||||||||||||
Phylogenomic databases | |||||||||||||
| eggNOG | COG0652. | ||||||||||||
| HOGENOM | HOG000161443. | ||||||||||||
| HOVERGEN | HBG097993. | ||||||||||||
| InParanoid | Q6UX04. | ||||||||||||
| KO | K12737. | ||||||||||||
| OMA | DASMQDS. | ||||||||||||
| OrthoDB | EOG4GXFMV. | ||||||||||||
Gene expression databases | |||||||||||||
| ArrayExpress | Q6UX04. | ||||||||||||
| Bgee | Q6UX04. | ||||||||||||
| CleanEx | HS_SDCCAG10. | ||||||||||||
| Genevestigator | Q6UX04. | ||||||||||||
Family and domain databases | |||||||||||||
| InterPro | IPR002130. Cyclophilin-like_PPIase_dom. IPR020892. Cyclophilin-type_PPIase_CS. [Graphical view] | ||||||||||||
| Pfam | PF00160. Pro_isomerase. 1 hit. [Graphical view] | ||||||||||||
| PRINTS | PR00153. CSAPPISMRASE. | ||||||||||||
| SUPFAM | SSF50891. CSA_PPIase. 1 hit. | ||||||||||||
| PROSITE | PS00170. CSA_PPIASE_1. 1 hit. PS50072. CSA_PPIASE_2. 1 hit. [Graphical view] | ||||||||||||
| ProtoNet | Search... | ||||||||||||
Other | |||||||||||||
| EvolutionaryTrace | Q6UX04. | ||||||||||||
| GenomeRNAi | 10283. | ||||||||||||
| NextBio | 38960. | ||||||||||||
Entry information
| Entry name | CWC27_HUMAN | ||||||||
| Accession | Primary (citable) accession number: Q6UX04 Secondary accession number(s): O60529, O60530, Q96EM3 | ||||||||
| 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 5 Human chromosome 5: 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 |
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| SIMILARITY comments Index of protein domains and families |

Clusters with
