Reviewed,
UniProtKB/Swiss-Prot P13674 (P4HA1_HUMAN)
Last modified
November 25, 2008.
Version 106.
History...
Clusters with 100%,
90%,
50% identity |
Documents (5) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Prolyl 4-hydroxylase subunit alpha-1 EC=1.14.11.2 Alternative name(s): 4-PH alpha-1 Procollagen-proline,2-oxoglutarate-4-dioxygenase subunit alpha-1 | ||||
| Gene names |
| ||||
| Organism | Homo sapiens (Human) | ||||
| Taxonomic identifier | 9606 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo |
Protein attributes
| Sequence length | 534 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Function | Catalyzes the post-translational formation of 4-hydroxyproline in -Xaa-Pro-Gly- sequences in collagens and other proteins. |
| Catalytic activity | Procollagen L-proline + 2-oxoglutarate + O(2) = procollagen trans-4-hydroxy-L-proline + succinate + CO(2). |
| Cofactor | Binds 1 Fe(2+) ion per subunit. Ascorbate. |
| Subunit structure | Heterotetramer of two alpha-1 chains and two beta chains (the beta chain is the multi-functional PDI). |
| Subcellular location | |
| Sequence similarities | Belongs to the P4HA family. Contains 1 PKHD (prolyl/lysyl hydroxylase) domain. Contains 1 TPR repeat. |
Ontologies
Alternative products
| This entry describes 2 isoforms produced by alternative splicing. [Align] [Select] | ||||||
| Isoform 1 (identifier: P13674-1) 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: P13674-2) The sequence of this isoform differs from the canonical sequence as follows: 361-380: RRATISNPITGDLETVHYRI → SRATVHDPETGKLTTAQYRV |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||||||||||
Molecule processing | |||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Signal peptide | 1 – 17 | 17 | |||||||||||||||||
| Chain | 18 – 534 | 517 | Prolyl 4-hydroxylase subunit alpha-1 | PRO_0000022723 | |||||||||||||||
Regions | |||||||||||||||||||
| Repeat | 205 – 238 | 34 | TPR | ||||||||||||||||
| Domain | 335 – 518 | 184 | PKHD | ||||||||||||||||
Sites | |||||||||||||||||||
| Metal binding | 429 | 1 | Iron By similarity | ||||||||||||||||
| Metal binding | 431 | 1 | Iron By similarity | ||||||||||||||||
| Metal binding | 500 | 1 | Iron By similarity | ||||||||||||||||
| Binding site | 510 | 1 | 2-oxoglutarate Potential | ||||||||||||||||
Amino acid modifications | |||||||||||||||||||
| Glycosylation | 113 | 1 | N-linked (GlcNAc...) | ||||||||||||||||
| Glycosylation | 259 | 1 | N-linked (GlcNAc...) | ||||||||||||||||
Natural variations | |||||||||||||||||||
| Alternative sequence | 361 – 380 | 20 | RRATI…VHYRI → SRATVHDPETGKLTTAQYRV in isoform 2. | VSP_004504 | |||||||||||||||
Experimental info | |||||||||||||||||||
| Mutagenesis | 210 | 1 | Y → A: Strongly reduced affinity for peptide substrate | ||||||||||||||||
| Mutagenesis | 213 | 1 | Y → A: Strongly reduced affinity for peptide substrate | ||||||||||||||||
| Mutagenesis | 247 | 1 | Y → A: Strongly reduced affinity for peptide substrate | ||||||||||||||||
| Sequence conflict | 119 – 122 | 4 | QYFP → PVLS in AAA36534 and AAA36535. Ref.1 | ||||||||||||||||
Secondary structure | |||||||||||||||||||
Helix Strand Turn | |||||||||||||||||||
| Helix | 164 – 176 | 13 | |||||||||||||||||
| Helix | 180 – 195 | 16 | |||||||||||||||||
| Helix | 204 – 217 | 14 | |||||||||||||||||
| Helix | 221 – 234 | 14 | |||||||||||||||||
| Helix | 239 – 253 | 15 | |||||||||||||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Molecular cloning of the alpha-subunit of human prolyl 4-hydroxylase: the complete cDNA-derived amino acid sequence and evidence for alternative splicing of RNA transcripts." Helaakoski T., Vuori K., Myllylae R., Kivirikko K.I., Pihlajaniemi T. Proc. Natl. Acad. Sci. U.S.A. 86:4392-4396(1989) [PubMed: 2543975] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2). |
| [2] | "Structure and expression of the human gene for the alpha subunit of prolyl 4-hydroxylase. The two alternatively spliced types of mRNA correspond to two homologous exons the sequences of which are expressed in a variety of tissues." Helaakoski T., Veijola J., Vuori K., Rehn M., Chow L.T., Taillon-Miller P., Kivirikko K.I., Pihlajaniemi T. J. Biol. Chem. 269:27847-27854(1994) [PubMed: 7961714] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING. |
| [3] | "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: 15164054] [Abstract] 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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Brain. |
| [5] | "The peptide-substrate-binding domain of collagen prolyl 4-hydroxylases is a tetratricopeptide repeat domain with functional aromatic residues." Pekkala M., Hieta R., Bergmann U., Kivirikko K.I., Wierenga R.K., Myllyharju J. J. Biol. Chem. 279:52255-52261(2004) [PubMed: 15456751] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 161-261, SUBUNIT, MUTAGENESIS OF TYR-210; TYR-213 AND TYR-247. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| M24486 mRNA. Translation: AAA36534.1. M24487 mRNA. Translation: AAA36535.1. U14620 U14619 Genomic DNA. Translation: AAA59068.1. U14620 U14619 Genomic DNA. Translation: AAA59069.1. AL731563 Genomic DNA. Translation: CAH72754.1. BC034998 mRNA. Translation: AAH34998.1. | |||||||||||||
| PIR | DAHUA1. A33919. DAHUA2. I37173. | ||||||||||||
| RefSeq | NP_000908.2. NP_001017962.1. | ||||||||||||
| UniGene | Hs.500047 | ||||||||||||
3D structure databases | |||||||||||||
| |||||||||||||
| ModBase | Search... | ||||||||||||
PTM databases | |||||||||||||
| PhosphoSite | P13674. | ||||||||||||
Genome annotation databases | |||||||||||||
| Ensembl | ENSG00000122884. Homo sapiens. [Contig view] | ||||||||||||
| GeneID | 5033. | ||||||||||||
| KEGG | hsa:5033. | ||||||||||||
Organism-specific databases | |||||||||||||
| H-InvDB | HIX0025926. | ||||||||||||
| HGNC | HGNC:8546. P4HA1. | ||||||||||||
| HPA | HPA007599. | ||||||||||||
| MIM | 176710. gene. | ||||||||||||
| PharmGKB | PA32874. | ||||||||||||
| GenAtlas | Search... | ||||||||||||
| GeneCards | Search... | ||||||||||||
Phylogenomic databases | |||||||||||||
| HOVERGEN | P13674. | ||||||||||||
Gene expression databases | |||||||||||||
| ArrayExpress | P13674. | ||||||||||||
| CleanEx | HS_P4HA1. | ||||||||||||
| GermOnline | ENSG00000122884. Homo sapiens. | ||||||||||||
Family and domain databases | |||||||||||||
| InterPro | IPR005123. 2OG-FeII_Oase. IPR006620. Pro_4_hyd_alph. IPR013547. Pro_4_hyd_alph_N. IPR011990. TPR-like_helical. IPR013105. TPR_2. IPR013026. TPR_region. [Graphical view] | ||||||||||||
| Gene3D | G3DSA:1.25.40.10. TPR-like_helical. 1 hit. | ||||||||||||
| Pfam | PF03171. 2OG-FeII_Oxy. 1 hit. PF08336. P4Ha_N. 1 hit. PF07719. TPR_2. 1 hit. [Graphical view] | ||||||||||||
| SMART | SM00702. P4Hc. 1 hit. [Graphical view] | ||||||||||||
| PROSITE | PS50005. TPR. 1 hit. PS50293. TPR_REGION. 1 hit. [Graphical view] | ||||||||||||
| ProtoNet | Search... | ||||||||||||
Other Resources | |||||||||||||
| DrugBank | DB01275. Hydralazine. DB00172. L-Proline. DB00139. Succinic acid. DB00126. Vitamin C. | ||||||||||||
| LinkHub | P13674. | ||||||||||||
| NextBio | 19392. | ||||||||||||
| SOURCE | Search... | ||||||||||||
Entry information
| Entry name | P4HA1_HUMAN | ||||||||
| Accession | Primary (citable) accession number: P13674 Secondary accession number(s): Q15082, Q15083, Q5VSQ5 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||
Relevant documents
| Human chromosome 10 Human chromosome 10: entries, gene names and cross-references to MIM |
| 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 |
| UniProtKB secondary accession numbers Index of UniProtKB secondary accession numbers |
| SIMILARITY comments Index of protein domains and families |

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