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P13674

- P4HA1_HUMAN

UniProt

P13674 - P4HA1_HUMAN

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Protein

Prolyl 4-hydroxylase subunit alpha-1

Gene

P4HA1

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

Functioni

Catalyzes the post-translational formation of 4-hydroxyproline in -Xaa-Pro-Gly- sequences in collagens and other proteins.

Catalytic activityi

L-proline-[procollagen] + 2-oxoglutarate + O2 = trans-4-hydroxy-L-proline-[procollagen] + succinate + CO2.

Cofactori

Binds 1 Fe2+ ion per subunit.
Ascorbate.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi429 – 4291IronPROSITE-ProRule annotation
Metal bindingi431 – 4311IronPROSITE-ProRule annotation
Metal bindingi500 – 5001IronPROSITE-ProRule annotation
Binding sitei510 – 51012-oxoglutaratePROSITE-ProRule annotation

GO - Molecular functioni

  1. iron ion binding Source: InterPro
  2. L-ascorbic acid binding Source: UniProtKB-KW
  3. oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen Source: InterPro
  4. procollagen-proline 4-dioxygenase activity Source: ProtInc

GO - Biological processi

  1. collagen fibril organization Source: Ensembl
  2. peptidyl-proline hydroxylation to 4-hydroxy-L-proline Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Dioxygenase, Oxidoreductase

Keywords - Ligandi

Iron, Metal-binding, Vitamin C

Enzyme and pathway databases

BRENDAi1.14.11.2. 2681.

Names & Taxonomyi

Protein namesi
Recommended name:
Prolyl 4-hydroxylase subunit alpha-1 (EC:1.14.11.2)
Short name:
4-PH alpha-1
Alternative name(s):
Procollagen-proline,2-oxoglutarate-4-dioxygenase subunit alpha-1
Gene namesi
Name:P4HA1
Synonyms:P4HA
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 10

Organism-specific databases

HGNCiHGNC:8546. P4HA1.

Subcellular locationi

GO - Cellular componenti

  1. endoplasmic reticulum Source: HPA
  2. intracellular membrane-bounded organelle Source: HPA
  3. membrane Source: UniProtKB
  4. mitochondrion Source: HPA
  5. procollagen-proline 4-dioxygenase complex Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi210 – 2101Y → A: Strongly reduced affinity for peptide substrate. 1 Publication
Mutagenesisi213 – 2131Y → A: Strongly reduced affinity for peptide substrate. 1 Publication
Mutagenesisi247 – 2471Y → A: Strongly reduced affinity for peptide substrate. 1 Publication

Organism-specific databases

PharmGKBiPA32874.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1717Add
BLAST
Chaini18 – 534517Prolyl 4-hydroxylase subunit alpha-1PRO_0000022723Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi113 – 1131N-linked (GlcNAc...)1 Publication
Glycosylationi259 – 2591N-linked (GlcNAc...)

Keywords - PTMi

Glycoprotein

Proteomic databases

MaxQBiP13674.
PaxDbiP13674.
PRIDEiP13674.

PTM databases

PhosphoSiteiP13674.

Expressioni

Gene expression databases

BgeeiP13674.
CleanExiHS_P4HA1.
ExpressionAtlasiP13674. baseline and differential.
GenevestigatoriP13674.

Organism-specific databases

HPAiHPA007599.
HPA026593.

Interactioni

Subunit structurei

Heterotetramer of two alpha-1 chains and two beta chains (the beta chain is the multi-functional PDI).1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
HTTP428585EBI-1237386,EBI-466029

Protein-protein interaction databases

BioGridi111072. 15 interactions.
DIPiDIP-38180N.
IntActiP13674. 7 interactions.
MINTiMINT-4657265.
STRINGi9606.ENSP00000263556.

Structurei

Secondary structure

1
534
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi21 – 7151
Helixi74 – 796
Helixi81 – 9212
Helixi94 – 10310
Helixi108 – 11811
Helixi124 – 14118
Helixi145 – 1495
Beta strandi153 – 1564
Helixi164 – 17613
Helixi180 – 19516
Helixi204 – 21714
Helixi221 – 23414
Helixi239 – 25214

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1TJCX-ray2.30A/B161-261[»]
2V5FX-ray2.03A161-263[»]
2YQ8X-ray2.99A/B18-255[»]
4BT8X-ray2.20A/B18-255[»]
4BT9X-ray1.90A/B18-255[»]
4BTAX-ray2.95A/B18-261[»]
4BTBX-ray1.90A18-255[»]
ProteinModelPortaliP13674.
SMRiP13674. Positions 18-254, 335-518.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP13674.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati205 – 23834TPRAdd
BLAST
Domaini411 – 519109Fe2OG dioxygenasePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the P4HA family.Curated
Contains 1 Fe2OG dioxygenase domain.PROSITE-ProRule annotation
Contains 1 TPR repeat.PROSITE-ProRule annotation

Keywords - Domaini

Signal, TPR repeat

Phylogenomic databases

eggNOGiNOG78926.
GeneTreeiENSGT00390000018885.
HOGENOMiHOG000230465.
HOVERGENiHBG006834.
InParanoidiP13674.
KOiK00472.
OMAiNDEDQIG.
OrthoDBiEOG7W6WKC.
PhylomeDBiP13674.
TreeFamiTF313393.

Family and domain databases

Gene3Di1.25.40.10. 2 hits.
InterProiIPR005123. Oxoglu/Fe-dep_dioxygenase.
IPR006620. Pro_4_hyd_alph.
IPR013547. Pro_4_hyd_alph_N.
IPR013026. TPR-contain_dom.
IPR011990. TPR-like_helical_dom.
IPR019734. TPR_repeat.
[Graphical view]
PfamiPF03171. 2OG-FeII_Oxy. 1 hit.
PF08336. P4Ha_N. 1 hit.
[Graphical view]
SMARTiSM00702. P4Hc. 1 hit.
[Graphical view]
PROSITEiPS51471. FE2OG_OXY. 1 hit.
PS50005. TPR. 1 hit.
PS50293. TPR_REGION. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P13674-1) [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
MIWYILIIGI LLPQSLAHPG FFTSIGQMTD LIHTEKDLVT SLKDYIKAEE
60 70 80 90 100
DKLEQIKKWA EKLDRLTSTA TKDPEGFVGH PVNAFKLMKR LNTEWSELEN
110 120 130 140 150
LVLKDMSDGF ISNLTIQRQY FPNDEDQVGA AKALLRLQDT YNLDTDTISK
160 170 180 190 200
GNLPGVKHKS FLTAEDCFEL GKVAYTEADY YHTELWMEQA LRQLDEGEIS
210 220 230 240 250
TIDKVSVLDY LSYAVYQQGD LDKALLLTKK LLELDPEHQR ANGNLKYFEY
260 270 280 290 300
IMAKEKDVNK SASDDQSDQK TTPKKKGVAV DYLPERQKYE MLCRGEGIKM
310 320 330 340 350
TPRRQKKLFC RYHDGNRNPK FILAPAKQED EWDKPRIIRF HDIISDAEIE
360 370 380 390 400
IVKDLAKPRL RRATISNPIT GDLETVHYRI SKSAWLSGYE NPVVSRINMR
410 420 430 440 450
IQDLTGLDVS TAEELQVANY GVGGQYEPHF DFARKDEPDA FKELGTGNRI
460 470 480 490 500
ATWLFYMSDV SAGGATVFPE VGASVWPKKG TAVFWYNLFA SGEGDYSTRH
510 520 530
AACPVLVGNK WVSNKWLHER GQEFRRPCTL SELE
Length:534
Mass (Da):61,049
Last modified:November 1, 1997 - v2
Checksum:iEBAFA8CCF09A1DDB
GO
Isoform 2 (identifier: P13674-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     361-380: RRATISNPITGDLETVHYRI → SRATVHDPETGKLTTAQYRV

Show »
Length:534
Mass (Da):60,967
Checksum:i5FE1B10A8AC5E792
GO
Isoform 3 (identifier: P13674-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     361-380: RRATISNPITGDLETVHYRI → SRATVHDPETGKLTTAQYRV
     417-434: Missing.

Note: No experimental confirmation available.

Show »
Length:516
Mass (Da):58,958
Checksum:iED30BECCFB48CD7E
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti119 – 1224QYFP → PVLS in AAA36534. (PubMed:2543975)Curated
Sequence conflicti119 – 1224QYFP → PVLS in AAA36535. (PubMed:2543975)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei361 – 38020RRATI…VHYRI → SRATVHDPETGKLTTAQYRV in isoform 2 and isoform 3. 2 PublicationsVSP_004504Add
BLAST
Alternative sequencei417 – 43418Missing in isoform 3. 1 PublicationVSP_044578Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M24486 mRNA. Translation: AAA36534.1.
M24487 mRNA. Translation: AAA36535.1.
U14620
, U14607, U14605, U14608, U14609, U14611, U14610, U14612, U14614, U14615, U14616, U14617, U14618, U14619 Genomic DNA. Translation: AAA59068.1.
U14620
, U14607, U14605, U14608, U14609, U14611, U14610, U14612, U14613, U14615, U14616, U14617, U14618, U14619 Genomic DNA. Translation: AAA59069.1.
CD013929 Genomic DNA. No translation available.
AL731563 Genomic DNA. Translation: CAH72754.1.
BC034998 mRNA. Translation: AAH34998.1.
CCDSiCCDS41537.1. [P13674-1]
CCDS44432.1. [P13674-3]
CCDS7320.1. [P13674-2]
PIRiA33919. DAHUA1.
I37173. DAHUA2.
RefSeqiNP_000908.2. NM_000917.3. [P13674-2]
NP_001017962.1. NM_001017962.2. [P13674-1]
NP_001136067.1. NM_001142595.1. [P13674-1]
NP_001136068.1. NM_001142596.1. [P13674-3]
UniGeneiHs.500047.
Hs.593005.

Genome annotation databases

EnsembliENST00000263556; ENSP00000263556; ENSG00000122884. [P13674-2]
ENST00000307116; ENSP00000307318; ENSG00000122884. [P13674-1]
ENST00000373008; ENSP00000362099; ENSG00000122884. [P13674-2]
ENST00000394890; ENSP00000378353; ENSG00000122884. [P13674-1]
ENST00000440381; ENSP00000414464; ENSG00000122884. [P13674-3]
GeneIDi5033.
KEGGihsa:5033.
UCSCiuc001jtg.3. human. [P13674-1]

Polymorphism databases

DMDMi2507090.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M24486 mRNA. Translation: AAA36534.1 .
M24487 mRNA. Translation: AAA36535.1 .
U14620
, U14607 , U14605 , U14608 , U14609 , U14611 , U14610 , U14612 , U14614 , U14615 , U14616 , U14617 , U14618 , U14619 Genomic DNA. Translation: AAA59068.1 .
U14620
, U14607 , U14605 , U14608 , U14609 , U14611 , U14610 , U14612 , U14613 , U14615 , U14616 , U14617 , U14618 , U14619 Genomic DNA. Translation: AAA59069.1 .
CD013929 Genomic DNA. No translation available.
AL731563 Genomic DNA. Translation: CAH72754.1 .
BC034998 mRNA. Translation: AAH34998.1 .
CCDSi CCDS41537.1. [P13674-1 ]
CCDS44432.1. [P13674-3 ]
CCDS7320.1. [P13674-2 ]
PIRi A33919. DAHUA1.
I37173. DAHUA2.
RefSeqi NP_000908.2. NM_000917.3. [P13674-2 ]
NP_001017962.1. NM_001017962.2. [P13674-1 ]
NP_001136067.1. NM_001142595.1. [P13674-1 ]
NP_001136068.1. NM_001142596.1. [P13674-3 ]
UniGenei Hs.500047.
Hs.593005.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1TJC X-ray 2.30 A/B 161-261 [» ]
2V5F X-ray 2.03 A 161-263 [» ]
2YQ8 X-ray 2.99 A/B 18-255 [» ]
4BT8 X-ray 2.20 A/B 18-255 [» ]
4BT9 X-ray 1.90 A/B 18-255 [» ]
4BTA X-ray 2.95 A/B 18-261 [» ]
4BTB X-ray 1.90 A 18-255 [» ]
ProteinModelPortali P13674.
SMRi P13674. Positions 18-254, 335-518.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111072. 15 interactions.
DIPi DIP-38180N.
IntActi P13674. 7 interactions.
MINTi MINT-4657265.
STRINGi 9606.ENSP00000263556.

Chemistry

ChEMBLi CHEMBL1250350.
DrugBanki DB01275. Hydralazine.
DB00172. L-Proline.
DB00139. Succinic acid.
DB00126. Vitamin C.

PTM databases

PhosphoSitei P13674.

Polymorphism databases

DMDMi 2507090.

Proteomic databases

MaxQBi P13674.
PaxDbi P13674.
PRIDEi P13674.

Protocols and materials databases

DNASUi 5033.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000263556 ; ENSP00000263556 ; ENSG00000122884 . [P13674-2 ]
ENST00000307116 ; ENSP00000307318 ; ENSG00000122884 . [P13674-1 ]
ENST00000373008 ; ENSP00000362099 ; ENSG00000122884 . [P13674-2 ]
ENST00000394890 ; ENSP00000378353 ; ENSG00000122884 . [P13674-1 ]
ENST00000440381 ; ENSP00000414464 ; ENSG00000122884 . [P13674-3 ]
GeneIDi 5033.
KEGGi hsa:5033.
UCSCi uc001jtg.3. human. [P13674-1 ]

Organism-specific databases

CTDi 5033.
GeneCardsi GC10M074769.
HGNCi HGNC:8546. P4HA1.
HPAi HPA007599.
HPA026593.
MIMi 176710. gene.
neXtProti NX_P13674.
PharmGKBi PA32874.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG78926.
GeneTreei ENSGT00390000018885.
HOGENOMi HOG000230465.
HOVERGENi HBG006834.
InParanoidi P13674.
KOi K00472.
OMAi NDEDQIG.
OrthoDBi EOG7W6WKC.
PhylomeDBi P13674.
TreeFami TF313393.

Enzyme and pathway databases

BRENDAi 1.14.11.2. 2681.

Miscellaneous databases

EvolutionaryTracei P13674.
GeneWikii P4HA1.
GenomeRNAii 5033.
NextBioi 19392.
PROi P13674.
SOURCEi Search...

Gene expression databases

Bgeei P13674.
CleanExi HS_P4HA1.
ExpressionAtlasi P13674. baseline and differential.
Genevestigatori P13674.

Family and domain databases

Gene3Di 1.25.40.10. 2 hits.
InterProi IPR005123. Oxoglu/Fe-dep_dioxygenase.
IPR006620. Pro_4_hyd_alph.
IPR013547. Pro_4_hyd_alph_N.
IPR013026. TPR-contain_dom.
IPR011990. TPR-like_helical_dom.
IPR019734. TPR_repeat.
[Graphical view ]
Pfami PF03171. 2OG-FeII_Oxy. 1 hit.
PF08336. P4Ha_N. 1 hit.
[Graphical view ]
SMARTi SM00702. P4Hc. 1 hit.
[Graphical view ]
PROSITEi PS51471. FE2OG_OXY. 1 hit.
PS50005. TPR. 1 hit.
PS50293. TPR_REGION. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING.
  3. "PCR isolation and cloning of novel splice variant mRNAs from known drug target genes."
    Jin P., Fu G.K., Wilson A.D., Yang J., Chien D., Hawkins P.R., Au-Young J., Stuve L.L.
    Genomics 83:566-571(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
  4. "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].
  5. "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).
    Tissue: Brain.
  6. "Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
    Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
    J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-113.
    Tissue: Liver.
  7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. "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] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 161-261, SUBUNIT, MUTAGENESIS OF TYR-210; TYR-213 AND TYR-247.

Entry informationi

Entry nameiP4HA1_HUMAN
AccessioniPrimary (citable) accession number: P13674
Secondary accession number(s): C9JL12
, Q15082, Q15083, Q5VSQ5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: November 1, 1997
Last modified: October 29, 2014
This is version 168 of the entry and version 2 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. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3