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P10746 (HEM4_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 140. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Uroporphyrinogen-III synthase

Short name=UROIIIS
Short name=UROS
EC=4.2.1.75
Alternative name(s):
Hydroxymethylbilane hydrolyase [cyclizing]
Uroporphyrinogen-III cosynthase
Gene names
Name:UROS
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length265 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes cyclization of the linear tetrapyrrole, hydroxymethylbilane, to the macrocyclic uroporphyrinogen III, the branch point for the various sub-pathways leading to the wide diversity of porphyrins. Porphyrins act as cofactors for a multitude of enzymes that perform a variety of processes within the cell such as methionine synthesis (vitamin B12) or oxygen transport (heme).

Catalytic activity

Hydroxymethylbilane = uroporphyrinogen III + H2O. Ref.8

Pathway

Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 3/4.

Subunit structure

Monomer. Ref.8

Tissue specificity

Ubiquitous. Ref.2

Involvement in disease

Congenital erythropoietic porphyria (CEP) [MIM:263700]: Porphyrias are inherited defects in the biosynthesis of heme, resulting in the accumulation and increased excretion of porphyrins or porphyrin precursors. They are classified as erythropoietic or hepatic, depending on whether the enzyme deficiency occurs in red blood cells or in the liver. The manifestations of CEP are heterogeneous, ranging from nonimmune hydrops fetalis due to severe hemolytic anemia in utero to milder, later onset forms, which have only skin lesions due to cutaneous photosensitivity in adult life. The deficiency in UROS activity results in the non-enzymatic conversion of hydroxymethylbilane (HMB) into the uroporphyrinogen-I isomer.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.16 Ref.17 Ref.18 Ref.19 Ref.20 Ref.21

Severe congenital erythropoietic porphyria is associated with non-immune hydrops fetalis, a generalized edema of the fetus with fluid accumulation in the body cavities due to non-immune causes. Non-immune hydrops fetalis is not a diagnosis in itself but a symptom, a feature of many genetic disorders, and the end-stage of a wide variety of disorders.

Sequence similarities

Belongs to the uroporphyrinogen-III synthase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 265265Uroporphyrinogen-III synthase
PRO_0000135251

Natural variations

Natural variant31V → F in CEP; no residual activity. Ref.14
VAR_021615
Natural variant41L → F in CEP. Ref.10
VAR_003674
Natural variant191Y → C in CEP. Ref.12
VAR_003675
Natural variant471S → P in CEP; less than 3% wild-type activity; severe cutaneous lesions. Ref.19
VAR_021616
Natural variant531P → L in CEP; no detectable activity; severe phenotype. Ref.9
VAR_003676
Natural variant621T → A in CEP; no detectable activity according to PubMed:1737856, while it does not affect enzymatic activity according to PubMed:11689424. Ref.8 Ref.11
Corresponds to variant rs28941775 [ dbSNP | Ensembl ].
VAR_003677
Natural variant661A → V in CEP; residual activity; mild phenotype. Ref.11
Corresponds to variant rs28941774 [ dbSNP | Ensembl ].
VAR_003678
Natural variant691A → T in CEP; less than 2% wild-type activity; moderately-severe phenotype. Ref.18
VAR_021617
Natural variant731C → R in CEP; frequent mutation in Western countries; no detectable activity; severe phenotype. Ref.9 Ref.10 Ref.11 Ref.16 Ref.18
VAR_003679
Natural variant821V → F in CEP; high residual activity; mild phenotype. Ref.12
Corresponds to variant rs121908016 [ dbSNP | Ensembl ].
VAR_003680
Natural variant991V → A in CEP. Ref.12
VAR_003681
Natural variant1041A → V in CEP; residual activity. Ref.12
VAR_003682
Natural variant1241K → R.
Corresponds to variant rs17153561 [ dbSNP | Ensembl ].
VAR_049345
Natural variant1291I → T in CEP; no residual activity. Ref.17
VAR_021618
Natural variant1711V → G.
Corresponds to variant rs17173752 [ dbSNP | Ensembl ].
VAR_049346
Natural variant1881G → R in CEP; less than 5% wild-type activity. Ref.15
VAR_013558
Natural variant1881G → W in CEP; less than 2% wild-type activity; mild phenotype. Ref.18
VAR_021619
Natural variant210 – 2112EL → HIQSQAQSQAQDN in CEP.
VAR_021620
Natural variant2121S → P in CEP; no residual activity. Ref.13
VAR_003683
Natural variant2191I → S in CEP; less than 2% wild-type activity; moderately-severe phenotype. Ref.18
VAR_021621
Natural variant2251G → S in CEP. Ref.12
VAR_003684
Natural variant2281T → M in CEP; no detectable activity. Ref.10 Ref.11 Ref.18
VAR_003685
Natural variant2371L → P in CEP. Ref.21
VAR_067318
Natural variant2481P → Q in CEP. Ref.20
VAR_066247

Experimental info

Mutagenesis631S → A: Does not affect enzymatic activity. Ref.8
Mutagenesis651R → A: Slightly affects enzymatic activity. Ref.8
Mutagenesis1031T → A: Slightly affects enzymatic activity. Ref.8
Mutagenesis1271E → A: Does not affect enzymatic activity. Ref.8
Mutagenesis1681Y → F: Impairs enzymatic activity. Ref.8
Mutagenesis1971S → A: Does not affect enzymatic activity. Ref.8
Mutagenesis2201K → A: Does not affect enzymatic activity. Ref.8
Mutagenesis2271T → A: Does not affect enzymatic activity. Ref.8
Mutagenesis2281T → A: Impairs enzymatic activity. Ref.8

Secondary structure

................................................... 265
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P10746 [UniParc].

Last modified July 1, 1989. Version 1.
Checksum: CEF171401361F61E

FASTA26528,628
        10         20         30         40         50         60 
MKVLLLKDAK EDDCGQDPYI RELGLYGLEA TLIPVLSFEF LSLPSFSEKL SHPEDYGGLI 

        70         80         90        100        110        120 
FTSPRAVEAA ELCLEQNNKT EVWERSLKEK WNAKSVYVVG NATASLVSKI GLDTEGETCG 

       130        140        150        160        170        180 
NAEKLAEYIC SRESSALPLL FPCGNLKREI LPKALKDKGI AMESITVYQT VAHPGIQGNL 

       190        200        210        220        230        240 
NSYYSQQGVP ASITFFSPSG LTYSLKHIQE LSGDNIDQIK FAAIGPTTAR ALAAQGLPVS 

       250        260 
CTAESPTPQA LATGIRKALQ PHGCC 

« Hide

References

« Hide 'large scale' references
[1]"Human uroporphyrinogen III synthase: molecular cloning, nucleotide sequence, and expression of a full-length cDNA."
Tsai S.-F., Bishop D.F., Desnick R.J.
Proc. Natl. Acad. Sci. U.S.A. 85:7049-7053(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
[2]"Human uroporphyrinogen-III synthase: genomic organization, alternative promoters, and erythroid-specific expression."
Aizencang G., Solis C., Bishop D.F., Warner C., Desnick R.J.
Genomics 70:223-231(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], TISSUE SPECIFICITY.
Tissue: Liver.
[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].
Tissue: Cerebellum.
[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. 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].
[5]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].
[6]"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].
Tissue: Brain.
[7]"Molecular basis of congenital erythropoietic porphyria: mutations in the human uroporphyrinogen III synthase gene."
Xu W., Astrin K.H., Desnick R.J.
Hum. Mutat. 7:187-192(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW ON VARIANTS.
[8]"Crystal structure of human uroporphyrinogen III synthase."
Mathews M.A., Schubert H.L., Whitby F.G., Alexander K.J., Schadick K., Bergonia H.A., Phillips J.D., Hill C.P.
EMBO J. 20:5832-5839(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.84 ANGSTROMS), CATALYTIC ACTIVITY, SUBUNIT, MUTAGENESIS OF SER-63; ARG-65; THR-103; GLU-127; TYR-168; SER-197; LYS-220; THR-227 AND THR-228, CHARACTERIZATION OF VARIANT ALA-62.
[9]"Point mutations in the uroporphyrinogen III synthase gene in congenital erythropoietic porphyria (Gunther's disease)."
Deybach J.-C., de Verneuil H., Boulechfar S., Grandchamp B., Nordmann Y.
Blood 75:1763-1765(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS CEP LEU-53 AND ARG-73.
[10]"Heterogeneity of mutations in the uroporphyrinogen III synthase gene in congenital erythropoietic porphyria."
Boulechfar S., da Silva V., Deybach J.-C., Nordmann Y., Grandchamp B., de Verneuil H.
Hum. Genet. 88:320-324(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS CEP PHE-4; ARG-73 AND MET-228.
[11]"Congenital erythropoietic porphyria: identification and expression of exonic mutations in the uroporphyrinogen III synthase gene."
Warner C.A., Yoo H.-W., Roberts A.G., Desnick R.J.
J. Clin. Invest. 89:693-700(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS CEP ALA-62; VAL-66; ARG-73 AND MET-228.
[12]"Congenital erythropoietic porphyria: identification and expression of 10 mutations in the uroporphyrinogen III synthase gene."
Xu W., Warner C.A., Desnick R.J.
J. Clin. Invest. 95:905-912(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS CEP CYS-19; PHE-82; ALA-99; VAL-104 AND SER-225.
[13]"A novel point mutation in congenital erythropoietic porphyria in two members of Japanese family."
Tanigawa K., Bensidhoum M., Takamura N., Namba H., Yamashita S., de Verneuil H., Ged C.
Hum. Genet. 97:557-560(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT CEP PRO-212.
[14]"Novel point mutation in the uroporphyrinogen III synthase gene causes congenital erythropoietic porphyria of a Japanese family."
Takamura N., Hombrados I., Tanigawa K., Namba H., Nagayama Y., de Verneuil H., Yamashita S.
Am. J. Med. Genet. 70:299-302(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT CEP PHE-3, CHARACTERIZATION OF VARIANT CEP PHE-3.
[15]"Congenital erythropoietic porphyria successfully treated by allogeneic bone marrow transplantation."
Tezcan I., Xu W., Gurgey A., Tuncer M., Cetin M., Oener C., Yetgin S., Ersoy F., Aizencang G., Astrin K.H., Desnick R.J.
Blood 92:4053-4058(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT CEP ARG-188.
[16]"C73R is a hotspot mutation in the uroporphyrinogen III synthase gene in congenital erythropoietic porphyria."
Frank J., Wang X., Lam H.M., Aita V.M., Jugert F.K., Goerz G., Merk H.F., Poh-Fitzpatrick M.B., Christiano A.M.
Ann. Hum. Genet. 62:225-230(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT CEP ARG-73.
[17]"Congenital erythropoietic porphyria: a novel homozygous mutation in a Japanese patient."
Rogounovitch T., Takamura N., Hombrados I., Morel C., Tanaka T., Kameyoshi Y., Shimizu-Yoshida Y., de Verneuil H., Yamashita S.
J. Invest. Dermatol. 115:1156-1156(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT CEP THR-129, CHARACTERIZATION OF VARIANT CEP THR-129.
[18]"Congenital erythropoietic porphyria: identification and expression of eight novel mutations in the uroporphyrinogen III synthase gene."
Shady A.A., Colby B.R., Cunha L.F., Astrin K.H., Bishop D.F., Desnick R.J.
Br. J. Haematol. 117:980-987(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS CEP THR-69; ARG-73; TRP-188; 210-GLU-LEU-211 DELINS HIS-ILE-GLN-SER-GLN-ALA-GLN-SER-GLN-ALA-GLN-ASP-ASN; SER-219 AND MET-228, CHARACTERIZATION OF VARIANTS CEP THR-69; TRP-188 AND SER-219.
[19]"Congenital erythropoietic porphyria: report of a novel mutation with absence of clinical manifestations in a homozygous mutant sibling."
Ged C., Megarbane H., Chouery E., Lalanne M., Megarbane A., de Verneuil H.
J. Invest. Dermatol. 123:589-591(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT CEP PRO-47, CHARACTERIZATION OF VARIANT CEP PRO-47.
[20]"ALAS2 acts as a modifier gene in patients with congenital erythropoietic porphyria."
To-Figueras J., Ducamp S., Clayton J., Badenas C., Delaby C., Ged C., Lyoumi S., Gouya L., de Verneuil H., Beaumont C., Ferreira G.C., Deybach J.C., Herrero C., Puy H.
Blood 118:1443-1451(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT CEP GLN-248.
[21]"Mutational analysis of uroporphyrinogen III cosynthase gene in Iranian families with congenital erythropoietic porphyria."
Moghbeli M., Maleknejad M., Arabi A., Abbaszadegan M.R.
Mol. Biol. Rep. 39:6731-6735(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT CEP PRO-237.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
J03824 mRNA. Translation: AAA60273.1.
AF230665 mRNA. Translation: AAG36795.1.
AH010036 Genomic DNA. Translation: AAG36794.1.
AK314896 mRNA. Translation: BAG37410.1.
AL360176 Genomic DNA. Translation: CAI12087.1.
CH471066 Genomic DNA. Translation: EAW49221.1.
CH471066 Genomic DNA. Translation: EAW49222.1.
BC002573 mRNA. Translation: AAH02573.1.
PIRA40483.
RefSeqNP_000366.1. NM_000375.2.
UniGeneHs.501376.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1JR2X-ray1.84A/B1-265[»]
ProteinModelPortalP10746.
SMRP10746. Positions 1-260.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid113236. 3 interactions.
IntActP10746. 2 interactions.
MINTMINT-2863993.
STRING9606.ENSP00000357775.

Chemistry

ChEMBLCHEMBL4433.

PTM databases

PhosphoSiteP10746.

Polymorphism databases

DMDM122849.

Proteomic databases

PaxDbP10746.
PRIDEP10746.

Protocols and materials databases

DNASU7390.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000368786; ENSP00000357775; ENSG00000188690.
ENST00000368797; ENSP00000357787; ENSG00000188690.
GeneID7390.
KEGGhsa:7390.
UCSCuc001liw.4. human.

Organism-specific databases

CTD7390.
GeneCardsGC10M127467.
HGNCHGNC:12592. UROS.
HPAHPA044038.
MIM263700. phenotype.
606938. gene.
neXtProtNX_P10746.
Orphanet79277. Congenital erythropoietic porphyria.
PharmGKBPA37222.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1587.
HOGENOMHOG000007209.
HOVERGENHBG000492.
InParanoidP10746.
KOK01719.
OMADKGIAME.
OrthoDBEOG7K3TMH.
PhylomeDBP10746.
TreeFamTF324092.

Enzyme and pathway databases

BioCycMetaCyc:HS07569-MONOMER.
ReactomeREACT_111217. Metabolism.
UniPathwayUPA00251; UER00320.

Gene expression databases

ArrayExpressP10746.
BgeeP10746.
CleanExHS_UROS.
GenevestigatorP10746.

Family and domain databases

InterProIPR003754. 4pyrrol_synth_uPrphyn_synth.
[Graphical view]
PfamPF02602. HEM4. 1 hit.
[Graphical view]
SUPFAMSSF69618. SSF69618. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP10746.
GenomeRNAi7390.
NextBio28934.
PROP10746.
SOURCESearch...

Entry information

Entry nameHEM4_HUMAN
AccessionPrimary (citable) accession number: P10746
Secondary accession number(s): B2RC13, D3DRF7, Q9H2T1
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: April 16, 2014
This is version 140 of the entry and version 1 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

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

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