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Protein

Sterol 26-hydroxylase, mitochondrial

Gene

CYP27A1

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

Functioni

Catalyzes the first step in the oxidation of the side chain of sterol intermediates; the 27-hydroxylation of 5-beta-cholestane-3-alpha,7-alpha,12-alpha-triol. Has also a vitamin D3-25-hydroxylase activity.

Catalytic activityi

5-beta-cholestane-3-alpha,7-alpha,12-alpha-triol + 3 NADPH + 3 O2 = (25R)-3-alpha,7-alpha,12-alpha-trihydroxy-5-beta-cholestan-26-oate + 3 NADP+ + 4 H2O.

Cofactori

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi476 – 4761Iron (heme axial ligand)

GO - Molecular functioni

  1. cholestanetriol 26-monooxygenase activity Source: UniProtKB-EC
  2. cholesterol 26-hydroxylase activity Source: Ensembl
  3. heme binding Source: InterPro
  4. iron ion binding Source: InterPro
  5. steroid hydroxylase activity Source: ProtInc
  6. vitamin D3 25-hydroxylase activity Source: Ensembl

GO - Biological processi

  1. bile acid biosynthetic process Source: Reactome
  2. bile acid metabolic process Source: Reactome
  3. cholesterol metabolic process Source: Ensembl
  4. small molecule metabolic process Source: Reactome
  5. sterol metabolic process Source: Reactome
  6. xenobiotic metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Monooxygenase, Oxidoreductase

Keywords - Ligandi

Heme, Iron, Metal-binding, NADP

Enzyme and pathway databases

BRENDAi1.14.99.38. 2681.
ReactomeiREACT_11041. Synthesis of bile acids and bile salts via 7alpha-hydroxycholesterol.
REACT_11048. Synthesis of bile acids and bile salts via 27-hydroxycholesterol.
REACT_11053. Synthesis of bile acids and bile salts via 24-hydroxycholesterol.
REACT_13812. Endogenous sterols.
REACT_268413. Defective CYP27A1 causes Cerebrotendinous xanthomatosis (CTX).
UniPathwayiUPA00955.

Names & Taxonomyi

Protein namesi
Recommended name:
Sterol 26-hydroxylase, mitochondrial (EC:1.14.13.15)
Alternative name(s):
5-beta-cholestane-3-alpha,7-alpha,12-alpha-triol 27-hydroxylase
Cytochrome P-450C27/25
Cytochrome P450 27
Sterol 27-hydroxylase
Vitamin D(3) 25-hydroxylase
Gene namesi
Name:CYP27A1
Synonyms:CYP27
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 2

Organism-specific databases

HGNCiHGNC:2605. CYP27A1.

Subcellular locationi

GO - Cellular componenti

  1. mitochondrial inner membrane Source: Ensembl
  2. mitochondrial matrix Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Mitochondrion

Pathology & Biotechi

Involvement in diseasei

Cerebrotendinous xanthomatosis (CTX)5 Publications

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionRare sterol storage disorder characterized clinically by progressive neurologic dysfunction, premature atherosclerosis, and cataracts.

See also OMIM:213700
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti145 – 1451G → E in CTX. 1 Publication
VAR_016966
Natural varianti395 – 3951R → C in CTX. 1 Publication
VAR_001303
Natural varianti395 – 3951R → S in CTX. 1 Publication
VAR_012285
Natural varianti405 – 4051R → Q in CTX. 1 Publication
VAR_012286
Natural varianti474 – 4741R → Q in CTX. 1 Publication
VAR_012287
Natural varianti474 – 4741R → W in CTX. 1 Publication
VAR_012288
Natural varianti479 – 4791R → C in CTX. 1 Publication
VAR_001304

Keywords - Diseasei

Cataract, Disease mutation

Organism-specific databases

MIMi213700. phenotype.
Orphaneti909. Cerebrotendinous xanthomatosis.
PharmGKBiPA135.

Chemistry

DrugBankiDB06777. Chenodeoxycholic acid.
DB00169. Cholecalciferol.
DB00153. Ergocalciferol.
DB00082. Pegvisomant.

Polymorphism and mutation databases

BioMutaiCYP27A1.
DMDMi399288.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 3333MitochondrionAdd
BLAST
Chaini34 – 531498Sterol 26-hydroxylase, mitochondrialPRO_0000003618Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei283 – 2831N6-acetyllysineBy similarity
Modified residuei509 – 5091N6-acetyllysineBy similarity
Modified residuei520 – 5201N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ02318.
PaxDbiQ02318.
PeptideAtlasiQ02318.
PRIDEiQ02318.

PTM databases

PhosphoSiteiQ02318.

Expressioni

Gene expression databases

BgeeiQ02318.
CleanExiHS_CYP27A1.
ExpressionAtlasiQ02318. baseline and differential.
GenevestigatoriQ02318.

Organism-specific databases

HPAiHPA059155.

Interactioni

Protein-protein interaction databases

BioGridi107965. 1 interaction.
IntActiQ02318. 1 interaction.
STRINGi9606.ENSP00000258415.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1MFXmodel-A34-531[»]
ProteinModelPortaliQ02318.
SMRiQ02318. Positions 61-529.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni384 – 39815Sterol-bindingSequence AnalysisAdd
BLAST

Sequence similaritiesi

Belongs to the cytochrome P450 family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG2124.
GeneTreeiENSGT00760000119243.
HOGENOMiHOG000253961.
HOVERGENiHBG106909.
InParanoidiQ02318.
KOiK00488.
OMAiQISGYLH.
OrthoDBiEOG7ZGX4B.
PhylomeDBiQ02318.
TreeFamiTF105094.

Family and domain databases

Gene3Di1.10.630.10. 1 hit.
InterProiIPR001128. Cyt_P450.
IPR017972. Cyt_P450_CS.
IPR002401. Cyt_P450_E_grp-I.
[Graphical view]
PfamiPF00067. p450. 1 hit.
[Graphical view]
PRINTSiPR00463. EP450I.
PR00385. P450.
SUPFAMiSSF48264. SSF48264. 1 hit.
PROSITEiPS00086. CYTOCHROME_P450. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q02318-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAALGCARLR WALRGAGRGL CPHGARAKAA IPAALPSDKA TGAPGAGPGV
60 70 80 90 100
RRRQRSLEEI PRLGQLRFFF QLFVQGYALQ LHQLQVLYKA KYGPMWMSYL
110 120 130 140 150
GPQMHVNLAS APLLEQVMRQ EGKYPVRNDM ELWKEHRDQH DLTYGPFTTE
160 170 180 190 200
GHHWYQLRQA LNQRLLKPAE AALYTDAFNE VIDDFMTRLD QLRAESASGN
210 220 230 240 250
QVSDMAQLFY YFALEAICYI LFEKRIGCLQ RSIPEDTVTF VRSIGLMFQN
260 270 280 290 300
SLYATFLPKW TRPVLPFWKR YLDGWNAIFS FGKKLIDEKL EDMEAQLQAA
310 320 330 340 350
GPDGIQVSGY LHFLLASGQL SPREAMGSLP ELLMAGVDTT SNTLTWALYH
360 370 380 390 400
LSKDPEIQEA LHEEVVGVVP AGQVPQHKDF AHMPLLKAVL KETLRLYPVV
410 420 430 440 450
PTNSRIIEKE IEVDGFLFPK NTQFVFCHYV VSRDPTAFSE PESFQPHRWL
460 470 480 490 500
RNSQPATPRI QHPFGSVPFG YGVRACLGRR IAELEMQLLL ARLIQKYKVV
510 520 530
LAPETGELKS VARIVLVPNK KVGLQFLQRQ C
Length:531
Mass (Da):60,235
Last modified:July 1, 1993 - v1
Checksum:i62025EB670DBD8E9
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti20 – 256LCPHGA → SAPTG in CAA42481 (PubMed:7690968).Curated
Sequence conflicti171 – 1711A → R in CAA42481 (PubMed:7690968).Curated
Sequence conflicti359 – 3591E → K in AAO21126 (Ref. 3) Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti145 – 1451G → E in CTX. 1 Publication
VAR_016966
Natural varianti169 – 1691A → V.
Corresponds to variant rs59443548 [ dbSNP | Ensembl ].
VAR_061046
Natural varianti175 – 1751T → M.
Corresponds to variant rs2229381 [ dbSNP | Ensembl ].
VAR_048467
Natural varianti395 – 3951R → C in CTX. 1 Publication
VAR_001303
Natural varianti395 – 3951R → S in CTX. 1 Publication
VAR_012285
Natural varianti405 – 4051R → Q in CTX. 1 Publication
VAR_012286
Natural varianti474 – 4741R → Q in CTX. 1 Publication
VAR_012287
Natural varianti474 – 4741R → W in CTX. 1 Publication
VAR_012288
Natural varianti479 – 4791R → C in CTX. 1 Publication
VAR_001304

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M62401 mRNA. Translation: AAA52142.1.
X59812 mRNA. Translation: CAA42481.1.
AY178622 mRNA. Translation: AAO21126.1.
AK290418 mRNA. Translation: BAF83107.1.
CH471063 Genomic DNA. Translation: EAW70654.1.
BC040430 mRNA. Translation: AAH40430.1.
BC051851 mRNA. Translation: AAH51851.1.
S62709 Genomic DNA. Translation: AAB27199.1.
CCDSiCCDS2423.1.
PIRiA39740.
RefSeqiNP_000775.1. NM_000784.3.
UniGeneiHs.516700.

Genome annotation databases

EnsembliENST00000258415; ENSP00000258415; ENSG00000135929.
GeneIDi1593.
KEGGihsa:1593.
UCSCiuc002viz.4. human.

Polymorphism and mutation databases

BioMutaiCYP27A1.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M62401 mRNA. Translation: AAA52142.1.
X59812 mRNA. Translation: CAA42481.1.
AY178622 mRNA. Translation: AAO21126.1.
AK290418 mRNA. Translation: BAF83107.1.
CH471063 Genomic DNA. Translation: EAW70654.1.
BC040430 mRNA. Translation: AAH40430.1.
BC051851 mRNA. Translation: AAH51851.1.
S62709 Genomic DNA. Translation: AAB27199.1.
CCDSiCCDS2423.1.
PIRiA39740.
RefSeqiNP_000775.1. NM_000784.3.
UniGeneiHs.516700.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1MFXmodel-A34-531[»]
ProteinModelPortaliQ02318.
SMRiQ02318. Positions 61-529.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107965. 1 interaction.
IntActiQ02318. 1 interaction.
STRINGi9606.ENSP00000258415.

Chemistry

BindingDBiQ02318.
ChEMBLiCHEMBL5992.
DrugBankiDB06777. Chenodeoxycholic acid.
DB00169. Cholecalciferol.
DB00153. Ergocalciferol.
DB00082. Pegvisomant.

PTM databases

PhosphoSiteiQ02318.

Polymorphism and mutation databases

BioMutaiCYP27A1.
DMDMi399288.

Proteomic databases

MaxQBiQ02318.
PaxDbiQ02318.
PeptideAtlasiQ02318.
PRIDEiQ02318.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000258415; ENSP00000258415; ENSG00000135929.
GeneIDi1593.
KEGGihsa:1593.
UCSCiuc002viz.4. human.

Organism-specific databases

CTDi1593.
GeneCardsiGC02P219646.
GeneReviewsiCYP27A1.
HGNCiHGNC:2605. CYP27A1.
HPAiHPA059155.
MIMi213700. phenotype.
606530. gene.
neXtProtiNX_Q02318.
Orphaneti909. Cerebrotendinous xanthomatosis.
PharmGKBiPA135.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG2124.
GeneTreeiENSGT00760000119243.
HOGENOMiHOG000253961.
HOVERGENiHBG106909.
InParanoidiQ02318.
KOiK00488.
OMAiQISGYLH.
OrthoDBiEOG7ZGX4B.
PhylomeDBiQ02318.
TreeFamiTF105094.

Enzyme and pathway databases

UniPathwayiUPA00955.
BRENDAi1.14.99.38. 2681.
ReactomeiREACT_11041. Synthesis of bile acids and bile salts via 7alpha-hydroxycholesterol.
REACT_11048. Synthesis of bile acids and bile salts via 27-hydroxycholesterol.
REACT_11053. Synthesis of bile acids and bile salts via 24-hydroxycholesterol.
REACT_13812. Endogenous sterols.
REACT_268413. Defective CYP27A1 causes Cerebrotendinous xanthomatosis (CTX).

Miscellaneous databases

ChiTaRSiCYP27A1. human.
GeneWikiiCYP27A1.
GenomeRNAii1593.
NextBioi6548.
PROiQ02318.
SOURCEiSearch...

Gene expression databases

BgeeiQ02318.
CleanExiHS_CYP27A1.
ExpressionAtlasiQ02318. baseline and differential.
GenevestigatoriQ02318.

Family and domain databases

Gene3Di1.10.630.10. 1 hit.
InterProiIPR001128. Cyt_P450.
IPR017972. Cyt_P450_CS.
IPR002401. Cyt_P450_E_grp-I.
[Graphical view]
PfamiPF00067. p450. 1 hit.
[Graphical view]
PRINTSiPR00463. EP450I.
PR00385. P450.
SUPFAMiSSF48264. SSF48264. 1 hit.
PROSITEiPS00086. CYTOCHROME_P450. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Characterization of human sterol 27-hydroxylase. A mitochondrial cytochrome P-450 that catalyzes multiple oxidation reaction in bile acid biosynthesis."
    Cali J.J., Russell D.W.
    J. Biol. Chem. 266:7774-7778(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Liver.
  2. "Transfected human liver cytochrome P-450 hydroxylates vitamin D analogs at different side-chain positions."
    Guo Y.-D., Strugnell S., Back D.W., Jones G.
    Proc. Natl. Acad. Sci. U.S.A. 90:8668-8672(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Liver.
  3. Zhang H.T., Gong Y.
    Submitted (NOV-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Kidney.
  4. "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.
    , 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: Umbilical cord blood.
  5. 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 and Colon.
  7. "Frameshift and splice-junction mutations in the sterol 27-hydroxylase gene cause cerebrotendinous xanthomatosis in Jews or Moroccan origin."
    Leitersdorf E., Reshef A., Meiner V., Levitzki R., Schwartz S.P., Dann E.J., Berkman N., Cali J.J., Klapholz L., Berginer V.M.
    J. Clin. Invest. 91:2488-2496(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-15.
  8. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  9. "Mutations in the bile acid biosynthetic enzyme sterol 27-hydroxylase underlie cerebrotendinous xanthomatosis."
    Cali J.J., Hsieh C.-L., Francke U., Russell D.W.
    J. Biol. Chem. 266:7779-7783(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS CTX CYS-395 AND CYS-479.
  10. "Identification of new mutations in sterol 27-hydroxylase gene in Japanese patients with cerebrotendinous xanthomatosis (CTX)."
    Kim K.-K., Kubota S., Kuriyama M., Fujiyama J., Bjorkhem I., Eggertsen G., Seyama Y.
    J. Lipid Res. 35:1031-1039(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS CTX GLN-474 AND TRP-474.
  11. "Novel homozygous and compound heterozygous mutations of sterol 27-hydroxylase gene (CYP27) cause cerebrotendinous xanthomatosis in three Japanese patients from two unrelated families."
    Chen W., Kubota S., Kim K.-S., Cheng J., Kuriyama M., Eggertsen G., Bjorkhem I., Seyama Y.
    J. Lipid Res. 38:870-879(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT CTX GLN-405.
  12. "A novel arg362ser mutation in the sterol 27-hydroxylase gene (CYP27): its effects on pre-mRNA splicing and enzyme activity."
    Chen W., Kubota S., Ujike H., Ishihara T., Seyama Y.
    Biochemistry 37:15050-15056(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT CTX SER-395.
  13. "Two novel mutations in the sterol 27-hydroxylase gene causing cerebrotendinous xanthomatosis."
    Lamon-Fava S., Schaefer E.J., Garuti R., Salen G., Calandra S.
    Clin. Genet. 61:185-191(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT CTX GLU-145.

Entry informationi

Entry nameiCP27A_HUMAN
AccessioniPrimary (citable) accession number: Q02318
Secondary accession number(s): A8K303, Q6LDB4, Q86YQ6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: July 1, 1993
Last modified: April 29, 2015
This is version 157 of the entry and version 1 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 2
    Human chromosome 2: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.