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Q02318

- CP27A_HUMAN

UniProt

Q02318 - CP27A_HUMAN

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Protein

Sterol 26-hydroxylase, mitochondrial

Gene

CYP27A1

Organism
Homo sapiens (Human)
Status
Reviewed - 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

Heme group.

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

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.
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: 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) [MIM:213700]: Rare sterol storage disorder characterized clinically by progressive neurologic dysfunction, premature atherosclerosis, and cataracts.5 Publications
Note: The disease is caused by mutations affecting the gene represented in this entry.
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.

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

Secondary structure

1
531
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi67 – 715
Helixi83 – 919
Turni92 – 943
Helixi101 – 1033
Helixi111 – 1144
Turni115 – 1173
Turni120 – 1223
Helixi131 – 14010
Beta strandi142 – 1476
Helixi152 – 1609
Turni161 – 1666
Helixi170 – 19021
Helixi207 – 22216
Turni228 – 2303
Helixi236 – 25217
Turni262 – 2643
Helixi266 – 2683
Helixi269 – 29325
Helixi304 – 3107
Turni314 – 3163
Helixi322 – 35332
Helixi355 – 36814
Beta strandi370 – 3756
Helixi377 – 3815
Helixi384 – 39613
Beta strandi404 – 4063
Turni413 – 4153
Helixi428 – 4314
Helixi435 – 4384
Beta strandi439 – 4424
Helixi446 – 4483
Turni449 – 4513
Beta strandi458 – 4603
Helixi464 – 4663
Beta strandi468 – 4703
Beta strandi472 – 4765
Helixi479 – 49618
Beta strandi512 – 5165

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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. 1 PublicationCurated

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:
EMBL
GenBank
DDBJ
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 databases

DMDMi399288.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS2423.1.
PIRi A39740.
RefSeqi NP_000775.1. NM_000784.3.
UniGenei Hs.516700.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1MFX model - A 34-531 [» ]
ProteinModelPortali Q02318.
SMRi Q02318. Positions 61-529.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 107965. 1 interaction.
IntActi Q02318. 1 interaction.
STRINGi 9606.ENSP00000258415.

Chemistry

BindingDBi Q02318.
ChEMBLi CHEMBL5992.
DrugBanki DB06777. Chenodeoxycholic acid.
DB00169. Cholecalciferol.
DB00153. Ergocalciferol.
DB00082. Pegvisomant.

PTM databases

PhosphoSitei Q02318.

Polymorphism databases

DMDMi 399288.

Proteomic databases

MaxQBi Q02318.
PaxDbi Q02318.
PeptideAtlasi Q02318.
PRIDEi Q02318.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000258415 ; ENSP00000258415 ; ENSG00000135929 .
GeneIDi 1593.
KEGGi hsa:1593.
UCSCi uc002viz.4. human.

Organism-specific databases

CTDi 1593.
GeneCardsi GC02P219646.
GeneReviewsi CYP27A1.
HGNCi HGNC:2605. CYP27A1.
HPAi HPA059155.
MIMi 213700. phenotype.
606530. gene.
neXtProti NX_Q02318.
Orphaneti 909. Cerebrotendinous xanthomatosis.
PharmGKBi PA135.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG2124.
GeneTreei ENSGT00760000119243.
HOGENOMi HOG000253961.
HOVERGENi HBG106909.
InParanoidi Q02318.
KOi K00488.
OMAi QISGYLH.
OrthoDBi EOG7ZGX4B.
PhylomeDBi Q02318.
TreeFami TF105094.

Enzyme and pathway databases

UniPathwayi UPA00955 .
Reactomei REACT_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.

Miscellaneous databases

ChiTaRSi CYP27A1. human.
GeneWikii CYP27A1.
GenomeRNAii 1593.
NextBioi 6548.
PROi Q02318.
SOURCEi Search...

Gene expression databases

Bgeei Q02318.
CleanExi HS_CYP27A1.
ExpressionAtlasi Q02318. baseline and differential.
Genevestigatori Q02318.

Family and domain databases

Gene3Di 1.10.630.10. 1 hit.
InterProi IPR001128. Cyt_P450.
IPR017972. Cyt_P450_CS.
IPR002401. Cyt_P450_E_grp-I.
[Graphical view ]
Pfami PF00067. p450. 1 hit.
[Graphical view ]
PRINTSi PR00463. EP450I.
PR00385. P450.
SUPFAMi SSF48264. SSF48264. 1 hit.
PROSITEi PS00086. CYTOCHROME_P450. 1 hit.
[Graphical view ]
ProtoNeti Search...

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. "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.
  9. "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.
  10. "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.
  11. "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.
  12. "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: October 29, 2014
This is version 152 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