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P16435 (NCPR_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 168. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
NADPH--cytochrome P450 reductase

Short name=CPR
Short name=P450R
EC=1.6.2.4
Gene names
Name:POR
Synonyms:CYPOR
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length677 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

This enzyme is required for electron transfer from NADP to cytochrome P450 in microsomes. It can also provide electron transfer to heme oxygenase and cytochrome B5.

Catalytic activity

NADPH + n oxidized hemoprotein = NADP+ + n reduced hemoprotein.

Cofactor

FAD.

FMN.

Subcellular location

Endoplasmic reticulum membrane; Peripheral membrane protein. Note: Anchored to the ER membrane by its N-terminal hydrophobic region.

Involvement in disease

Antley-Bixler syndrome, with genital anomalies and disordered steroidogenesis (ABS1) [MIM:201750]: A disease characterized by the association of Antley-Bixler syndrome with steroidogenesis defects and abnormal genitalia. Antley-Bixler syndrome is characterized by craniosynostosis, radiohumeral synostosis present from the perinatal period, midface hypoplasia, choanal stenosis or atresia, femoral bowing and multiple joint contractures.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.10 Ref.11 Ref.13

Disordered steroidogenesis due to cytochrome P450 oxidoreductase deficiency (DISPORD) [MIM:613571]: A disorder resulting in a rare variant of congenital adrenal hyperplasia, with apparent combined P450C17 and P450C21 deficiency and accumulation of steroid metabolites. Affected girls are born with ambiguous genitalia, but their circulating androgens are low and virilization does not progress. Conversely, affected boys are sometimes born undermasculinized. Boys and girls can present with bone malformations, in some cases resembling the pattern seen in patients with Antley-Bixler syndrome.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.12 Ref.13

Sequence similarities

In the C-terminal section; belongs to the flavoprotein pyridine nucleotide cytochrome reductase family.

Contains 1 FAD-binding FR-type domain.

Contains 1 flavodoxin-like domain.

Sequence caution

The sequence AAH34277.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
   Cellular componentEndoplasmic reticulum
Membrane
   Coding sequence diversityPolymorphism
   DiseaseCongenital adrenal hyperplasia
Craniosynostosis
Disease mutation
   LigandFAD
Flavoprotein
FMN
NADP
   Molecular functionOxidoreductase
   PTMAcetylation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processcarnitine metabolic process

Inferred from electronic annotation. Source: Ensembl

cellular organofluorine metabolic process

Inferred from direct assay PubMed 19448135. Source: BHF-UCL

cellular response to follicle-stimulating hormone stimulus

Inferred from electronic annotation. Source: Ensembl

cellular response to peptide hormone stimulus

Inferred from electronic annotation. Source: Ensembl

demethylation

Inferred from electronic annotation. Source: Ensembl

fatty acid oxidation

Inferred from electronic annotation. Source: Ensembl

flavonoid metabolic process

Inferred from electronic annotation. Source: Ensembl

internal peptidyl-lysine acetylation

Inferred from electronic annotation. Source: Ensembl

negative regulation of apoptotic process

Inferred from electronic annotation. Source: Ensembl

negative regulation of cysteine-type endopeptidase activity involved in apoptotic process

Inferred from electronic annotation. Source: Ensembl

negative regulation of lipase activity

Inferred from electronic annotation. Source: Ensembl

nitrate catabolic process

Inferred from electronic annotation. Source: Ensembl

nitric oxide catabolic process

Inferred from electronic annotation. Source: Ensembl

oxidation-reduction process

Traceable author statement Ref.9. Source: UniProtKB

positive regulation of cholesterol biosynthetic process

Inferred from electronic annotation. Source: Ensembl

positive regulation of chondrocyte differentiation

Inferred from electronic annotation. Source: Ensembl

positive regulation of monooxygenase activity

Inferred from direct assay PubMed 19448135. Source: BHF-UCL

positive regulation of smoothened signaling pathway

Inferred from electronic annotation. Source: Ensembl

positive regulation of steroid hormone biosynthetic process

Inferred from electronic annotation. Source: Ensembl

regulation of growth plate cartilage chondrocyte proliferation

Inferred from electronic annotation. Source: Ensembl

response to drug

Inferred from electronic annotation. Source: Ensembl

response to nutrient

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentendoplasmic reticulum membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

intracellular membrane-bounded organelle

Inferred from direct assay PubMed 9618440. Source: UniProtKB

mitochondrion

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionFMN binding

Inferred from electronic annotation. Source: Ensembl

NADP binding

Inferred from electronic annotation. Source: Ensembl

NADPH-hemoprotein reductase activity

Traceable author statement Ref.9Ref.7. Source: UniProtKB

cytochrome-b5 reductase activity, acting on NAD(P)H

Inferred from electronic annotation. Source: Ensembl

electron carrier activity

Inferred from electronic annotation. Source: Ensembl

flavin adenine dinucleotide binding

Inferred from electronic annotation. Source: Ensembl

hydrolase activity

Inferred from electronic annotation. Source: Ensembl

iron ion binding

Inferred from electronic annotation. Source: InterPro

iron-cytochrome-c reductase activity

Inferred from electronic annotation. Source: Ensembl

nitric oxide dioxygenase activity

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

CYP2C2P001814EBI-726554,EBI-4320576From a different organism.
PGRMC1O002645EBI-726554,EBI-1045534

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.7
Chain2 – 677676NADPH--cytochrome P450 reductase
PRO_0000167596

Regions

Domain80 – 224145Flavodoxin-like
Domain279 – 521243FAD-binding FR-type
Nucleotide binding170 – 20132FMN By similarity
Nucleotide binding314 – 32512FAD By similarity
Nucleotide binding451 – 46111FAD By similarity
Nucleotide binding529 – 54719NADP By similarity
Nucleotide binding623 – 63917NADP By similarity

Amino acid modifications

Modified residue21N-acetylglycine

Natural variations

Natural variant1781Y → D in DISPORD; complete loss of activity. Ref.12
VAR_021154
Natural variant2251P → L. Ref.4 Ref.6
VAR_047885
Natural variant2521D → N. Ref.4
VAR_047886
Natural variant2841A → P in ABS1 and DISPORD; significant reduction of activity. Ref.12 Ref.13
VAR_021155
Natural variant4541R → H in ABS1 and DISPORD; significant reduction of activity. Ref.10 Ref.11 Ref.12 Ref.13
VAR_021156
Natural variant4891V → E in ABS1; significant reduction of activity. Ref.13
VAR_021157
Natural variant5001A → V. Ref.1 Ref.4 Ref.6 Ref.11
Corresponds to variant rs1057868 [ dbSNP | Ensembl ].
VAR_004617
Natural variant5511R → Q.
VAR_004618
Natural variant5661C → Y in DISPORD; significant reduction of activity. Ref.12 Ref.13
VAR_021158
Natural variant5751Y → C in ABS1. Ref.11
VAR_021159
Natural variant6051V → F in DISPORD; significant reduction of activity. Ref.13
VAR_021160
Natural variant609 – 6179LKQDREHLW → R in ABS1.
VAR_021161

Experimental info

Sequence conflict4051M → L in BAB18572. Ref.3
Sequence conflict5181F → L in AAB21814. Ref.1
Sequence conflict5181F → L in BAB18572. Ref.3
Sequence conflict537 – 5382VA → WH in AAB21814. Ref.1

Secondary structure

................................................................................................................. 677
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P16435 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 2F7D4B9CDFDF5A74

FASTA67776,690
        10         20         30         40         50         60 
MGDSHVDTSS TVSEAVAEEV SLFSMTDMIL FSLIVGLLTY WFLFRKKKEE VPEFTKIQTL 

        70         80         90        100        110        120 
TSSVRESSFV EKMKKTGRNI IVFYGSQTGT AEEFANRLSK DAHRYGMRGM SADPEEYDLA 

       130        140        150        160        170        180 
DLSSLPEIDN ALVVFCMATY GEGDPTDNAQ DFYDWLQETD VDLSGVKFAV FGLGNKTYEH 

       190        200        210        220        230        240 
FNAMGKYVDK RLEQLGAQRI FELGLGDDDG NLEEDFITWR EQFWPAVCEH FGVEATGEES 

       250        260        270        280        290        300 
SIRQYELVVH TDIDAAKVYM GEMGRLKSYE NQKPPFDAKN PFLAAVTTNR KLNQGTERHL 

       310        320        330        340        350        360 
MHLELDISDS KIRYESGDHV AVYPANDSAL VNQLGKILGA DLDVVMSLNN LDEESNKKHP 

       370        380        390        400        410        420 
FPCPTSYRTA LTYYLDITNP PRTNVLYELA QYASEPSEQE LLRKMASSSG EGKELYLSWV 

       430        440        450        460        470        480 
VEARRHILAI LQDCPSLRPP IDHLCELLPR LQARYYSIAS SSKVHPNSVH ICAVVVEYET 

       490        500        510        520        530        540 
KAGRINKGVA TNWLRAKEPA GENGGRALVP MFVRKSQFRL PFKATTPVIM VGPGTGVAPF 

       550        560        570        580        590        600 
IGFIQERAWL RQQGKEVGET LLYYGCRRSD EDYLYREELA QFHRDGALTQ LNVAFSREQS 

       610        620        630        640        650        660 
HKVYVQHLLK QDREHLWKLI EGGAHIYVCG DARNMARDVQ NTFYDIVAEL GAMEHAQAVD 

       670 
YIKKLMTKGR YSLDVWS 

« Hide

References

« Hide 'large scale' references
[1]"Quantification of cytochrome P450 reductase gene expression in human tissues."
Shephard E.A., Palmer C.N., Segall H.J., Phillips I.R.
Arch. Biochem. Biophys. 294:168-172(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT VAL-500.
[2]"Polymorphism of human CYPOR: expression of new allele."
Czerwinski M., Sahni M., Madan A., Parkinson A.
Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Liver.
[3]"cDNA cloning and characterization of NADPH-cytochrome P-450 reductase in human HL-60 cell."
Murakami H.O., Ogawa H., Nisimoto Y.
Submitted (NOV-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[4]NIEHS SNPs program
Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS LEU-225; ASN-252 AND VAL-500.
[5]"The DNA sequence of human chromosome 7."
Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L. expand/collapse author list , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract]
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], VARIANTS LEU-225 AND VAL-500.
Tissue: Lung.
[7]"Structural and functional analysis of NADPH-cytochrome P-450 reductase from human liver: complete sequence of human enzyme and NADPH-binding sites."
Haniu M., McManus M.E., Birkett D.J., Lee T.D., Shively J.E.
Biochemistry 28:8639-8645(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-677.
Tissue: Liver.
[8]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[9]"Crystal structure of the FMN-binding domain of human cytochrome P450 reductase at 1.93 A resolution."
Zhao Q., Modi S., Smith G., Paine M., McDonagh P.D., Wolf C.R., Tew D., Lian L.Y., Roberts G.C., Driessen H.P.
Protein Sci. 8:298-306(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.93 ANGSTROMS) OF 62-242.
[10]"Compound heterozygous mutations of cytochrome P450 oxidoreductase gene (POR) in two patients with Antley-Bixler syndrome."
Adachi M., Tachibana K., Asakura Y., Yamamoto T., Hanaki K., Oka A.
Am. J. Med. Genet. A 128:333-339(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT ABS1 HIS-454.
[11]"Cytochrome P450 oxidoreductase gene mutations and Antley-Bixler syndrome with abnormal genitalia and/or impaired steroidogenesis: molecular and clinical studies in 10 patients."
Fukami M., Horikawa R., Nagai T., Tanaka T., Naiki Y., Sato N., Okuyama T., Nakai H., Soneda S., Tachibana K., Matsuo N., Sato S., Homma K., Nishimura G., Hasegawa T., Ogata T.
J. Clin. Endocrinol. Metab. 90:414-426(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS ABS1 HIS-454; CYS-575 AND 608-LEU--TRP-617 DELINS ARG, VARIANT VAL-500.
[12]"Congenital adrenal hyperplasia caused by mutant P450 oxidoreductase and human androgen synthesis: analytical study."
Arlt W., Walker E.A., Draper N., Ivison H.E., Ride J.P., Hammer F., Chalder S.M., Borucka-Mankiewicz M., Hauffa B.P., Malunowicz E.M., Stewart P.M., Shackleton C.H.L.
Lancet 363:2128-2135(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS DISPORD ASP-178; PRO-284; HIS-454 AND TYR-566, CHARACTERIZATION OF VARIANTS DISPORD ASP-178; PRO-284; HIS-454 AND TYR-566.
[13]"Mutant P450 oxidoreductase causes disordered steroidogenesis with and without Antley-Bixler syndrome."
Flueck C.E., Tajima T., Pandey A.V., Arlt W., Okuhara K., Verge C.F., Jabs E.W., Mendonca B.B., Fujieda K., Miller W.L.
Nat. Genet. 36:228-230(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS ABS1 PRO-284; HIS-454 AND GLU-489, VARIANTS DISPORD TYR-566 AND PHE-605, CHARACTERIZATION OF VARIANTS ABS1 PRO-284; HIS-454 AND GLU-489, CHARACTERIZATION OF VARIANTS DISPORD TYR-566 AND PHE-605.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
S90469 mRNA. Translation: AAB21814.1.
AF258341 mRNA. Translation: AAG09798.1.
AB051763 mRNA. Translation: BAB18572.1.
DQ640499 Genomic DNA. Translation: ABF70199.1.
AC005067 Genomic DNA. Translation: AAD45961.1.
AC006330 Genomic DNA. No translation available.
BC034277 mRNA. Translation: AAH34277.1. Different initiation.
PIRA60557. A33421.
RefSeqNP_000932.3. NM_000941.2.
UniGeneHs.354056.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1B1CX-ray1.93A61-241[»]
3FJOX-ray2.50A232-677[»]
3QE2X-ray1.75A/B64-677[»]
3QFCX-ray1.80A/B64-677[»]
3QFRX-ray2.40A/B64-677[»]
3QFSX-ray1.40A241-677[»]
3QFTX-ray1.40A241-677[»]
ProteinModelPortalP16435.
SMRP16435. Positions 66-677.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111443. 15 interactions.
DIPDIP-29682N.
IntActP16435. 5 interactions.
MINTMINT-1212161.
STRING9606.ENSP00000265302.

Chemistry

ChEMBLCHEMBL2169731.
DrugBankDB00865. Benzphetamine.
DB00694. Daunorubicin.
DB00166. Lipoic Acid.
DB00170. Menadione.
DB01028. Methoxyflurane.
DB00305. Mitomycin.
DB00665. Nilutamide.

PTM databases

PhosphoSiteP16435.

Polymorphism databases

DMDM2851393.

Proteomic databases

PaxDbP16435.
PRIDEP16435.

Protocols and materials databases

DNASU5447.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000394893; ENSP00000378355; ENSG00000127948.
ENST00000412064; ENSP00000404731; ENSG00000127948.
ENST00000412521; ENSP00000409238; ENSG00000127948.
ENST00000414186; ENSP00000399327; ENSG00000127948.
ENST00000418341; ENSP00000389719; ENSG00000127948.
ENST00000432753; ENSP00000389409; ENSG00000127948.
ENST00000439963; ENSP00000390540; ENSG00000127948.
ENST00000449920; ENSP00000399556; ENSG00000127948.
ENST00000453773; ENSP00000395813; ENSG00000127948.
ENST00000454934; ENSP00000414263; ENSG00000127948.
ENST00000461988; ENSP00000419970; ENSG00000127948.
GeneID5447.
KEGGhsa:5447.
UCSCuc011kge.2. human.

Organism-specific databases

CTD5447.
GeneCardsGC07P075528.
HGNCHGNC:9208. POR.
HPACAB004372.
HPA010136.
MIM124015. gene.
201750. phenotype.
613571. phenotype.
neXtProtNX_P16435.
Orphanet95699. Congenital adrenal hyperplasia due to cytochrome P450 oxidoreductase deficiency.
PharmGKBPA33532.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0369.
HOGENOMHOG000282027.
HOVERGENHBG000432.
InParanoidP16435.
KOK00327.
OrthoDBEOG7HQN7J.
PhylomeDBP16435.
TreeFamTF105719.

Enzyme and pathway databases

BioCycMetaCyc:HS05140-MONOMER.
SABIO-RKP16435.

Gene expression databases

ArrayExpressP16435.
BgeeP16435.
CleanExHS_POR.
GenevestigatorP16435.

Family and domain databases

Gene3D1.20.990.10. 1 hit.
InterProIPR003097. FAD-binding_1.
IPR017927. Fd_Rdtase_FAD-bd.
IPR001094. Flavdoxin.
IPR008254. Flavodoxin/NO_synth.
IPR001709. Flavoprot_Pyr_Nucl_cyt_Rdtase.
IPR023173. NADPH_Cyt_P450_Rdtase_dom3.
IPR001433. OxRdtase_FAD/NAD-bd.
IPR023208. P450R.
IPR017938. Riboflavin_synthase-like_b-brl.
[Graphical view]
PfamPF00667. FAD_binding_1. 1 hit.
PF00258. Flavodoxin_1. 1 hit.
PF00175. NAD_binding_1. 1 hit.
[Graphical view]
PIRSFPIRSF000208. P450R. 1 hit.
PRINTSPR00369. FLAVODOXIN.
PR00371. FPNCR.
SUPFAMSSF63380. SSF63380. 1 hit.
PROSITEPS51384. FAD_FR. 1 hit.
PS50902. FLAVODOXIN_LIKE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPOR. human.
EvolutionaryTraceP16435.
GeneWikiCytochrome_P450_reductase.
GenomeRNAi5447.
NextBio21083.
PROP16435.
SOURCESearch...

Entry information

Entry nameNCPR_HUMAN
AccessionPrimary (citable) accession number: P16435
Secondary accession number(s): Q16455 expand/collapse secondary AC list , Q197M5, Q8N181, Q9H3M8, Q9UDT3
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 168 of the entry and version 2 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

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 7

Human chromosome 7: entries, gene names and cross-references to MIM