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Q32P28 (P3H1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 97. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Prolyl 3-hydroxylase 1

EC=1.14.11.7
Alternative name(s):
Growth suppressor 1
Leucine- and proline-enriched proteoglycan 1
Short name=Leprecan-1
Gene names
Name:LEPRE1
Synonyms:GROS1, P3H1
ORF Names:PSEC0109
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length736 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Basement membrane-associated chondroitin sulfate proteoglycan (CSPG). Has prolyl 3-hydroxylase activity catalyzing the post-translational formation of 3-hydroxyproline in -Xaa-Pro-Gly- sequences in collagens, especially types IV and V. May be involved in the secretory pathway of cells. Has growth suppressive activity in fibroblasts. Ref.1

Catalytic activity

L-proline-[procollagen] + 2-oxoglutarate + O2 = trans-3-hydroxy-L-proline-[procollagen] + succinate + CO2.

Cofactor

Iron By similarity.

Ascorbate By similarity.

Subcellular location

Isoform 1: Endoplasmic reticulum Ref.7.

Secretedextracellular spaceextracellular matrix By similarity. Note: Secreted into the extracellular matrix as a chondroitin sulfate proteoglycan (CSPG). Ref.7

Post-translational modification

O-glycosylated; chondroitin sulfate By similarity.

Involvement in disease

Osteogenesis imperfecta 8 (OI8) [MIM:610915]: A form of osteogenesis imperfecta, a connective tissue disorder characterized by low bone mass, bone fragility and susceptibility to fractures after minimal trauma. Disease severity ranges from very mild forms without fractures to intrauterine fractures and perinatal lethality. Extraskeletal manifestations, which affect a variable number of patients, are dentinogenesis imperfecta, hearing loss, and blue sclerae. OI8 is characterized by disproportionate short stature, severe osteoporosis, shortening of the long bones, white sclerae, a round face and a short barrel-shaped chest.
Note: The disease is caused by mutations affecting the gene represented in this entry. A splice site mutation leading to the absence of isoform 1 has been reported in 2 OI8 patients. Isoform 1 is the only form predicted to be located in the endoplasmic reticulum, which the appropriate location for the catalysis of collagen hydroxylation. These patients show indeed severely reduced COL1A1 hydroxylation (Ref.7). Ref.6 Ref.7

Sequence similarities

Belongs to the leprecan family.

Contains 1 Fe2OG dioxygenase domain.

Contains 4 TPR repeats.

Sequence caution

The sequence AAH15309.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

The sequence BAB15256.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Ontologies

Keywords
   Cellular componentEndoplasmic reticulum
Extracellular matrix
Secreted
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseDwarfism
Osteogenesis imperfecta
   DomainCoiled coil
Repeat
Signal
TPR repeat
   LigandIron
Metal-binding
Vitamin C
   Molecular functionDioxygenase
Oxidoreductase
   PTMGlycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processbone development

Inferred from mutant phenotype Ref.6PubMed 22615817. Source: UniProt

cell growth

Inferred from electronic annotation. Source: Ensembl

chaperone-mediated protein folding

Inferred from sequence or structural similarity PubMed 15044469. Source: UniProt

collagen fibril organization

Inferred from electronic annotation. Source: Ensembl

collagen metabolic process

Inferred from sequence or structural similarity PubMed 15044469. Source: UniProt

extracellular matrix organization

Traceable author statement. Source: Reactome

negative regulation of cell proliferation

Non-traceable author statement Ref.1. Source: UniProtKB

negative regulation of post-translational protein modification

Inferred from mutant phenotype Ref.6PubMed 22615817. Source: UniProt

peptidyl-proline hydroxylation

Inferred from sequence or structural similarity PubMed 15044469. Source: GOC

protein folding

Inferred from mutant phenotype Ref.6. Source: UniProt

protein hydroxylation

Inferred from mutant phenotype Ref.6. Source: UniProt

protein stabilization

Inferred from mutant phenotype PubMed 19846465PubMed 22615817. Source: UniProt

regulation of ossification

Inferred from electronic annotation. Source: Ensembl

regulation of protein secretion

Inferred from mutant phenotype Ref.6. Source: UniProt

   Cellular_componentendoplasmic reticulum

Inferred from direct assay PubMed 19846465PubMed 20089953. Source: UniProt

endoplasmic reticulum lumen

Traceable author statement. Source: Reactome

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867. Source: UniProt

macromolecular complex

Inferred from sequence or structural similarity PubMed 15044469. Source: UniProt

nucleus

Inferred from electronic annotation. Source: Ensembl

proteinaceous extracellular matrix

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionL-ascorbic acid binding

Inferred from electronic annotation. Source: UniProtKB-KW

iron ion binding

Inferred from electronic annotation. Source: InterPro

procollagen-proline 3-dioxygenase activity

Inferred from sequence or structural similarity PubMed 15044469. Source: UniProt

protein complex binding

Inferred from sequence or structural similarity PubMed 15044469. Source: UniProt

Complete GO annotation...

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q32P28-1)

Also known as: GROS1-L; LEPREa; P3H1a;

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.
Isoform 2 (identifier: Q32P28-2)

Also known as: GROS1-S;

The sequence of this isoform differs from the canonical sequence as follows:
     361-363: SAK → QGT
     364-736: Missing.
Isoform 3 (identifier: Q32P28-3)

Also known as: LEPREc;

The sequence of this isoform differs from the canonical sequence as follows:
     686-736: DRVQADDLVK...GSESKPKDEL → VRAARAGESS...NLPCPLGSSS
Note: No experimental confirmation available.
Isoform 4 (identifier: Q32P28-4)

Also known as: LEPREb; P3H1b;

The sequence of this isoform differs from the canonical sequence as follows:
     686-736: DRVQADDLVKMLFSPEEMDLSQEQPLDAQQGPPEPAQESLSGSESKPKDEL → VRAARAGQGAGR

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2222 Potential
Chain23 – 736714Prolyl 3-hydroxylase 1
PRO_0000240352

Regions

Repeat35 – 6834TPR 1
Repeat143 – 17634TPR 2
Repeat205 – 23834TPR 3
Repeat301 – 33434TPR 4
Domain564 – 678115Fe2OG dioxygenase
Coiled coil401 – 43939 Potential
Motif733 – 7364Prevents secretion from ER Potential

Sites

Active site6691 By similarity
Metal binding5871Iron
Metal binding5891Iron
Metal binding6591Iron

Amino acid modifications

Glycosylation3161N-linked (GlcNAc...) Potential
Glycosylation4671N-linked (GlcNAc...) Potential
Glycosylation5401N-linked (GlcNAc...) Ref.8

Natural variations

Alternative sequence361 – 3633SAK → QGT in isoform 2.
VSP_019346
Alternative sequence364 – 736373Missing in isoform 2.
VSP_019347
Alternative sequence686 – 73651DRVQA…PKDEL → VRAARAGESSWCCGDPFPER PWFAFLFPKSHCQWLRHERS TWDTSSNALSLWSHCLVLPG PAVNGIQVGKEVKTGSDAEF LVPSLGPTSAVLFQRVGPAG KEMSLGPLRNLPCPLGSSS in isoform 3.
VSP_019348
Alternative sequence686 – 73651DRVQA…PKDEL → VRAARAGQGAGR in isoform 4.
VSP_054864
Natural variant3491G → R.
Corresponds to variant rs6700677 [ dbSNP | Ensembl ].
VAR_033252
Natural variant5061P → R.
Corresponds to variant rs3738501 [ dbSNP | Ensembl ].
VAR_033253
Natural variant5491M → I.
Corresponds to variant rs11581921 [ dbSNP | Ensembl ].
VAR_033254
Natural variant6441Q → K.
Corresponds to variant rs3738497 [ dbSNP | Ensembl ].
VAR_050442

Experimental info

Sequence conflict1021A → G in AAG31018. Ref.1
Sequence conflict1021A → G in AAG31019. Ref.1
Sequence conflict3211V → G in AAG31018. Ref.1
Sequence conflict3211V → G in AAG31019. Ref.1
Sequence conflict3961E → G in BAB55264. Ref.2
Sequence conflict4691S → Y in AAG31019. Ref.1
Sequence conflict6051P → L in BAB15256. Ref.2
Sequence conflict7111L → M in BAB55291. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (GROS1-L) (LEPREa) (P3H1a) [UniParc].

Last modified June 27, 2006. Version 2.
Checksum: EA1909828FAE685E

FASTA73683,394
        10         20         30         40         50         60 
MAVRALKLLT TLLAVVAAAS QAEVESEAGW GMVTPDLLFA EGTAAYARGD WPGVVLSMER 

        70         80         90        100        110        120 
ALRSRAALRA LRLRCRTQCA ADFPWELDPD WSPSPAQASG AAALRDLSFF GGLLRRAACL 

       130        140        150        160        170        180 
RRCLGPPAAH SLSEEMELEF RKRSPYNYLQ VAYFKINKLE KAVAAAHTFF VGNPEHMEMQ 

       190        200        210        220        230        240 
QNLDYYQTMS GVKEADFKDL ETQPHMQEFR LGVRLYSEEQ PQEAVPHLEA ALQEYFVAYE 

       250        260        270        280        290        300 
ECRALCEGPY DYDGYNYLEY NADLFQAITD HYIQVLNCKQ NCVTELASHP SREKPFEDFL 

       310        320        330        340        350        360 
PSHYNYLQFA YYNIGNYTQA VECAKTYLLF FPNDEVMNQN LAYYAAMLGE EHTRSIGPRE 

       370        380        390        400        410        420 
SAKEYRQRSL LEKELLFFAY DVFGIPFVDP DSWTPEEVIP KRLQEKQKSE RETAVRISQE 

       430        440        450        460        470        480 
IGNLMKEIET LVEEKTKESL DVSRLTREGG PLLYEGISLT MNSKLLNGSQ RVVMDGVISD 

       490        500        510        520        530        540 
HECQELQRLT NVAATSGDGY RGQTSPHTPN EKFYGVTVFK ALKLGQEGKV PLQSAHLYYN 

       550        560        570        580        590        600 
VTEKVRRIME SYFRLDTPLY FSYSHLVCRT AIEEVQAERK DDSHPVHVDN CILNAETLVC 

       610        620        630        640        650        660 
VKEPPAYTFR DYSAILYLNG DFDGGNFYFT ELDAKTVTAE VQPQCGRAVG FSSGTENPHG 

       670        680        690        700        710        720 
VKAVTRGQRC AIALWFTLDP RHSERDRVQA DDLVKMLFSP EEMDLSQEQP LDAQQGPPEP 

       730 
AQESLSGSES KPKDEL 

« Hide

Isoform 2 (GROS1-S) [UniParc].

Checksum: 5B1837D6923D9C4A
Show »

FASTA36341,215
Isoform 3 (LEPREc) [UniParc].

Checksum: DF635702F430A113
Show »

FASTA80490,616
Isoform 4 (LEPREb) (P3H1b) [UniParc].

Checksum: DF642E0B7E26E7F3
Show »

FASTA69778,922

References

« Hide 'large scale' references
[1]"Gros1, a potential growth suppressor on chromosome 1: its identity to basement membrane-associated proteoglycan, leprecan."
Kaul S.C., Sugihara T., Yoshida A., Nomura H., Wadhwa R.
Oncogene 19:3576-3583(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION.
Tissue: Testis.
[2]"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] (ISOFORMS 1 AND 3).
Tissue: Epithelium and Teratocarcinoma.
[3]"Signal sequence and keyword trap in silico for selection of full-length human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA libraries."
Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J., Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S., Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y. expand/collapse author list , Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S., Isogai T.
DNA Res. 12:117-126(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Teratocarcinoma.
[4]"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] (ISOFORMS 1 AND 4).
Tissue: Duodenum and Testis.
[5]"Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 347-736 (ISOFORM 1).
[6]"Prolyl 3-hydroxylase 1 deficiency causes a recessive metabolic bone disorder resembling lethal/severe osteogenesis imperfecta."
Cabral W.A., Chang W., Barnes A.M., Weis M., Scott M.A., Leikin S., Makareeva E., Kuznetsova N.V., Rosenbaum K.N., Tifft C.J., Bulas D.I., Kozma C., Smith P.A., Eyre D.R., Marini J.C.
Nat. Genet. 39:359-365(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN OI8.
[7]"Recessive osteogenesis imperfecta caused by LEPRE1 mutations: clinical documentation and identification of the splice form responsible for prolyl 3-hydroxylation."
Willaert A., Malfait F., Symoens S., Gevaert K., Kayserili H., Megarbane A., Mortier G., Leroy J.G., Coucke P.J., De Paepe A.
J. Med. Genet. 46:233-241(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN OI8, SUBCELLULAR LOCATION, ALTERNATIVE SPLICING (ISOFORMS 1; 3 AND 4).
[8]"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-540.
Tissue: Liver.
[9]"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].
+Additional computationally mapped references.

Web resources

Osteogenesis imperfecta variant database

Prolyl 3-hydroxylase 1 (LEPRE1)

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF097431 mRNA. Translation: AAG31018.1.
AF097432 mRNA. Translation: AAG31019.1.
AK025841 mRNA. Translation: BAB15256.1. Different initiation.
AK027648 mRNA. Translation: BAB55264.1.
AK027680 mRNA. Translation: BAB55291.1.
AK027697 mRNA. Translation: BAB55305.1.
AK075418 mRNA. Translation: BAC11608.1.
BC015309 mRNA. Translation: AAH15309.2. Different initiation.
BC108311 mRNA. Translation: AAI08312.1.
BT007039 mRNA. Translation: AAP35688.1.
CCDSCCDS472.2. [Q32P28-1]
CCDS57986.1. [Q32P28-3]
RefSeqNP_001139761.1. NM_001146289.1.
NP_001230175.1. NM_001243246.1. [Q32P28-3]
NP_071751.3. NM_022356.3. [Q32P28-1]
UniGeneHs.720014.

3D structure databases

ProteinModelPortalQ32P28.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid122098. 50 interactions.
IntActQ32P28. 7 interactions.
MINTMINT-4537432.

Chemistry

DrugBankDB00172. L-Proline.
DB00139. Succinic acid.
DB00126. Vitamin C.

PTM databases

PhosphoSiteQ32P28.

Polymorphism databases

DMDM109892809.

Proteomic databases

MaxQBQ32P28.
PaxDbQ32P28.
PRIDEQ32P28.

Protocols and materials databases

DNASU64175.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000236040; ENSP00000236040; ENSG00000117385. [Q32P28-3]
ENST00000296388; ENSP00000296388; ENSG00000117385. [Q32P28-1]
ENST00000397054; ENSP00000380245; ENSG00000117385.
GeneID64175.
KEGGhsa:64175.
UCSCuc001chv.2. human. [Q32P28-1]
uc001chw.2. human. [Q32P28-3]
uc001chy.4. human. [Q32P28-2]

Organism-specific databases

CTD64175.
GeneCardsGC01M043185.
HGNCHGNC:19316. LEPRE1.
HPAHPA012113.
HPA016980.
MIM610339. gene.
610915. phenotype.
neXtProtNX_Q32P28.
Orphanet216804. Osteogenesis imperfecta type 2.
216812. Osteogenesis imperfecta type 3.
PharmGKBPA134930599.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG269251.
HOVERGENHBG053224.
KOK08134.
OMAFNYLQFS.
OrthoDBEOG7BZVSS.
PhylomeDBQ32P28.
TreeFamTF320837.

Enzyme and pathway databases

ReactomeREACT_118779. Extracellular matrix organization.

Gene expression databases

ArrayExpressQ32P28.
BgeeQ32P28.
GenevestigatorQ32P28.

Family and domain databases

Gene3D1.25.40.10. 2 hits.
InterProIPR005123. Oxoglu/Fe-dep_dioxygenase.
IPR006620. Pro_4_hyd_alph.
IPR011990. TPR-like_helical.
[Graphical view]
PfamPF13640. 2OG-FeII_Oxy_3. 1 hit.
[Graphical view]
SMARTSM00702. P4Hc. 1 hit.
[Graphical view]
PROSITEPS00014. ER_TARGET. 1 hit.
PS51471. FE2OG_OXY. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSLEPRE1. human.
GenomeRNAi64175.
NextBio66095.
PROQ32P28.
SOURCESearch...

Entry information

Entry nameP3H1_HUMAN
AccessionPrimary (citable) accession number: Q32P28
Secondary accession number(s): Q7KZR4 expand/collapse secondary AC list , Q96BR8, Q96SK8, Q96SL5, Q96SN3, Q9H6K3, Q9HC86, Q9HC87
Entry history
Integrated into UniProtKB/Swiss-Prot: June 27, 2006
Last sequence update: June 27, 2006
Last modified: July 9, 2014
This is version 97 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

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 1

Human chromosome 1: entries, gene names and cross-references to MIM