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Q13753 (LAMC2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 149. 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:
Laminin subunit gamma-2
Alternative name(s):
Cell-scattering factor 140 kDa subunit
Short name=CSF 140 kDa subunit
Epiligrin subunit gamma
Kalinin subunit gamma
Kalinin/nicein/epiligrin 100 kDa subunit
Ladsin 140 kDa subunit
Laminin B2t chain
Laminin-5 subunit gamma
Large adhesive scatter factor 140 kDa subunit
Nicein subunit gamma
Gene names
Name:LAMC2
Synonyms:LAMB2T, LAMNB2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1193 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Binding to cells via a high affinity receptor, laminin is thought to mediate the attachment, migration and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components. Ladsin exerts cell-scattering activity toward a wide variety of cells, including epithelial, endothelial, and fibroblastic cells. Ref.7

Subunit structure

Laminin is a complex glycoprotein, consisting of three different polypeptide chains (alpha, beta, gamma), which are bound to each other by disulfide bonds into a cross-shaped molecule comprising one long and three short arms with globules at each end. Gamma-2 is a subunit of laminin-5 (laminin-332 or epiligrin/kalinin/nicein).

Subcellular location

Secretedextracellular spaceextracellular matrixbasement membrane. Note: Major component.

Tissue specificity

The large variant is expressed only in specific epithelial cells of embryonic and neonatal tissues. In 17-week old embryo the small variant is found in cerebral cortex, lung, and distal tubes of kidney, but not in epithelia except for distal tubuli.

Domain

The alpha-helical domains I and II are thought to interact with other laminin chains to form a coiled coil structure.

Domain IV is globular.

Involvement in disease

Epidermolysis bullosa, junctional, Herlitz type (H-JEB) [MIM:226700]: An infantile and lethal form of junctional epidermolysis bullosa, a group of blistering skin diseases characterized by tissue separation which occurs within the dermo-epidermal basement In the Herlitz type, death occurs usually within the first six months of life. Occasionally, children survive to teens. It is marked by bullous lesions at birth and extensive denudation of skin and mucous membranes that may be hemorrhagic.
Note: The disease is caused by mutations affecting the gene represented in this entry.

Miscellaneous

Binds heparin By similarity.

Sequence similarities

Contains 8 laminin EGF-like domains.

Contains 1 laminin IV type A domain.

Ontologies

Keywords
   Biological processCell adhesion
   Cellular componentBasement membrane
Extracellular matrix
Secreted
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseEpidermolysis bullosa
   DomainCoiled coil
Laminin EGF-like domain
Repeat
Signal
   LigandHeparin-binding
   PTMDisulfide bond
Glycoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processcell adhesion

Inferred from electronic annotation. Source: UniProtKB-KW

cell junction assembly

Traceable author statement. Source: Reactome

epidermis development

Traceable author statement PubMed 8012394. Source: ProtInc

extracellular matrix disassembly

Traceable author statement. Source: Reactome

extracellular matrix organization

Traceable author statement. Source: Reactome

hemidesmosome assembly

Traceable author statement. Source: Reactome

   Cellular_componentcell cortex

Inferred from electronic annotation. Source: Ensembl

extracellular region

Traceable author statement. Source: Reactome

extracellular space

Inferred from electronic annotation. Source: Ensembl

laminin-2 complex

Inferred from electronic annotation. Source: Ensembl

laminin-5 complex

Inferred from electronic annotation. Source: Ensembl

membrane

Inferred from electronic annotation. Source: Ensembl

perinuclear region of cytoplasm

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionheparin binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform Long (identifier: Q13753-1)

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 Short (identifier: Q13753-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1110-1193: DQPLSVDEEG...CYNTQALEQQ → GM

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2121 Potential
Chain22 – 11931172Laminin subunit gamma-2
PRO_0000017077

Regions

Domain28 – 8356Laminin EGF-like 1
Domain84 – 13047Laminin EGF-like 2
Domain139 – 18648Laminin EGF-like 3
Domain187 – 19610Laminin EGF-like 4; first part
Domain213 – 381169Laminin IV type A
Domain382 – 41534Laminin EGF-like 4; second part
Domain416 – 46146Laminin EGF-like 5
Domain462 – 51655Laminin EGF-like 6
Domain517 – 57256Laminin EGF-like 7
Domain573 – 60230Laminin EGF-like 8; truncated
Region603 – 1193591Domain II and I
Coiled coil611 – 718108 Potential
Coiled coil811 – 1076266 Potential
Coiled coil1117 – 119377 Potential

Amino acid modifications

Glycosylation3421N-linked (GlcNAc...) Potential
Glycosylation3621N-linked (GlcNAc...) Potential
Glycosylation9421N-linked (GlcNAc...) Potential
Glycosylation10331N-linked (GlcNAc...) Potential
Disulfide bond28 ↔ 37 By similarity
Disulfide bond30 ↔ 53 By similarity
Disulfide bond56 ↔ 65 By similarity
Disulfide bond68 ↔ 81 By similarity
Disulfide bond84 ↔ 96 By similarity
Disulfide bond86 ↔ 102 By similarity
Disulfide bond104 ↔ 113 By similarity
Disulfide bond116 ↔ 128 By similarity
Disulfide bond139 ↔ 150 By similarity
Disulfide bond141 ↔ 155 By similarity
Disulfide bond157 ↔ 166 By similarity
Disulfide bond169 ↔ 184 By similarity
Disulfide bond462 ↔ 470 By similarity
Disulfide bond464 ↔ 481 By similarity
Disulfide bond484 ↔ 493 By similarity
Disulfide bond496 ↔ 514 By similarity
Disulfide bond517 ↔ 531 By similarity
Disulfide bond519 ↔ 538 By similarity
Disulfide bond541 ↔ 550 By similarity
Disulfide bond553 ↔ 570 By similarity
Disulfide bond573 ↔ 585 By similarity
Disulfide bond575 ↔ 591 By similarity
Disulfide bond593 ↔ 602 By similarity
Disulfide bond609Interchain Probable
Disulfide bond612Interchain Probable
Disulfide bond1184Interchain Probable

Natural variations

Alternative sequence1110 – 119384DQPLS…ALEQQ → GM in isoform Short.
VSP_003040
Natural variant1111A → P.
Corresponds to variant rs12065473 [ dbSNP | Ensembl ].
VAR_050081
Natural variant1151R → Q.
Corresponds to variant rs17481405 [ dbSNP | Ensembl ].
VAR_050082
Natural variant1241T → M.
Corresponds to variant rs11586699 [ dbSNP | Ensembl ].
VAR_050083
Natural variant1361D → V.
Corresponds to variant rs12037099 [ dbSNP | Ensembl ].
VAR_050084
Natural variant2471D → E.
Corresponds to variant rs2296306 [ dbSNP | Ensembl ].
VAR_022017
Natural variant6081S → I.
Corresponds to variant rs4373715 [ dbSNP | Ensembl ].
VAR_050085
Natural variant7331S → T.
Corresponds to variant rs2296303 [ dbSNP | Ensembl ].
VAR_020304

Experimental info

Sequence conflict121F → L in CAA52108. Ref.2
Sequence conflict4731M → I in CAA78728. Ref.1
Sequence conflict4731M → I in CAA78729. Ref.1
Sequence conflict5211N → S in CAA78728. Ref.1
Sequence conflict5211N → S in CAA78729. Ref.1
Sequence conflict8571R → P in CAA78728. Ref.1
Sequence conflict8571R → P in CAA78729. Ref.1
Sequence conflict8831S → T in AAC50457. Ref.3
Sequence conflict8831S → T in AAC50456. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Isoform Long [UniParc].

Last modified March 7, 2006. Version 2.
Checksum: 0BBE1A56516C5C9A

FASTA1,193130,976
        10         20         30         40         50         60 
MPALWLGCCL CFSLLLPAAR ATSRREVCDC NGKSRQCIFD RELHRQTGNG FRCLNCNDNT 

        70         80         90        100        110        120 
DGIHCEKCKN GFYRHRERDR CLPCNCNSKG SLSARCDNSG RCSCKPGVTG ARCDRCLPGF 

       130        140        150        160        170        180 
HMLTDAGCTQ DQRLLDSKCD CDPAGIAGPC DAGRCVCKPA VTGERCDRCR SGYYNLDGGN 

       190        200        210        220        230        240 
PEGCTQCFCY GHSASCRSSA EYSVHKITST FHQDVDGWKA VQRNGSPAKL QWSQRHQDVF 

       250        260        270        280        290        300 
SSAQRLDPVY FVAPAKFLGN QQVSYGQSLS FDYRVDRGGR HPSAHDVILE GAGLRITAPL 

       310        320        330        340        350        360 
MPLGKTLPCG LTKTYTFRLN EHPSNNWSPQ LSYFEYRRLL RNLTALRIRA TYGEYSTGYI 

       370        380        390        400        410        420 
DNVTLISARP VSGAPAPWVE QCICPVGYKG QFCQDCASGY KRDSARLGPF GTCIPCNCQG 

       430        440        450        460        470        480 
GGACDPDTGD CYSGDENPDI ECADCPIGFY NDPHDPRSCK PCPCHNGFSC SVMPETEEVV 

       490        500        510        520        530        540 
CNNCPPGVTG ARCELCADGY FGDPFGEHGP VRPCQPCQCN NNVDPSASGN CDRLTGRCLK 

       550        560        570        580        590        600 
CIHNTAGIYC DQCKAGYFGD PLAPNPADKC RACNCNPMGS EPVGCRSDGT CVCKPGFGGP 

       610        620        630        640        650        660 
NCEHGAFSCP ACYNQVKIQM DQFMQQLQRM EALISKAQGG DGVVPDTELE GRMQQAEQAL 

       670        680        690        700        710        720 
QDILRDAQIS EGASRSLGLQ LAKVRSQENS YQSRLDDLKM TVERVRALGS QYQNRVRDTH 

       730        740        750        760        770        780 
RLITQMQLSL AESEASLGNT NIPASDHYVG PNGFKSLAQE ATRLAESHVE SASNMEQLTR 

       790        800        810        820        830        840 
ETEDYSKQAL SLVRKALHEG VGSGSGSPDG AVVQGLVEKL EKTKSLAQQL TREATQAEIE 

       850        860        870        880        890        900 
ADRSYQHSLR LLDSVSRLQG VSDQSFQVEE AKRIKQKADS LSSLVTRHMD EFKRTQKNLG 

       910        920        930        940        950        960 
NWKEEAQQLL QNGKSGREKS DQLLSRANLA KSRAQEALSM GNATFYEVES ILKNLREFDL 

       970        980        990       1000       1010       1020 
QVDNRKAEAE EAMKRLSYIS QKVSDASDKT QQAERALGSA AADAQRAKNG AGEALEISSE 

      1030       1040       1050       1060       1070       1080 
IEQEIGSLNL EANVTADGAL AMEKGLASLK SEMREVEGEL ERKELEFDTN MDAVQMVITE 

      1090       1100       1110       1120       1130       1140 
AQKVDTRAKN AGVTIQDTLN TLDGLLHLMD QPLSVDEEGL VLLEQKLSRA KTQINSQLRP 

      1150       1160       1170       1180       1190 
MMSELEERAR QQRGHLHLLE TSIDGILADV KNLENIRDNL PPGCYNTQAL EQQ 

« Hide

Isoform Short [UniParc].

Checksum: 7762993F3D7F89DF
Show »

FASTA1,111121,604

References

« Hide 'large scale' references
[1]"A truncated laminin chain homologous to the B2 chain: structure, spatial expression, and chromosomal assignment."
Kallunki P., Sainio K., Eddy R., Byers M., Kallunki T., Sariola H., Beck K., Hirvonen H., Shows T.B., Tryggvason K.
J. Cell Biol. 119:679-693(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], ALTERNATIVE SPLICING.
Tissue: Fibrosarcoma.
[2]"The 100-kDa chain of nicein/kalinin is a laminin B2 chain variant."
Vailly J., Verrando P., Champliaud M.-F., Gerecke D., Wagman D.W., Baudoin C., Aberdam D., Burgeson R., Bauer E., Ortonne J.-P.
Eur. J. Biochem. 219:209-218(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 1090-1114.
Tissue: Epidermis and Keratinocyte.
[3]"Structure of the human laminin gamma 2 chain gene (LAMC2): alternative splicing with different tissue distribution of two transcripts."
Airenne T., Haakana H., Sainio K., Kallunki T., Kallunki P., Sariola H., Tryggvason K.
Genomics 32:54-64(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING.
Tissue: Placenta.
[4]"The DNA sequence and biological annotation of human chromosome 1."
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. expand/collapse author list , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
Nature 441:315-321(2006) [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 (JUL-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] (ISOFORM SHORT).
Tissue: Cerebellum.
[7]"A large cell-adhesive scatter factor secreted by human gastric carcinoma cells."
Miyazaki K., Kikkawa Y., Nakamura A., Yasumitsu H., Umeda M.
Proc. Natl. Acad. Sci. U.S.A. 90:11767-11771(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE OF 435-449, FUNCTION, HEPARIN-BINDING.
[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].
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z15008 mRNA. Translation: CAA78728.1.
Z15009 mRNA. Translation: CAA78729.1.
X73902 mRNA. Translation: CAA52108.1.
U31201 expand/collapse EMBL AC list , U31178, U31179, U31180, U31181, U31182, U31183, U31184, U31186, U31187, U31188, U31189, U31190, U31191, U31192, U31193, U31194, U31195, U31196, U31197, U31198, U31199 Genomic DNA. Translation: AAC50457.1.
U31200 expand/collapse EMBL AC list , U31178, U31179, U31180, U31181, U31182, U31183, U31184, U31186, U31187, U31188, U31189, U31190, U31191, U31192, U31193, U31194, U31195, U31196, U31197, U31198 Genomic DNA. Translation: AAC50456.1.
AL354953 Genomic DNA. Translation: CAH70980.1.
CH471067 Genomic DNA. Translation: EAW91146.1.
BC113378 mRNA. Translation: AAI13379.1.
PIRA44018.
RefSeqNP_005553.2. NM_005562.2.
NP_061486.2. NM_018891.2.
UniGeneHs.591484.

3D structure databases

ProteinModelPortalQ13753.
SMRQ13753. Positions 6-198, 380-604.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid110112. 5 interactions.
DIPDIP-190N.
IntActQ13753. 1 interaction.
MINTMINT-4053464.
STRING9606.ENSP00000264144.

Chemistry

ChEMBLCHEMBL2364187.

Protein family/group databases

Allergome8331. Hom s Laminin gamma_2.

PTM databases

PhosphoSiteQ13753.

Polymorphism databases

DMDM90185107.

Proteomic databases

PaxDbQ13753.
PeptideAtlasQ13753.
PRIDEQ13753.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000264144; ENSP00000264144; ENSG00000058085. [Q13753-1]
ENST00000493293; ENSP00000432063; ENSG00000058085. [Q13753-2]
GeneID3918.
KEGGhsa:3918.
UCSCuc001gpz.4. human. [Q13753-2]
uc001gqa.2. human. [Q13753-1]

Organism-specific databases

CTD3918.
GeneCardsGC01P183155.
HGNCHGNC:6493. LAMC2.
HPACAB004257.
HPA024638.
MIM150292. gene.
226700. phenotype.
neXtProtNX_Q13753.
Orphanet79402. Generalized junctional epidermolysis bullosa, non-Herlitz type.
79405. Junctional epidermolysis bullosa inversa.
79404. Junctional epidermolysis bullosa, Herlitz type.
PharmGKBPA30281.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG285700.
HOVERGENHBG062127.
InParanoidQ13753.
KOK06246.
OMADRCLPCN.
OrthoDBEOG7SR4KJ.
PhylomeDBQ13753.

Enzyme and pathway databases

ReactomeREACT_111155. Cell-Cell communication.
REACT_118779. Extracellular matrix organization.

Gene expression databases

BgeeQ13753.
CleanExHS_LAMC2.
GenevestigatorQ13753.

Family and domain databases

InterProIPR002049. EGF_laminin.
IPR018031. Laminin_B_subgr.
IPR000034. Laminin_B_type_IV.
[Graphical view]
PfamPF00052. Laminin_B. 1 hit.
PF00053. Laminin_EGF. 7 hits.
[Graphical view]
SMARTSM00180. EGF_Lam. 6 hits.
SM00281. LamB. 1 hit.
[Graphical view]
PROSITEPS00022. EGF_1. 4 hits.
PS01186. EGF_2. 2 hits.
PS01248. EGF_LAM_1. 6 hits.
PS50027. EGF_LAM_2. 6 hits.
PS51115. LAMININ_IVA. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSLAMC2. human.
GeneWikiLaminin,_gamma_2.
GenomeRNAi3918.
NextBio15391.
PMAP-CutDBQ13753.
PROQ13753.
SOURCESearch...

Entry information

Entry nameLAMC2_HUMAN
AccessionPrimary (citable) accession number: Q13753
Secondary accession number(s): Q02536 expand/collapse secondary AC list , Q02537, Q13752, Q14941, Q14DF7, Q5VYE8
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: March 7, 2006
Last modified: April 16, 2014
This is version 149 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