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P55268 (LAMB2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 139. 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·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Laminin subunit beta-2
Alternative name(s):
Laminin B1s chain
Laminin-11 subunit beta
Laminin-14 subunit beta
Laminin-15 subunit beta
Laminin-3 subunit beta
Laminin-4 subunit beta
Laminin-7 subunit beta
Laminin-9 subunit beta
S-laminin subunit beta
Short name=S-LAM beta
Gene names
Name:LAMB2
Synonyms:LAMS
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1798 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.

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. Beta-2 is a subunit of laminin-3 (laminin-121 or S-laminin), laminin-4 (laminin-221 or S-merosin), laminin-7 (laminin-321 or KS-laminin), laminin-9 (laminin-421), laminin-11 (laminin-521), laminin-14 (laminin-423) and laminin-15 (laminin-523).

Subcellular location

Secretedextracellular spaceextracellular matrixbasement membrane. Note: S-laminin is concentrated in the synaptic cleft of the neuromuscular junction.

Domain

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

Domains VI and IV are globular.

Involvement in disease

Pierson syndrome (PIERSS) [MIM:609049]: Characterized by nephrotic syndrome with neonatal onset, diffuse mesangial sclerosis and eye abnormalities with microcoria as the leading clinical feature. Death usually occurs within the first weeks of life. Disease severity depends on the mutation type: nontruncating LAMB2 mutations may display variable phenotypes ranging from a milder variant of Pierson syndrome to isolated congenital nephrotic syndrome.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.5 Ref.6

Nephrotic syndrome 5 with or without ocular abnormalities (NPHS5) [MIM:614199]: A form of nephrotic syndrome, a renal disease clinically characterized by severe proteinuria, resulting in complications such as hypoalbuminemia, hyperlipidemia and edema. Kidney biopsies show non-specific histologic changes such as focal segmental glomerulosclerosis and diffuse mesangial proliferation. Some affected individuals have an inherited steroid-resistant form and progress to end-stage renal failure. NPHS5 is characterized by very early onset of progressive renal failure. A subset of patients may develop mild ocular anomalies, such as myopia, nystagmus, and strabismus.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.7

Sequence similarities

Contains 13 laminin EGF-like domains.

Contains 1 laminin IV type B domain.

Contains 1 laminin N-terminal domain.

Ontologies

Keywords
   Biological processCell adhesion
   Cellular componentBasement membrane
Extracellular matrix
Secreted
   Coding sequence diversityPolymorphism
   DiseaseDisease mutation
   DomainCoiled coil
Laminin EGF-like domain
Repeat
Signal
   PTMDisulfide bond
Glycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processSchwann cell development

Inferred from electronic annotation. Source: Ensembl

astrocyte development

Inferred from electronic annotation. Source: Ensembl

axon extension involved in regeneration

Inferred from electronic annotation. Source: Ensembl

axon guidance

Inferred from electronic annotation. Source: Ensembl

cell adhesion

Inferred from electronic annotation. Source: UniProtKB-KW

extracellular matrix organization

Traceable author statement. Source: Reactome

metanephric glomerular basement membrane development

Inferred from electronic annotation. Source: Ensembl

metanephric glomerular visceral epithelial cell development

Inferred from electronic annotation. Source: Ensembl

neuromuscular junction development

Inferred from electronic annotation. Source: Ensembl

retina development in camera-type eye

Inferred from electronic annotation. Source: Ensembl

visual perception

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentbasal lamina

Traceable author statement Ref.1. Source: ProtInc

basement membrane

Inferred from direct assay PubMed 10964500PubMed 14557481PubMed 2099832. Source: UniProtKB

extracellular region

Traceable author statement. Source: Reactome

extracellular vesicular exosome

Inferred from direct assay PubMed 19199708. Source: UniProt

laminin-11 complex

Traceable author statement PubMed 16236823. Source: BHF-UCL

laminin-3 complex

Inferred from physical interaction PubMed 10964500. Source: UniProtKB

synapse

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionstructural molecule activity

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

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3232 Potential
Chain33 – 17981766Laminin subunit beta-2
PRO_0000017068

Regions

Domain43 – 282240Laminin N-terminal
Domain283 – 34664Laminin EGF-like 1
Domain347 – 40963Laminin EGF-like 2
Domain410 – 46960Laminin EGF-like 3
Domain470 – 52152Laminin EGF-like 4
Domain522 – 55231Laminin EGF-like 5; truncated
Domain561 – 777217Laminin IV type B
Domain783 – 83048Laminin EGF-like 6
Domain831 – 87646Laminin EGF-like 7
Domain877 – 92650Laminin EGF-like 8
Domain927 – 98559Laminin EGF-like 9
Domain986 – 103752Laminin EGF-like 10
Domain1038 – 109457Laminin EGF-like 11
Domain1095 – 114248Laminin EGF-like 12
Domain1143 – 118947Laminin EGF-like 13
Region1190 – 1409220Domain II
Region1410 – 144233Domain alpha
Region1443 – 1798356Domain I
Coiled coil1253 – 131967 Potential
Coiled coil1472 – 152655 Potential
Coiled coil1577 – 1790214 Potential

Amino acid modifications

Glycosylation2481N-linked (GlcNAc...) Potential
Glycosylation3681N-linked (GlcNAc...) Potential
Glycosylation10851N-linked (GlcNAc...) Potential
Glycosylation12491N-linked (GlcNAc...) Potential
Glycosylation13081N-linked (GlcNAc...) Ref.3
Glycosylation13481N-linked (GlcNAc...) Ref.3
Glycosylation14991N-linked (GlcNAc...) Ref.3
Disulfide bond283 ↔ 292 By similarity
Disulfide bond285 ↔ 310 By similarity
Disulfide bond312 ↔ 321 By similarity
Disulfide bond324 ↔ 344 By similarity
Disulfide bond347 ↔ 356 By similarity
Disulfide bond349 ↔ 374 By similarity
Disulfide bond377 ↔ 386 By similarity
Disulfide bond389 ↔ 407 By similarity
Disulfide bond410 ↔ 423 By similarity
Disulfide bond412 ↔ 438 By similarity
Disulfide bond440 ↔ 449 By similarity
Disulfide bond452 ↔ 467 By similarity
Disulfide bond470 ↔ 484 By similarity
Disulfide bond472 ↔ 491 By similarity
Disulfide bond493 ↔ 502 By similarity
Disulfide bond505 ↔ 519 By similarity
Disulfide bond522 ↔ 534 By similarity
Disulfide bond524 ↔ 541 By similarity
Disulfide bond543 ↔ 552 By similarity
Disulfide bond783 ↔ 795 By similarity
Disulfide bond785 ↔ 802 By similarity
Disulfide bond804 ↔ 813 By similarity
Disulfide bond816 ↔ 828 By similarity
Disulfide bond831 ↔ 843 By similarity
Disulfide bond833 ↔ 850 By similarity
Disulfide bond852 ↔ 861 By similarity
Disulfide bond864 ↔ 874 By similarity
Disulfide bond877 ↔ 886 By similarity
Disulfide bond879 ↔ 893 By similarity
Disulfide bond896 ↔ 905 By similarity
Disulfide bond908 ↔ 924 By similarity
Disulfide bond927 ↔ 943 By similarity
Disulfide bond929 ↔ 954 By similarity
Disulfide bond956 ↔ 965 By similarity
Disulfide bond968 ↔ 983 By similarity
Disulfide bond986 ↔ 1000 By similarity
Disulfide bond988 ↔ 1007 By similarity
Disulfide bond1010 ↔ 1019 By similarity
Disulfide bond1022 ↔ 1035 By similarity
Disulfide bond1038 ↔ 1058 By similarity
Disulfide bond1040 ↔ 1065 By similarity
Disulfide bond1067 ↔ 1076 By similarity
Disulfide bond1079 ↔ 1092 By similarity
Disulfide bond1095 ↔ 1107 By similarity
Disulfide bond1097 ↔ 1114 By similarity
Disulfide bond1116 ↔ 1125 By similarity
Disulfide bond1128 ↔ 1140 By similarity
Disulfide bond1143 ↔ 1155 By similarity
Disulfide bond1145 ↔ 1162 By similarity
Disulfide bond1164 ↔ 1173 By similarity
Disulfide bond1176 ↔ 1187 By similarity
Disulfide bond1190Interchain Probable
Disulfide bond1193Interchain Probable
Disulfide bond1797Interchain Probable

Natural variations

Natural variant1471H → R in NPHS5. Ref.7
VAR_066492
Natural variant2461R → Q in PIERSS; without ocular abnormalities. Ref.6
VAR_031968
Natural variant2461R → W in PIERSS. Ref.5
VAR_031969
Natural variant3211C → R in PIERSS; with mild ocular abnormalities. Ref.6
VAR_031970
Natural variant9871E → K.
Corresponds to variant rs34759087 [ dbSNP | Ensembl ].
VAR_031971
Natural variant13801N → K in PIERSS; with mild ocular abnormalities; associated with F-1393. Ref.6
VAR_031972
Natural variant13931L → F in PIERSS; with mild ocular abnormalities; associated with K-1380. Ref.6
VAR_031973

Experimental info

Sequence conflict9141G → R in CAA92279. Ref.1
Sequence conflict11791G → A in AAB34682. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P55268 [UniParc].

Last modified August 21, 2007. Version 2.
Checksum: FFB3531AD13E1486

FASTA1,798195,981
        10         20         30         40         50         60 
MELTSRERGR GQPLPWELRL GLLLSVLAAT LAQAPAPDVP GCSRGSCYPA TGDLLVGRAD 

        70         80         90        100        110        120 
RLTASSTCGL NGPQPYCIVS HLQDEKKCFL CDSRRPFSAR DNPHSHRIQN VVTSFAPQRR 

       130        140        150        160        170        180 
AAWWQSENGI PAVTIQLDLE AEFHFTHLIM TFKTFRPAAM LVERSADFGR TWHVYRYFSY 

       190        200        210        220        230        240 
DCGADFPGVP LAPPRHWDDV VCESRYSEIE PSTEGEVIYR VLDPAIPIPD PYSSRIQNLL 

       250        260        270        280        290        300 
KITNLRVNLT RLHTLGDNLL DPRREIREKY YYALYELVVR GNCFCYGHAS ECAPAPGAPA 

       310        320        330        340        350        360 
HAEGMVHGAC ICKHNTRGLN CEQCQDFYRD LPWRPAEDGH SHACRKCECH GHTHSCHFDM 

       370        380        390        400        410        420 
AVYLASGNVS GGVCDGCQHN TAGRHCELCR PFFYRDPTKD LRDPAVCRSC DCDPMGSQDG 

       430        440        450        460        470        480 
GRCDSHDDPA LGLVSGQCRC KEHVVGTRCQ QCRDGFFGLS ISDRLGCRRC QCNARGTVPG 

       490        500        510        520        530        540 
STPCDPNSGS CYCKRLVTGR GCDRCLPGHW GLSHDLLGCR PCDCDVGGAL DPQCDEGTGQ 

       550        560        570        580        590        600 
CHCRQHMVGR RCEQVQPGYF RPFLDHLIWE AEDTRGQVLD VVERLVTPGE TPSWTGSGFV 

       610        620        630        640        650        660 
RLQEGQTLEF LVASVPKAMD YDLLLRLEPQ VPEQWAELEL IVQRPGPVPA HSLCGHLVPK 

       670        680        690        700        710        720 
DDRIQGTLQP HARYLIFPNP VCLEPGISYK LHLKLVRTGG SAQPETPYSG PGLLIDSLVL 

       730        740        750        760        770        780 
LPRVLVLEMF SGGDAAALER QATFERYQCH EEGLVPSKTS PSEACAPLLI SLSTLIYNGA 

       790        800        810        820        830        840 
LPCQCNPQGS LSSECNPHGG QCLCKPGVVG RRCDLCAPGY YGFGPTGCQA CQCSHEGALS 

       850        860        870        880        890        900 
SLCEKTSGQC LCRTGAFGLR CDRCQRGQWG FPSCRPCVCN GHADECNTHT GACLGCRDHT 

       910        920        930        940        950        960 
GGEHCERCIA GFHGDPRLPY GGQCRPCPCP EGPGSQRHFA TSCHQDEYSQ QIVCHCRAGY 

       970        980        990       1000       1010       1020 
TGLRCEACAP GHFGDPSRPG GRCQLCECSG NIDPMDPDAC DPHTGQCLRC LHHTEGPHCA 

      1030       1040       1050       1060       1070       1080 
HCKPGFHGQA ARQSCHRCTC NLLGTNPQQC PSPDQCHCDP SSGQCPCLPN VQGPSCDRCA 

      1090       1100       1110       1120       1130       1140 
PNFWNLTSGH GCQPCACHPS RARGPTCNEF TGQCHCRAGF GGRTCSECQE LHWGDPGLQC 

      1150       1160       1170       1180       1190       1200 
HACDCDSRGI DTPQCHRFTG HCSCRPGVSG VRCDQCARGF SGIFPACHPC HACFGDWDRV 

      1210       1220       1230       1240       1250       1260 
VQDLAARTQR LEQRAQELQQ TGVLGAFESS FWHMQEKLGI VQGIVGARNT SAASTAQLVE 

      1270       1280       1290       1300       1310       1320 
ATEELRREIG EATEHLTQLE ADLTDVQDEN FNANHALSGL ERDRLALNLT LRQLDQHLDL 

      1330       1340       1350       1360       1370       1380 
LKHSNFLGAY DSIRHAHSQS AEAERRANTS ALAVPSPVSN SASARHRTEA LMDAQKEDFN 

      1390       1400       1410       1420       1430       1440 
SKHMANQRAL GKLSAHTHTL SLTDINELVC GAPGDAPCAT SPCGGAGCRD EDGQPRCGGL 

      1450       1460       1470       1480       1490       1500 
SCNGAAATAD LALGRARHTQ AELQRALAEG GSILSRVAET RRQASEAQQR AQAALDKANA 

      1510       1520       1530       1540       1550       1560 
SRGQVEQANQ ELQELIQSVK DFLNQEGADP DSIEMVATRV LELSIPASAE QIQHLAGAIA 

      1570       1580       1590       1600       1610       1620 
ERVRSLADVD AILARTVGDV RRAEQLLQDA RRARSWAEDE KQKAETVQAA LEEAQRAQGI 

      1630       1640       1650       1660       1670       1680 
AQGAIRGAVA DTRDTEQTLY QVQERMAGAE RALSSAGERA RQLDALLEAL KLKRAGNSLA 

      1690       1700       1710       1720       1730       1740 
ASTAEETAGS AQGRAQEAEQ LLRGPLGDQY QTVKALAERK AQGVLAAQAR AEQLRDEARD 

      1750       1760       1770       1780       1790 
LLQAAQDKLQ RLQELEGTYE ENERALESKA AQLDGLEARM RSVLQAINLQ VQIYNTCQ 

« Hide

References

« Hide 'large scale' references
[1]"Human beta 2 chain of laminin (formerly S chain): cDNA cloning, chromosomal localization, and expression in carcinomas."
Wewer U.M., Gerecke D.R., Durkin M.E., Kurtz K.S., Mattei M.-G., Champliaud M.-F., Burgeson R.E., Albrechtsen R.
Genomics 24:243-252(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
[2]"The human laminin beta 2 chain (S-laminin): structure, expression in fetal tissues and chromosomal assignment of the LAMB2 gene."
Iivanainen A., Vuolteenaho R., Sainio K., Eddy R., Shows T.B., Sariola H., Tryggvason K.
Matrix Biol. 14:489-497(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"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-1308; ASN-1348 AND ASN-1499.
Tissue: Liver.
[4]"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].
[5]"Human laminin beta2 deficiency causes congenital nephrosis with mesangial sclerosis and distinct eye abnormalities."
Zenker M., Aigner T., Wendler O., Tralau T., Muentefering H., Fenski R., Pitz S., Schumacher V., Royer-Pokora B., Wuehl E., Cochat P., Bouvier R., Kraus C., Mark K., Madlon H., Doetsch J., Rascher W., Maruniak-Chudek I. expand/collapse author list , Lennert T., Neumann L.M., Reis A.
Hum. Mol. Genet. 13:2625-2632(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT PIERSS TRP-246.
[6]"Recessive missense mutations in LAMB2 expand the clinical spectrum of LAMB2-associated disorders."
Hasselbacher K., Wiggins R.C., Matejas V., Hinkes B.G., Mucha B., Hoskins B.E., Ozaltin F., Nuernberg G., Becker C., Hangan D., Pohl M., Kuwertz-Broeking E., Griebel M., Schumacher V., Royer-Pokora B., Bakkaloglu A., Nuernberg P., Zenker M., Hildebrandt F.
Kidney Int. 70:1008-1012(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS PIERSS GLN-246; ARG-321; LYS-1380 AND PHE-1393.
[7]"A novel mutation of LAMB2 in a multigenerational mennonite family reveals a new phenotypic variant of Pierson syndrome."
Mohney B.G., Pulido J.S., Lindor N.M., Hogan M.C., Consugar M.B., Peters J., Pankratz V.S., Nasr S.H., Smith S.J., Gloor J., Kubly V., Spencer D., Nielson R., Puffenberger E.G., Strauss K.A., Morton D.H., Eldahdah L., Harris P.C.
Ophthalmology 118:1137-1144(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT NPHS5 ARG-147.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z68155, Z68156 Genomic DNA. Translation: CAA92279.1.
X79683 mRNA. Translation: CAA56130.1.
S77512 mRNA. Translation: AAB34682.2.
CCDSCCDS2789.1.
PIRA55677.
S53869.
RefSeqNP_002283.3. NM_002292.3.
XP_005265184.1. XM_005265127.2.
UniGeneHs.439726.

3D structure databases

ProteinModelPortalP55268.
SMRP55268. Positions 41-560, 792-1180.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid110107. 12 interactions.
DIPDIP-42106N.
IntActP55268. 10 interactions.
MINTMINT-1197111.
STRING9606.ENSP00000307156.

Chemistry

ChEMBLCHEMBL2364187.

PTM databases

PhosphoSiteP55268.

Polymorphism databases

DMDM156630892.

Proteomic databases

MaxQBP55268.
PaxDbP55268.
PRIDEP55268.

Protocols and materials databases

DNASU3913.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000305544; ENSP00000307156; ENSG00000172037.
ENST00000418109; ENSP00000388325; ENSG00000172037.
GeneID3913.
KEGGhsa:3913.
UCSCuc003cwe.3. human.

Organism-specific databases

CTD3913.
GeneCardsGC03M049133.
HGNCHGNC:6487. LAMB2.
HPACAB000053.
HPA001895.
HPA050033.
MIM150325. gene.
609049. phenotype.
614199. phenotype.
neXtProtNX_P55268.
Orphanet306507. LAMB-2-related infantile-onset nephrotic syndrome.
2670. Pierson syndrome.
98915. Synaptic congenital myasthenic syndromes.
PharmGKBPA164741827.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG241384.
HOGENOMHOG000007552.
HOVERGENHBG052301.
InParanoidP55268.
KOK06243.
OMAQPYCIVS.
OrthoDBEOG75XGK0.
PhylomeDBP55268.
TreeFamTF312903.

Enzyme and pathway databases

ReactomeREACT_118779. Extracellular matrix organization.

Gene expression databases

ArrayExpressP55268.
BgeeP55268.
CleanExHS_LAMB2.
GenevestigatorP55268.

Family and domain databases

InterProIPR013032. EGF-like_CS.
IPR002049. EGF_laminin.
IPR013015. Laminin_IV.
IPR008211. Laminin_N.
[Graphical view]
PfamPF00053. Laminin_EGF. 13 hits.
PF00055. Laminin_N. 1 hit.
[Graphical view]
SMARTSM00180. EGF_Lam. 13 hits.
SM00136. LamNT. 1 hit.
[Graphical view]
PROSITEPS00022. EGF_1. 10 hits.
PS01186. EGF_2. 2 hits.
PS01248. EGF_LAM_1. 12 hits.
PS50027. EGF_LAM_2. 13 hits.
PS51116. LAMININ_IVB. 1 hit.
PS51117. LAMININ_NTER. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSLAMB2. human.
GeneWikiLaminin,_beta_2.
GenomeRNAi3913.
NextBio15371.
PROP55268.
SOURCESearch...

Entry information

Entry nameLAMB2_HUMAN
AccessionPrimary (citable) accession number: P55268
Secondary accession number(s): Q16321
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: August 21, 2007
Last modified: July 9, 2014
This is version 139 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 3

Human chromosome 3: entries, gene names and cross-references to MIM