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Q13751 (LAMB3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 148. 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-3
Alternative name(s):
Epiligrin subunit bata
Kalinin B1 chain
Kalinin subunit beta
Laminin B1k chain
Laminin-5 subunit beta
Nicein subunit beta
Gene names
Name:LAMB3
Synonyms:LAMNB1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1172 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-3 is a subunit of laminin-5 (laminin-332 or epiligrin/kalinin/nicein). Interacts with ECM1. Ref.8

Subcellular location

Secretedextracellular spaceextracellular matrixbasement membrane.

Tissue specificity

Found in the basement membranes (major component).

Domain

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

Domain VI 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. Ref.10

Generalized atrophic benign epidermolysis bullosa (GABEB) [MIM:226650]: A non-lethal, adult form of junctional epidermolysis bullosa characterized by life-long blistering of the skin, associated with hair and tooth abnormalities.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.11 Ref.13

Sequence similarities

Contains 6 laminin EGF-like domains.

Contains 1 laminin N-terminal domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1717 Potential
Chain18 – 11721155Laminin subunit beta-3
PRO_0000017071

Regions

Domain22 – 249228Laminin N-terminal
Domain250 – 31566Laminin EGF-like 1
Domain316 – 37863Laminin EGF-like 2
Domain379 – 43052Laminin EGF-like 3
Domain431 – 48050Laminin EGF-like 4
Domain481 – 53353Laminin EGF-like 5
Domain534 – 58047Laminin EGF-like 6
Region579 – 785207Domain II
Region786 – 81631Domain alpha
Region817 – 1170354Domain I
Coiled coil723 – 75735 Potential
Coiled coil831 – 88454 Potential
Coiled coil948 – 1133186 Potential

Amino acid modifications

Glycosylation2201N-linked (GlcNAc...) Potential
Glycosylation6041N-linked (GlcNAc...) Potential
Glycosylation8101N-linked (GlcNAc...) Potential
Disulfide bond250 ↔ 259 By similarity
Disulfide bond252 ↔ 279 By similarity
Disulfide bond281 ↔ 290 By similarity
Disulfide bond293 ↔ 313 By similarity
Disulfide bond316 ↔ 325 By similarity
Disulfide bond318 ↔ 343 By similarity
Disulfide bond346 ↔ 355 By similarity
Disulfide bond358 ↔ 376 By similarity
Disulfide bond379 ↔ 392 By similarity
Disulfide bond381 ↔ 399 By similarity
Disulfide bond401 ↔ 410 By similarity
Disulfide bond413 ↔ 428 By similarity
Disulfide bond431 ↔ 444 By similarity
Disulfide bond433 ↔ 451 By similarity
Disulfide bond453 ↔ 462 By similarity
Disulfide bond465 ↔ 478 By similarity
Disulfide bond481 ↔ 493 By similarity
Disulfide bond483 ↔ 500 By similarity
Disulfide bond502 ↔ 511 By similarity
Disulfide bond519 ↔ 531 By similarity
Disulfide bond534 ↔ 546 By similarity
Disulfide bond536 ↔ 553 By similarity
Disulfide bond555 ↔ 564 By similarity
Disulfide bond567 ↔ 578 By similarity
Disulfide bond581Interchain Probable
Disulfide bond584Interchain Probable
Disulfide bond1171Interchain Probable

Natural variations

Natural variant1811N → D.
Corresponds to variant rs2235542 [ dbSNP | Ensembl ].
VAR_037309
Natural variant1991G → A in GABEB; somatic second-site mutation. Ref.13
VAR_037310
Natural variant2071K → Q in GABEB; somatic second-site mutation. Ref.13
VAR_037311
Natural variant2101E → K in GABEB. Ref.11 Ref.13
VAR_004170
Natural variant2921R → L.
Corresponds to variant rs12091253 [ dbSNP | Ensembl ].
VAR_037312
Natural variant4381S → T.
Corresponds to variant rs2229468 [ dbSNP | Ensembl ].
VAR_034060
Natural variant4501R → C in a colorectal cancer sample; somatic mutation. Ref.12
VAR_035820
Natural variant5271V → M.
Corresponds to variant rs2076349 [ dbSNP | Ensembl ].
VAR_037313
Natural variant6791P → L in H-JEB. Ref.10
VAR_004171
Natural variant6901N → S.
Corresponds to variant rs2229466 [ dbSNP | Ensembl ].
VAR_034061
Natural variant8521M → L. Ref.6
Corresponds to variant rs12748250 [ dbSNP | Ensembl ].
VAR_034062
Natural variant9261A → D.
Corresponds to variant rs2076222 [ dbSNP | Ensembl ].
VAR_037314
Natural variant9881R → W.
Corresponds to variant rs2229467 [ dbSNP | Ensembl ].
VAR_034063

Experimental info

Sequence conflict1241Q → R in AAA61834. Ref.1
Sequence conflict2691Missing in AAA61834. Ref.1
Sequence conflict3881P → A in AAA61834. Ref.1
Sequence conflict426 – 4272QG → RR in AAA61834. Ref.1
Sequence conflict440 – 4412RD → E in AAA61834. Ref.1
Sequence conflict489 – 50012LSPQC…FTGQC → PQPTVQPVHRAV in BAA22263. Ref.3
Sequence conflict6031R → P in AAA61834. Ref.1
Sequence conflict8151G → A in AAA61834. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q13751 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 61BC1A60BBD4FA05

FASTA1,172129,572
        10         20         30         40         50         60 
MRPFFLLCFA LPGLLHAQQA CSRGACYPPV GDLLVGRTRF LRASSTCGLT KPETYCTQYG 

        70         80         90        100        110        120 
EWQMKCCKCD SRQPHNYYSH RVENVASSSG PMRWWQSQND VNPVSLQLDL DRRFQLQEVM 

       130        140        150        160        170        180 
MEFQGPMPAG MLIERSSDFG KTWRVYQYLA ADCTSTFPRV RQGRPQSWQD VRCQSLPQRP 

       190        200        210        220        230        240 
NARLNGGKVQ LNLMDLVSGI PATQSQKIQE VGEITNLRVN FTRLAPVPQR GYHPPSAYYA 

       250        260        270        280        290        300 
VSQLRLQGSC FCHGHADRCA PKPGASAGPS TAVQVHDVCV CQHNTAGPNC ERCAPFYNNR 

       310        320        330        340        350        360 
PWRPAEGQDA HECQRCDCNG HSETCHFDPA VFAASQGAYG GVCDNCRDHT EGKNCERCQL 

       370        380        390        400        410        420 
HYFRNRRPGA SIQETCISCE CDPDGAVPGA PCDPVTGQCV CKEHVQGERC DLCKPGFTGL 

       430        440        450        460        470        480 
TYANPQGCHR CDCNILGSRR DMPCDEESGR CLCLPNVVGP KCDQCAPYHW KLASGQGCEP 

       490        500        510        520        530        540 
CACDPHNSLS PQCNQFTGQC PCREGFGGLM CSAAAIRQCP DRTYGDVATG CRACDCDFRG 

       550        560        570        580        590        600 
TEGPGCDKAS GRCLCRPGLT GPRCDQCQRG YCNRYPVCVA CHPCFQTYDA DLREQALRFG 

       610        620        630        640        650        660 
RLRNATASLW SGPGLEDRGL ASRILDAKSK IEQIRAVLSS PAVTEQEVAQ VASAILSLRR 

       670        680        690        700        710        720 
TLQGLQLDLP LEEETLSLPR DLESLDRSFN GLLTMYQRKR EQFEKISSAD PSGAFRMLST 

       730        740        750        760        770        780 
AYEQSAQAAQ QVSDSSRLLD QLRDSRREAE RLVRQAGGGG GTGSPKLVAL RLEMSSLPDL 

       790        800        810        820        830        840 
TPTFNKLCGN SRQMACTPIS CPGELCPQDN GTACGSRCRG VLPRAGGAFL MAGQVAEQLR 

       850        860        870        880        890        900 
GFNAQLQRTR QMIRAAEESA SQIQSSAQRL ETQVSASRSQ MEEDVRRTRL LIQQVRDFLT 

       910        920        930        940        950        960 
DPDTDAATIQ EVSEAVLALW LPTDSATVLQ KMNEIQAIAA RLPNVDLVLS QTKQDIARAR 

       970        980        990       1000       1010       1020 
RLQAEAEEAR SRAHAVEGQV EDVVGNLRQG TVALQEAQDT MQGTSRSLRL IQDRVAEVQQ 

      1030       1040       1050       1060       1070       1080 
VLRPAEKLVT SMTKQLGDFW TRMEELRHQA RQQGAEAVQA QQLAEGASEQ ALSAQEGFER 

      1090       1100       1110       1120       1130       1140 
IKQKYAELKD RLGQSSMLGE QGARIQSVKT EAEELFGETM EMMDRMKDME LELLRGSQAI 

      1150       1160       1170 
MLRSADLTGL EKRVEQIRDH INGRVLYYAT CK 

« Hide

References

« Hide 'large scale' references
[1]"The complete primary structure for a novel laminin chain, the laminin B1k chain."
Gerecke D.R., Wagman D.W., Champliaud M.-F., Burgeson R.E.
J. Biol. Chem. 269:11073-11080(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 172-190.
[2]"Cloning of the beta 3 chain gene (LAMB3) of human laminin 5, a candidate gene in junctional epidermolysis bullosa."
Pulkkinen L., Gerecke D.R., Christiano A.M., Wagman D.W., Burgeson R.E., Uitto J.
Genomics 25:192-198(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"Chromosomal loci of 50 human keratinocyte cDNAs assigned by fluorescence in situ hybridization."
Morishima Y., Ariyama T., Yamanishi K., Abe T., Ueda E., Yasuno H., Inazawa J.
Genomics 28:273-279(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Epidermis.
[4]"In vivo restoration of laminin 5 beta 3 expression and function in junctional epidermolysis bullosa."
Robbins P.B., Lin Q., Goodnough J.B., Tian H., Chen X., Khavari P.A.
Proc. Natl. Acad. Sci. U.S.A. 98:5193-5198(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[5]"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].
[6]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 (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT LEU-852.
[7]"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: Eye.
[8]"ECM1 interacts with fibulin-3 and the beta 3 chain of laminin 332 through its serum albumin subdomain-like 2 domain."
Sercu S., Lambeir A.M., Steenackers E., El Ghalbzouri A., Geentjens K., Sasaki T., Oyama N., Merregaert J.
Matrix Biol. 28:160-169(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ECM1.
[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].
[10]"Detection of sequence variants in the gene encoding the beta 3 chain of laminin 5 (LAMB3)."
Pulkkinen L., McGrath J.A., Christiano A.M., Uitto J.
Hum. Mutat. 6:77-84(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT H-JEB LEU-679.
[11]"E210K mutation in the gene encoding the beta3 chain of laminin-5 (LAMB3) is predictive of a phenotype of generalized atrophic benign epidermolysis bullosa."
Mellerio J.E., Eady R.A.J., Atherton D.J., Lake B.D., McGrath J.A.
Br. J. Dermatol. 139:325-331(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT GABEB LYS-210.
[12]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] CYS-450.
[13]"Revertant mosaicism in junctional epidermolysis bullosa due to multiple correcting second-site mutations in LAMB3."
Pasmooij A.M.G., Pas H.H., Bolling M.C., Jonkman M.F.
J. Clin. Invest. 117:1240-1248(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS GABEB ALA-199; GLN-207 AND LYS-210.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L25541 mRNA. Translation: AAA61834.1.
U17760 expand/collapse EMBL AC list , U17745, U17746, U17747, U17748, U17749, U17750, U17751, U17752, U17753, U17754, U17755, U17756, U17757, U17758, U17759 Genomic DNA. Translation: AAC51352.1.
D37766 mRNA. Translation: BAA22263.1.
AY035783 mRNA. Translation: AAK61364.1.
AL023754 Genomic DNA. Translation: CAA19297.2.
AL023754, AL031316 Genomic DNA. Translation: CAI19989.1.
AL031316, AL023754 Genomic DNA. Translation: CAI20062.1.
CH471100 Genomic DNA. Translation: EAW93448.1.
CH471100 Genomic DNA. Translation: EAW93449.1.
BC075838 mRNA. Translation: AAH75838.1.
CCDSCCDS1487.1.
PIRA53612.
RefSeqNP_000219.2. NM_000228.2.
NP_001017402.1. NM_001017402.1.
NP_001121113.1. NM_001127641.1.
XP_005273181.1. XM_005273124.2.
UniGeneHs.497636.

3D structure databases

ProteinModelPortalQ13751.
SMRQ13751. Positions 20-566.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid110108. 3 interactions.
IntActQ13751. 1 interaction.
MINTMINT-4053402.
STRING9606.ENSP00000348384.

Chemistry

ChEMBLCHEMBL2364187.

PTM databases

PhosphoSiteQ13751.

Polymorphism databases

DMDM2497600.

Proteomic databases

MaxQBQ13751.
PaxDbQ13751.
PRIDEQ13751.

Protocols and materials databases

DNASU3914.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000356082; ENSP00000348384; ENSG00000196878.
ENST00000367030; ENSP00000355997; ENSG00000196878.
ENST00000391911; ENSP00000375778; ENSG00000196878.
GeneID3914.
KEGGhsa:3914.
UCSCuc001hhg.3. human.

Organism-specific databases

CTD3914.
GeneCardsGC01M209788.
GeneReviewsLAMB3.
HGNCHGNC:6490. LAMB3.
HPAHPA008069.
MIM150310. gene.
226650. phenotype.
226700. phenotype.
neXtProtNX_Q13751.
Orphanet79402. Generalized junctional epidermolysis bullosa, non-Herlitz type.
100031. Hypoplastic amelogenesis imperfecta.
79404. Junctional epidermolysis bullosa, Herlitz type.
PharmGKBPA30278.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG289025.
HOGENOMHOG000113279.
HOVERGENHBG052302.
InParanoidQ13751.
KOK06244.
OMARSQMEED.
OrthoDBEOG77WWBQ.
PhylomeDBQ13751.
TreeFamTF352481.

Enzyme and pathway databases

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

Gene expression databases

ArrayExpressQ13751.
BgeeQ13751.
CleanExHS_LAMB3.
GenevestigatorQ13751.

Family and domain databases

InterProIPR013032. EGF-like_CS.
IPR002049. EGF_laminin.
IPR008211. Laminin_N.
[Graphical view]
PfamPF00053. Laminin_EGF. 6 hits.
PF00055. Laminin_N. 1 hit.
[Graphical view]
SMARTSM00180. EGF_Lam. 6 hits.
SM00136. LamNT. 1 hit.
[Graphical view]
PROSITEPS00022. EGF_1. 5 hits.
PS01186. EGF_2. 1 hit.
PS01248. EGF_LAM_1. 5 hits.
PS50027. EGF_LAM_2. 6 hits.
PS51117. LAMININ_NTER. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSLAMB3. human.
GeneWikiLaminin,_beta_3.
GenomeRNAi3914.
NextBio15375.
PMAP-CutDBQ13751.
PROQ13751.
SOURCESearch...

Entry information

Entry nameLAMB3_HUMAN
AccessionPrimary (citable) accession number: Q13751
Secondary accession number(s): D3DT88 expand/collapse secondary AC list , O14947, Q14733, Q9UJK4, Q9UJL1
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: July 9, 2014
This is version 148 of the entry and version 1 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