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Q08188 (TGM3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 140. 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·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Protein-glutamine gamma-glutamyltransferase E

EC=2.3.2.13
Alternative name(s):
Transglutaminase E
Short name=TG(E)
Short name=TGE
Short name=TGase E
Transglutaminase-3
Short name=TGase-3
Gene names
Name:TGM3
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length693 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the calcium-dependent formation of isopeptide cross-links between glutamine and lysine residues in various proteins, as well as the conjugation of polyamines to proteins. Involved in the formation of the cornified envelope (CE), a specialized component consisting of covalent cross-links of proteins beneath the plasma membrane of terminally differentiated keratinocytes. Catalyzes small proline-rich proteins (SPRR1 and SPRR2) and LOR cross-linking to form small interchain oligomers, which are further cross-linked by TGM1 onto the growing CE scaffold By similarity. In hair follicles, involved in cross-linking structural proteins to hardening the inner root sheath.

Catalytic activity

Protein glutamine + alkylamine = protein N(5)-alkylglutamine + NH3. Ref.11 Ref.12

Cofactor

Binds 3 calcium ions per subunit. Binds 1 calcium ion as a zymogen, and binds 2 more calcium ions, or other divalent metal cations, after proteolytic processing. Ref.11 Ref.12

Subunit structure

Consists of two polypeptide chains, which are synthesized as a precursor form of a single polypeptide.

Post-translational modification

Activated by proteolytic processing. In vitro activation is commonly achieved by cleavage with dispase, a neutral bacterial protease. Dispase cleavage site was proposed to lie between Ser-470 and Ser-471 (Ref.1) or between Pro-465 and Phe-466 (Ref.8). Physiological activation may be catalyzed by CTSL and, to a lesser extent, by CTSS, but not by CTSB, CTSD nor CTSV (Ref.8).

Sequence similarities

Belongs to the transglutaminase superfamily. Transglutaminase family.

Ontologies

Keywords
   Biological processKeratinization
   Coding sequence diversityPolymorphism
   LigandCalcium
Metal-binding
   Molecular functionAcyltransferase
Transferase
   PTMAcetylation
Phosphoprotein
Zymogen
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processcell envelope organization

Inferred from direct assay PubMed 24643. Source: UniProtKB

cellular protein modification process

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

hair follicle morphogenesis

Traceable author statement PubMed 15193648. Source: UniProtKB

keratinization

Inferred from electronic annotation. Source: UniProtKB-KW

keratinocyte differentiation

Inferred from expression pattern PubMed 12850301. Source: UniProtKB

peptide cross-linking

Inferred from direct assay Ref.12PubMed 24643. Source: UniProtKB

protein tetramerization

Inferred from direct assay PubMed 5038456. Source: UniProtKB

   Cellular_componentcytoplasm

Inferred from direct assay PubMed 12850301. Source: UniProtKB

extracellular vesicular exosome

Inferred from direct assay PubMed 19199708. Source: UniProt

extrinsic component of cytoplasmic side of plasma membrane

Inferred from direct assay PubMed 5038456. Source: UniProtKB

   Molecular_functioncalcium ion binding

Inferred from direct assay Ref.12. Source: UniProtKB

catalytic activity

Inferred from direct assay Ref.1. Source: UniProtKB

protein-glutamine gamma-glutamyltransferase activity

Inferred from direct assay Ref.12Ref.1. Source: UniProtKB

transferase activity, transferring acyl groups

Traceable author statement PubMed 15193648. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.7
Chain2 – 467466Protein-glutamine gamma-glutamyltransferase E 50 kDa catalytic chain
PRO_0000033652
Chain468 – 693226Protein-glutamine gamma-glutamyltransferase E 27 kDa non-catalytic chain
PRO_0000033653

Sites

Active site2731 By similarity
Active site3311 By similarity
Active site3541 By similarity
Metal binding2221Calcium 1; via carbonyl oxygen
Metal binding2251Calcium 1
Metal binding2271Calcium 1; via carbonyl oxygen
Metal binding2281Calcium 1
Metal binding2301Calcium 1; via carbonyl oxygen
Metal binding3021Calcium 2
Metal binding3041Calcium 2
Metal binding3061Calcium 2
Metal binding3081Calcium 2; via carbonyl oxygen
Metal binding3251Calcium 2
Metal binding3941Calcium 3
Metal binding4161Calcium 3; via carbonyl oxygen
Metal binding4441Calcium 3
Metal binding4491Calcium 3
Site467 – 4682Cleavage; by CTSL

Amino acid modifications

Modified residue21N-acetylalanine Ref.7
Modified residue1111Phosphotyrosine Ref.9
Modified residue1121Phosphothreonine Ref.9

Natural variations

Natural variant131T → K. Ref.1 Ref.2 Ref.3 Ref.5 Ref.6 Ref.7
Corresponds to variant rs214803 [ dbSNP | Ensembl ].
VAR_040067
Natural variant1631I → L. Ref.3
Corresponds to variant rs6048066 [ dbSNP | Ensembl ].
VAR_040068
Natural variant2491S → N. Ref.3
Corresponds to variant rs214814 [ dbSNP | Ensembl ].
VAR_040069
Natural variant5621K → R. Ref.1
Corresponds to variant rs1042617 [ dbSNP | Ensembl ].
VAR_040070
Natural variant6541G → R. Ref.1 Ref.2 Ref.3 Ref.5 Ref.6
Corresponds to variant rs214830 [ dbSNP | Ensembl ].
VAR_040071
Natural variant6871L → M. Ref.3
Corresponds to variant rs45581032 [ dbSNP | Ensembl ].
VAR_055360

Experimental info

Sequence conflict58 – 592VS → DT in AAA61155. Ref.1
Sequence conflict2511N → G in AAA61155. Ref.1
Sequence conflict3241S → G in BAF84040. Ref.2
Sequence conflict3461S → P in AAA61155. Ref.1
Sequence conflict6741D → G in BAF84040. Ref.2

Secondary structure

........................................................................................................................ 693
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q08188 [UniParc].

Last modified September 1, 2009. Version 4.
Checksum: EAFAC0C9A8AA5FD6

FASTA69376,632
        10         20         30         40         50         60 
MAALGVQSIN WQTAFNRQAH HTDKFSSQEL ILRRGQNFQV LMIMNKGLGS NERLEFIVST 

        70         80         90        100        110        120 
GPYPSESAMT KAVFPLSNGS SGGWSAVLQA SNGNTLTISI SSPASAPIGR YTMALQIFSQ 

       130        140        150        160        170        180 
GGISSVKLGT FILLFNPWLN VDSVFMGNHA EREEYVQEDA GIIFVGSTNR IGMIGWNFGQ 

       190        200        210        220        230        240 
FEEDILSICL SILDRSLNFR RDAATDVASR NDPKYVGRVL SAMINSNDDN GVLAGNWSGT 

       250        260        270        280        290        300 
YTGGRDPRSW NGSVEILKNW KKSGFSPVRY GQCWVFAGTL NTALRSLGIP SRVITNFNSA 

       310        320        330        340        350        360 
HDTDRNLSVD VYYDPMGNPL DKGSDSVWNF HVWNEGWFVR SDLGPSYGGW QVLDATPQER 

       370        380        390        400        410        420 
SQGVFQCGPA SVIGVREGDV QLNFDMPFIF AEVNADRITW LYDNTTGKQW KNSVNSHTIG 

       430        440        450        460        470        480 
RYISTKAVGS NARMDVTDKY KYPEGSDQER QVFQKALGKL KPNTPFAATS SMGLETEEQE 

       490        500        510        520        530        540 
PSIIGKLKVA GMLAVGKEVN LVLLLKNLSR DTKTVTVNMT AWTIIYNGTL VHEVWKDSAT 

       550        560        570        580        590        600 
MSLDPEEEAE HPIKISYAQY EKYLKSDNMI RITAVCKVPD ESEVVVERDI ILDNPTLTLE 

       610        620        630        640        650        660 
VLNEARVRKP VNVQMLFSNP LDEPVRDCVL MVEGSGLLLG NLKIDVPTLG PKEGSRVRFD 

       670        680        690 
ILPSRSGTKQ LLADFSCNKF PAIKAMLSID VAE 

« Hide

References

« Hide 'large scale' references
[1]"The deduced sequence of the novel protransglutaminase E (TGase3) of human and mouse."
Kim I.-G., Gorman J.J., Park S.-C., Chung S.-I., Steinert P.M.
J. Biol. Chem. 268:12682-12690(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS LYS-13; ARG-562 AND ARG-654.
Tissue: Foreskin.
[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], VARIANTS LYS-13 AND ARG-654.
Tissue: Tongue.
[3]NIEHS SNPs program
Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS LYS-13; LEU-163; ASN-249; ARG-654 AND MET-687.
[4]"The DNA sequence and comparative analysis of human chromosome 20."
Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E. expand/collapse author list , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.
Nature 414:865-871(2001) [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 (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANTS LYS-13 AND ARG-654.
[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 LYS-13 AND ARG-654.
[7]Bienvenut W.V., Bensaad K., Vousden K.H.
Submitted (FEB-2008) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 2-13 AND 670-684, VARIANT LYS-13, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Osteosarcoma.
[8]"Cystatin M/E is a high affinity inhibitor of cathepsin V and cathepsin L by a reactive site that is distinct from the legumain-binding site. A novel clue for the role of cystatin M/E in epidermal cornification."
Cheng T., Hitomi K., van Vlijmen-Willems I.M., de Jongh G.J., Yamamoto K., Nishi K., Watts C., Reinheckel T., Schalkwijk J., Zeeuwen P.L.
J. Biol. Chem. 281:15893-15899(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 468-479, PROTEOLYTIC CLEAVAGE BY CTSL.
[9]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-111 AND THR-112, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[10]"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].
[11]"Three-dimensional structure of the human transglutaminase 3 enzyme: binding of calcium ions changes structure for activation."
Ahvazi B., Kim H.C., Kee S.H., Nemes Z., Steinert P.M.
EMBO J. 21:2055-2067(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 2-693 IN COMPLEX WITH CALCIUM, COFACTOR, CATALYTIC ACTIVITY.
[12]"Roles of calcium ions in the activation and activity of the transglutaminase 3 enzyme."
Ahvazi B., Boeshans K.M., Idler W., Baxa U., Steinert P.M.
J. Biol. Chem. 278:23834-23841(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 2-693 IN COMPLEX WITH CALCIUM AND MAGNESIUM, COFACTOR, CATALYTIC ACTIVITY.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L10386 mRNA. Translation: AAA61155.1.
AK290324 mRNA. Translation: BAF83013.1.
AK291351 mRNA. Translation: BAF84040.1.
AK315236 mRNA. Translation: BAG37663.1.
EF102483 Genomic DNA. Translation: ABK41960.1.
AL031678 Genomic DNA. Translation: CAB37633.1.
CH471133 Genomic DNA. Translation: EAX10601.1.
CH471133 Genomic DNA. Translation: EAX10602.1.
BC109075 mRNA. Translation: AAI09076.1.
BC109076 mRNA. Translation: AAI09077.1.
PIRA45991.
RefSeqNP_003236.3. NM_003245.3.
UniGeneHs.2022.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1L9MX-ray2.10A/B2-693[»]
1L9NX-ray2.10A/B2-693[»]
1NUDX-ray2.70A/B2-693[»]
1NUFX-ray2.70A2-693[»]
1NUGX-ray2.40A/B2-693[»]
ProteinModelPortalQ08188.
SMRQ08188. Positions 2-693.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112911. 8 interactions.
IntActQ08188. 6 interactions.
MINTMINT-7950929.
STRING9606.ENSP00000370867.

Chemistry

ChEMBLCHEMBL3363.
DrugBankDB00130. L-Glutamine.

PTM databases

PhosphoSiteQ08188.

Polymorphism databases

DMDM257051080.

Proteomic databases

PaxDbQ08188.
PeptideAtlasQ08188.
PRIDEQ08188.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000381458; ENSP00000370867; ENSG00000125780.
GeneID7053.
KEGGhsa:7053.
UCSCuc002wfx.4. human.

Organism-specific databases

CTD7053.
GeneCardsGC20P002224.
HGNCHGNC:11779. TGM3.
HPAHPA004728.
MIM600238. gene.
neXtProtNX_Q08188.
PharmGKBPA36492.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG80379.
HOVERGENHBG004342.
InParanoidQ08188.
KOK05620.
OMAEILPTRS.
OrthoDBEOG7WT40M.
PhylomeDBQ08188.
TreeFamTF324278.

Gene expression databases

BgeeQ08188.
CleanExHS_TGM3.
GenevestigatorQ08188.

Family and domain databases

Gene3D2.60.40.10. 3 hits.
3.90.260.10. 1 hit.
InterProIPR023608. Gln_gamma-glutamylTfrase_euk.
IPR013783. Ig-like_fold.
IPR014756. Ig_E-set.
IPR002931. Transglutaminase-like.
IPR008958. Transglutaminase_C.
IPR013808. Transglutaminase_CS.
IPR001102. Transglutaminase_N.
[Graphical view]
PANTHERPTHR11590. PTHR11590. 1 hit.
PfamPF00927. Transglut_C. 2 hits.
PF01841. Transglut_core. 1 hit.
PF00868. Transglut_N. 1 hit.
[Graphical view]
PIRSFPIRSF000459. TGM_EBP42. 1 hit.
SMARTSM00460. TGc. 1 hit.
[Graphical view]
SUPFAMSSF49309. SSF49309. 2 hits.
SSF81296. SSF81296. 1 hit.
PROSITEPS00547. TRANSGLUTAMINASES. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ08188.
GeneWikiTGM3.
GenomeRNAi7053.
NextBio27579.
PROQ08188.
SOURCESearch...

Entry information

Entry nameTGM3_HUMAN
AccessionPrimary (citable) accession number: Q08188
Secondary accession number(s): A8K5N6 expand/collapse secondary AC list , B2RCR6, D3DVX1, O95933, Q32ML9, Q32MM0
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: September 1, 2009
Last modified: April 16, 2014
This is version 140 of the entry and version 4 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 20

Human chromosome 20: entries, gene names and cross-references to MIM