SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P10620

- MGST1_HUMAN

UniProt

P10620 - MGST1_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
Microsomal glutathione S-transferase 1
Gene
MGST1, GST12, MGST
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. Has a wide substrate specificity.

Catalytic activityi

RX + glutathione = HX + R-S-glutathione.

Enzyme regulationi

Can be activated by reagents that attack Cys-50 sulfhydryl, such as N-ethylmaleimide. Activation also occurs via nitration of Tyr-93 by peroxynitrite By similarity.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei38 – 381Glutathione By similarity
Sitei50 – 501Activates the enzyme when modified By similarity
Binding sitei73 – 731Glutathione By similarity
Binding sitei74 – 741Glutathione By similarity
Binding sitei76 – 761Glutathione By similarity
Binding sitei81 – 811Glutathione By similarity
Binding sitei121 – 1211Glutathione By similarity

GO - Molecular functioni

  1. glutathione binding Source: Ensembl
  2. glutathione peroxidase activity Source: UniProtKB
  3. glutathione transferase activity Source: UniProtKB
  4. protein binding Source: IntAct

GO - Biological processi

  1. Leydig cell differentiation Source: Ensembl
  2. cellular response to lipid hydroperoxide Source: UniProtKB
  3. glutathione derivative biosynthetic process Source: Reactome
  4. glutathione metabolic process Source: Ensembl
  5. oxidation-reduction process Source: UniProtKB
  6. protein homotrimerization Source: UniProtKB
  7. response to drug Source: Ensembl
  8. response to lipopolysaccharide Source: Ensembl
  9. response to organonitrogen compound Source: Ensembl
  10. small molecule metabolic process Source: Reactome
  11. xenobiotic metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Enzyme and pathway databases

ReactomeiREACT_6926. Glutathione conjugation.

Names & Taxonomyi

Protein namesi
Recommended name:
Microsomal glutathione S-transferase 1 (EC:2.5.1.18)
Short name:
Microsomal GST-1
Alternative name(s):
Microsomal GST-I
Gene namesi
Name:MGST1
Synonyms:GST12, MGST
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 12

Organism-specific databases

HGNCiHGNC:7061. MGST1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini3 – 97Lumenal By similarity
Transmembranei10 – 3324Helical; By similarity
Add
BLAST
Topological domaini34 – 6229Cytoplasmic By similarity
Add
BLAST
Transmembranei63 – 9634Helical; By similarity
Add
BLAST
Topological domaini97 – 993Lumenal By similarity
Transmembranei100 – 12324Helical; By similarity
Add
BLAST
Topological domaini124 – 1285Cytoplasmic By similarity
Transmembranei129 – 14820Helical; By similarity
Add
BLAST
Topological domaini149 – 1557Lumenal By similarity

GO - Cellular componenti

  1. apical part of cell Source: Ensembl
  2. endoplasmic reticulum Source: UniProtKB
  3. endoplasmic reticulum membrane Source: Reactome
  4. integral component of membrane Source: UniProtKB
  5. mitochondrial inner membrane Source: Ensembl
  6. mitochondrial outer membrane Source: UniProtKB-SubCell
  7. mitochondrion Source: UniProtKB
  8. nucleus Source: Ensembl
  9. peroxisomal membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane, Microsome, Mitochondrion, Mitochondrion outer membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA30791.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed By similarity
Chaini2 – 155154Microsomal glutathione S-transferase 1
PRO_0000217736Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei42 – 421N6-acetyllysine By similarity
Modified residuei55 – 551N6-acetyllysine By similarity
Modified residuei60 – 601N6-acetyllysine By similarity

Post-translational modificationi

Peroxynitrite induces nitration at Tyr-93 which activates the enzyme By similarity.

Keywords - PTMi

Acetylation, Nitration

Proteomic databases

MaxQBiP10620.
PaxDbiP10620.
PRIDEiP10620.

PTM databases

PhosphoSiteiP10620.

Expressioni

Tissue specificityi

Highly expressed in liver.

Gene expression databases

ArrayExpressiP10620.
BgeeiP10620.
CleanExiHS_MGST1.
GenevestigatoriP10620.

Organism-specific databases

HPAiHPA044840.

Interactioni

Subunit structurei

Homotrimer; The trimer binds only one molecule of glutathione By similarity.

Binary interactionsi

WithEntry#Exp.IntActNotes
NELFBQ8WX922EBI-2691601,EBI-347721

Protein-protein interaction databases

BioGridi110413. 2 interactions.
IntActiP10620. 2 interactions.
STRINGi9606.ENSP00000010404.

Structurei

3D structure databases

ProteinModelPortaliP10620.
SMRiP10620. Positions 10-148.

Family & Domainsi

Sequence similaritiesi

Belongs to the MAPEG family.

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG71159.
HOGENOMiHOG000231759.
HOVERGENiHBG052470.
InParanoidiP10620.
KOiK00799.
OMAiLIHFRIF.
PhylomeDBiP10620.
TreeFamiTF105327.

Family and domain databases

Gene3Di1.20.120.550. 1 hit.
InterProiIPR023352. MAPEG-like_dom.
IPR001129. Membr-assoc_MAPEG.
[Graphical view]
PfamiPF01124. MAPEG. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P10620-1) [UniParc]FASTAAdd to Basket

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.

« Hide

MVDLTQVMDD EVFMAFASYA TIILSKMMLM STATAFYRLT RKVFANPEDC    50
VAFGKGENAK KYLRTDDRVE RVRRAHLNDL ENIIPFLGIG LLYSLSGPDP 100
STAILHFRLF VGARIYHTIA YLTPLPQPNR ALSFFVGYGV TLSMAYRLLK 150
SKLYL 155
Length:155
Mass (Da):17,599
Last modified:July 1, 1989 - v1
Checksum:i892A529C97E3C853
GO
Isoform 2 (identifier: P10620-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     75-155: AHLNDLENII...YRLLKSKLYL → IKQTLSIYLASSI

Note: No experimental confirmation available.

Show »
Length:87
Mass (Da):9,984
Checksum:i8F4C9AF76F18EF97
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei75 – 15581AHLND…SKLYL → IKQTLSIYLASSI in isoform 2.
VSP_046160Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
J03746 mRNA. Translation: AAA35934.1.
U46498, AF092926, U46497 Genomic DNA. Translation: AAC50711.1.
U71213, U71211, U71212 Genomic DNA. Translation: AAB17184.1.
BT006982 mRNA. Translation: AAP35628.1.
AY368173 Genomic DNA. Translation: AAQ55111.1.
AK291148 mRNA. Translation: BAF83837.1.
AC007528 Genomic DNA. No translation available.
AC007529 Genomic DNA. No translation available.
AC007552 Genomic DNA. No translation available.
CH471094 Genomic DNA. Translation: EAW96362.1.
CH471094 Genomic DNA. Translation: EAW96367.1.
BC005923 mRNA. Translation: AAH05923.1.
BC056863 mRNA. No translation available.
CCDSiCCDS58209.1. [P10620-2]
CCDS8677.1. [P10620-1]
PIRiB28083.
RefSeqiNP_001247440.1. NM_001260511.1. [P10620-1]
NP_001247441.1. NM_001260512.1.
NP_001254527.1. NM_001267598.1. [P10620-2]
NP_064696.1. NM_020300.4. [P10620-1]
NP_665707.1. NM_145764.2. [P10620-1]
NP_665734.1. NM_145791.2. [P10620-1]
NP_665735.1. NM_145792.2. [P10620-1]
UniGeneiHs.389700.

Genome annotation databases

EnsembliENST00000010404; ENSP00000010404; ENSG00000008394. [P10620-1]
ENST00000396207; ENSP00000379510; ENSG00000008394. [P10620-1]
ENST00000396209; ENSP00000379512; ENSG00000008394. [P10620-1]
ENST00000396210; ENSP00000379513; ENSG00000008394. [P10620-1]
ENST00000535309; ENSP00000438308; ENSG00000008394. [P10620-2]
GeneIDi4257.
KEGGihsa:4257.
UCSCiuc001rdf.3. human. [P10620-1]
uc031qgm.1. human.

Polymorphism databases

DMDMi121740.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
J03746 mRNA. Translation: AAA35934.1 .
U46498 , AF092926 , U46497 Genomic DNA. Translation: AAC50711.1 .
U71213 , U71211 , U71212 Genomic DNA. Translation: AAB17184.1 .
BT006982 mRNA. Translation: AAP35628.1 .
AY368173 Genomic DNA. Translation: AAQ55111.1 .
AK291148 mRNA. Translation: BAF83837.1 .
AC007528 Genomic DNA. No translation available.
AC007529 Genomic DNA. No translation available.
AC007552 Genomic DNA. No translation available.
CH471094 Genomic DNA. Translation: EAW96362.1 .
CH471094 Genomic DNA. Translation: EAW96367.1 .
BC005923 mRNA. Translation: AAH05923.1 .
BC056863 mRNA. No translation available.
CCDSi CCDS58209.1. [P10620-2 ]
CCDS8677.1. [P10620-1 ]
PIRi B28083.
RefSeqi NP_001247440.1. NM_001260511.1. [P10620-1 ]
NP_001247441.1. NM_001260512.1.
NP_001254527.1. NM_001267598.1. [P10620-2 ]
NP_064696.1. NM_020300.4. [P10620-1 ]
NP_665707.1. NM_145764.2. [P10620-1 ]
NP_665734.1. NM_145791.2. [P10620-1 ]
NP_665735.1. NM_145792.2. [P10620-1 ]
UniGenei Hs.389700.

3D structure databases

ProteinModelPortali P10620.
SMRi P10620. Positions 10-148.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 110413. 2 interactions.
IntActi P10620. 2 interactions.
STRINGi 9606.ENSP00000010404.

Chemistry

ChEMBLi CHEMBL1743184.
DrugBanki DB00143. Glutathione.

PTM databases

PhosphoSitei P10620.

Polymorphism databases

DMDMi 121740.

Proteomic databases

MaxQBi P10620.
PaxDbi P10620.
PRIDEi P10620.

Protocols and materials databases

DNASUi 4257.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000010404 ; ENSP00000010404 ; ENSG00000008394 . [P10620-1 ]
ENST00000396207 ; ENSP00000379510 ; ENSG00000008394 . [P10620-1 ]
ENST00000396209 ; ENSP00000379512 ; ENSG00000008394 . [P10620-1 ]
ENST00000396210 ; ENSP00000379513 ; ENSG00000008394 . [P10620-1 ]
ENST00000535309 ; ENSP00000438308 ; ENSG00000008394 . [P10620-2 ]
GeneIDi 4257.
KEGGi hsa:4257.
UCSCi uc001rdf.3. human. [P10620-1 ]
uc031qgm.1. human.

Organism-specific databases

CTDi 4257.
GeneCardsi GC12P016500.
HGNCi HGNC:7061. MGST1.
HPAi HPA044840.
MIMi 138330. gene.
neXtProti NX_P10620.
PharmGKBi PA30791.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG71159.
HOGENOMi HOG000231759.
HOVERGENi HBG052470.
InParanoidi P10620.
KOi K00799.
OMAi LIHFRIF.
PhylomeDBi P10620.
TreeFami TF105327.

Enzyme and pathway databases

Reactomei REACT_6926. Glutathione conjugation.

Miscellaneous databases

GeneWikii Microsomal_glutathione_S-transferase_1.
GenomeRNAii 4257.
NextBioi 16787.
PROi P10620.
SOURCEi Search...

Gene expression databases

ArrayExpressi P10620.
Bgeei P10620.
CleanExi HS_MGST1.
Genevestigatori P10620.

Family and domain databases

Gene3Di 1.20.120.550. 1 hit.
InterProi IPR023352. MAPEG-like_dom.
IPR001129. Membr-assoc_MAPEG.
[Graphical view ]
Pfami PF01124. MAPEG. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Gene expression of rat and human microsomal glutathione S-transferases."
    Dejong J.L., Morgenstern R., Joernvall H., Depierre J.W., Tu C.-P.D.
    J. Biol. Chem. 263:8430-8436(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Liver.
  2. "Structural organization of the human microsomal glutathione S-transferase gene (GST12)."
    Kelner M.J., Stokely M.N., Stovall N.E., Montoya M.A.
    Genomics 36:100-103(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Tissue: Foreskin.
  3. "Microsomal GST-I: genomic organization, expression, and alternative splicing of the human gene."
    Lee S.H., DeJong J.
    Biochim. Biophys. Acta 1446:389-396(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  4. "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] (ISOFORM 1).
  5. NIEHS SNPs program
    Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  6. "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.
    , 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] (ISOFORM 1).
  7. "The finished DNA sequence of human chromosome 12."
    Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.
    , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
    Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  9. "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 2).
    Tissue: Brain and Prostate.
  10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiMGST1_HUMAN
AccessioniPrimary (citable) accession number: P10620
Secondary accession number(s): A8K533, G5EA53
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: September 3, 2014
This is version 129 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 12
    Human chromosome 12: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi