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Q9Y2G1 - MRF_HUMAN

UniProt

Q9Y2G1 - MRF_HUMAN

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Protein

Myelin regulatory factor

Gene

MYRF

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Myelin regulatory factor: Consitutes a precursor of the transcription factor. Mediates the autocatalytic cleavage that releases the Myelin regulatory factor, N-terminal component that specifically activates transcription of central nervous system (CNS) myelin genes (PubMed:23966832).1 Publication
Myelin regulatory factor, C-terminal: Membrane-bound part that has no transcription factor activity and remains attached to the endoplasmic reticulum membrane following cleavage.1 Publication
Myelin regulatory factor, N-terminal: Transcription factor that specifically activates expression of myelin genes such as MBP, MOG, MAG and PLP1 during oligodendrocyte (OL) maturation, thereby playing a central role in oligodendrocyte maturation and CNS myelination. Specifically recognizes and binds DNA sequence 5'-CTGGYAC-3' in the regulatory regions of myelin-specific genes and directly activates their expression. Not only required during oligodendrocyte differentiation but is also required on an ongoing basis for the maintenance of expression of myelin genes and for the maintenance of a mature, viable oligodendrocyte phenotype (PubMed:23966832).1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei586 – 5872Cleavage; by autolysis1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi250 – 541292NDT80PROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  1. DNA binding Source: UniProtKB-KW
  2. peptidase activity Source: UniProtKB-KW
  3. sequence-specific DNA binding transcription factor activity Source: InterPro

GO - Biological processi

  1. central nervous system myelination Source: UniProtKB
  2. central nervous system myelin maintenance Source: UniProtKB
  3. oligodendrocyte development Source: UniProtKB
  4. oligodendrocyte differentiation Source: UniProtKB
  5. positive regulation of myelination Source: UniProtKB
  6. positive regulation of transcription, DNA-templated Source: UniProtKB
  7. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Activator, Hydrolase, Protease

Keywords - Biological processi

Differentiation, Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Myelin regulatory factor (EC:3.4.-.-)
Alternative name(s):
Myelin gene regulatory factor
Cleaved into the following 2 chains:
Myelin regulatory factor, N-terminal
Myelin regulatory factor, C-terminal
Gene namesi
Name:MYRF
Synonyms:C11orf9, KIAA0954, MRF
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
ProteomesiUP000005640: Chromosome 11

Organism-specific databases

HGNCiHGNC:1181. MYRF.

Subcellular locationi

Chain Myelin regulatory factor : Endoplasmic reticulum membrane; Single-pass membrane protein
Chain Myelin regulatory factor, N-terminal : Nucleus. Cytoplasm
Note: Translocates from the cytoplasm to the nucleus upon autocatalytic cleavage.
Chain Myelin regulatory factor, C-terminal : Endoplasmic reticulum membrane; Single-pass membrane protein

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 768768CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei769 – 78921HelicalSequence AnalysisAdd
BLAST
Topological domaini790 – 1151362LumenalSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. endoplasmic reticulum membrane Source: UniProtKB-SubCell
  2. integral component of membrane Source: UniProtKB-KW
  3. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Endoplasmic reticulum, Membrane, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi587 – 5871S → A: Prevents autocatalytic cleavage and generation of Myelin regulatory factor, N-terminal part. 1 Publication
Mutagenesisi588 – 5881D → A: Reduces autocatalytic cleavage and generation of Myelin regulatory factor, N-terminal part. 1 Publication
Mutagenesisi592 – 5921K → A: Prevents autocatalytic cleavage and generation of Myelin regulatory factor, N-terminal part. 1 Publication
Mutagenesisi608 – 6081S → A: Does not affect autocatalytic cleavage. 1 Publication
Mutagenesisi635 – 6351G → A: Reduces autocatalytic cleavage and generation of Myelin regulatory factor, N-terminal part. 1 Publication
Mutagenesisi688 – 6881L → A: Does not affect autocatalytic cleavage. 1 Publication
Mutagenesisi699 – 6991L → A: Prevents autocatalytic cleavage and generation of Myelin regulatory factor, N-terminal part. 1 Publication

Organism-specific databases

PharmGKBiPA25500.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 11511151Myelin regulatory factorPRO_0000318919Add
BLAST
Chaini1 – 586586Myelin regulatory factor, N-terminalPRO_0000424310Add
BLAST
Chaini587 – 1151565Myelin regulatory factor, C-terminalPRO_0000424311Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei123 – 1231N6-acetyllysine1 Publication
Glycosylationi919 – 9191N-linked (GlcNAc...)Sequence Analysis
Glycosylationi1043 – 10431N-linked (GlcNAc...)Sequence Analysis
Glycosylationi1065 – 10651N-linked (GlcNAc...)Sequence Analysis
Glycosylationi1129 – 11291N-linked (GlcNAc...)Sequence Analysis

Post-translational modificationi

Myelin regulatory factor, C-terminal: Glycosylated.1 Publication
Myelin regulatory factor: Follows autocatalytic cleavage via the peptidase S74 domain. Autoprocessing is apparently constitutive and is essential for transcriptional activity.1 Publication

Keywords - PTMi

Acetylation, Autocatalytic cleavage, Glycoprotein

Proteomic databases

MaxQBiQ9Y2G1.
PaxDbiQ9Y2G1.
PRIDEiQ9Y2G1.

PTM databases

PhosphoSiteiQ9Y2G1.

Expressioni

Tissue specificityi

Expressed in lung, ARPE-19 cell line, brainstem, uterus and, to a lesser extent, in basal ganglion and liver. Weakly expressed in cerebellum and retina.1 Publication

Gene expression databases

BgeeiQ9Y2G1.
CleanExiHS_C11orf9.
ExpressionAtlasiQ9Y2G1. baseline and differential.
GenevestigatoriQ9Y2G1.

Organism-specific databases

HPAiHPA018310.

Interactioni

Subunit structurei

Homotrimer.1 Publication

Protein-protein interaction databases

BioGridi107203. 1 interaction.
DIPiDIP-60483N.
STRINGi9606.ENSP00000278836.

Structurei

3D structure databases

ProteinModelPortaliQ9Y2G1.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini587 – 696110Peptidase S74Add
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili680 – 71132Sequence AnalysisAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi254 – 2574Nuclear localization signal
Motifi491 – 4944Nuclear localization signal

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi77 – 330254Pro-richAdd
BLAST

Domaini

Myelin regulatory factor, N-terminal: The nuclear localization signals mediate translocation to the nucleus.1 Publication
Myelin regulatory factor: The peptidase S74 domain, also named Intramolecular Chaperone Auto-processed (ICA) domain or Intramolecuar Chaperone Domain (ICD), has protease activity and mediates autocatalytic processing of the protein to generate the Myelin regulatory factor, N-terminal active transcription factor and the Myelin regulatory factor, C-terminal components.1 Publication

Sequence similaritiesi

Belongs to the MRF family.Curated
Contains 1 NDT80 DNA-binding domain.PROSITE-ProRule annotation
Contains 1 peptidase S74 domain.Curated

Keywords - Domaini

Coiled coil, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG253930.
GeneTreeiENSGT00530000063626.
HOGENOMiHOG000111718.
InParanoidiQ9Y2G1.
OMAiSTNRSGP.
OrthoDBiEOG77M8N4.
PhylomeDBiQ9Y2G1.
TreeFamiTF312888.

Family and domain databases

Gene3Di2.60.40.1390. 1 hit.
InterProiIPR026933. MRF.
IPR026932. MRF_C1.
IPR025719. MRF_C2.
IPR024061. NDT80_DNA-bd_dom.
IPR008967. p53-like_TF_DNA-bd.
IPR030392. S74_ICA.
[Graphical view]
PANTHERiPTHR13029:SF16. PTHR13029:SF16. 1 hit.
PfamiPF13887. MRF_C1. 1 hit.
PF13888. MRF_C2. 1 hit.
PF05224. NDT80_PhoG. 1 hit.
[Graphical view]
SUPFAMiSSF49417. SSF49417. 1 hit.
PROSITEiPS51688. ICA. 1 hit.
PS51517. NDT80. 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: Q9Y2G1-1) [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

        10         20         30         40         50
MEVVDETEAL QRFFEGHDIN GALEPSNIDT SILEEYISKE DASDLCFPDI 
        60         70         80         90        100
SAPASSASYS HGQPAMPGSS GVHHLSPPGG GPSPGRHGPL PPPGYGTPLN 
       110        120        130        140        150
CNNNNGMGAA PKPFPGGTGP PIKAEPKAPY APGTLPDSPP DSGSEAYSPQ 
       160        170        180        190        200
QVNEPHLLRT ITPETLCHVG VPSRLEHPPP PPAHLPGPPP PPPPPPHYPV 
       210        220        230        240        250
LQRDLYMKAE PPIPHYAAMG QGLVPTDLHH TQQSQMLHQL LQQHGAELPT 
       260        270        280        290        300
HPSKKRKHSE SPPSTLNAQM LNGMIKQEPG TVTALPLHPT RAPSPPWPPQ 
       310        320        330        340        350
GPLSPGPGSL PLSIARVQTP PWHPPGAPSP GLLQDSDSLS GSYLDPNYQS 
       360        370        380        390        400
IKWQPHQQNK WATLYDANYK ELPMLTYRVD ADKGFNFSVG DDAFVCQKKN 
       410        420        430        440        450
HFQVTVYIGM LGEPKYVKTP EGLKPLDCFY LKLHGVKLEA LNQSINIEQS 
       460        470        480        490        500
QSDRSKRPFN PVTVNLPPEQ VTKVTVGRLH FSETTANNMR KKGKPNPDQR 
       510        520        530        540        550
YFMLVVALQA HAQNQNYTLA AQISERIIVR ASNPGQFESD SDVLWQRAQV 
       560        570        580        590        600
PDTVFHHGRV GINTDRPDEA LVVHGNVKVM GSLMHPSDLR AKEHVQEVDT 
       610        620        630        640        650
TEQLKRISRM RLVHYRYKPE FAASAGIEAT APETGVIAQE VKEILPEAVK 
       660        670        680        690        700
DTGDMVFANG KTIENFLVVN KERIFMENVG AVKELCKLTD NLETRIDELE 
       710        720        730        740        750
RWSHKLAKLR RLDSLKSTGS SGAFSHAGSQ FSRAGSVPHK KRPPKVASKS 
       760        770        780        790        800
SSVVPDQACI SQRFLQGTII ALVVVMAFSV VSMSTLYVLS LRTEEDLVDT 
       810        820        830        840        850
DGSFAVSTSC LLALLRPQPP GGSEALCPWS SQSFGTTQLR QSPLTTGLPG 
       860        870        880        890        900
IQPSLLLVTT SLTSSAPGSA VRTLDMCSSH PCPVICCSSP TTNPTTGPSL 
       910        920        930        940        950
GPSFNPGHVL SPSPSPSTNR SGPSQMALLP VTNIRAKSWG LSVNGIGHSK 
       960        970        980        990       1000
HHKSLEPLAS PAVPFPGGQG KAKNSPSLGF HGRARRGALQ SSVGPAEPTW 
      1010       1020       1030       1040       1050
AQGQSASLLA EPVPSLTSIQ VLENSMSITS QYCAPGDACR PGNFTYHIPV 
      1060       1070       1080       1090       1100
SSGTPLHLSL TLQMNSSSPV SVVLCSLRSK EEPCEEGSLP QSLHTHQDTQ 
      1110       1120       1130       1140       1150
GTSHRWPITI LSFREFTYHF RVALLGQANC SSEALAQPAT DYHFHFYRLC 

D
Length:1,151
Mass (Da):124,397
Last modified:February 26, 2008 - v3
Checksum:i9875DE9D72B6C50C
GO
Isoform 2 (identifier: Q9Y2G1-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-15: MEVVDETEALQRFFE → MHWLPA
     803-829: SFAVSTSCLLALLRPQPPGGSEALCPW → R
     1006-1010: Missing.

Note: No experimental confirmation available.

Show »
Length:1,111
Mass (Da):120,225
Checksum:i5B9CAAD3EC8C8B03
GO

Sequence cautioni

The sequence BAA76798.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti478 – 4847RLHFSET → GGCIQRD in AAB92668. (PubMed:9615227)Curated
Sequence conflicti606 – 6061R → K in AAB92668. (PubMed:9615227)Curated
Sequence conflicti657 – 6582FA → LP in AAB92668. (PubMed:9615227)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti723 – 7231A → T.
Corresponds to variant rs34038946 [ dbSNP | Ensembl ].		VAR_038907

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 1515MEVVD…QRFFE → MHWLPA in isoform 2. 1 PublicationVSP_031300Add
BLAST
Alternative sequencei803 – 82927SFAVS…ALCPW → R in isoform 2. 1 PublicationVSP_031301Add
BLAST
Alternative sequencei1006 – 10105Missing in isoform 2. 1 PublicationVSP_031302

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF086762 mRNA. Translation: AAF28400.1.
AB023171 mRNA. Translation: BAA76798.2. Different initiation.
CH471076 Genomic DNA. Translation: EAW73968.1.
AF038536 mRNA. Translation: AAB92668.1.
CCDSiCCDS31579.1. [Q9Y2G1-2]
CCDS44622.1. [Q9Y2G1-1]
RefSeqiNP_001120864.1. NM_001127392.2. [Q9Y2G1-1]
NP_037411.1. NM_013279.3. [Q9Y2G1-2]
UniGeneiHs.473109.

Genome annotation databases

EnsembliENST00000265460; ENSP00000265460; ENSG00000124920. [Q9Y2G1-2]
ENST00000278836; ENSP00000278836; ENSG00000124920. [Q9Y2G1-1]
GeneIDi745.
KEGGihsa:745.
UCSCiuc001nsc.1. human. [Q9Y2G1-1]
uc001nse.1. human. [Q9Y2G1-2]

Polymorphism databases

DMDMi182637560.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF086762 mRNA. Translation: AAF28400.1.
AB023171 mRNA. Translation: BAA76798.2. Different initiation.
CH471076 Genomic DNA. Translation: EAW73968.1.
AF038536 mRNA. Translation: AAB92668.1.
CCDSiCCDS31579.1. [Q9Y2G1-2]
CCDS44622.1. [Q9Y2G1-1]
RefSeqiNP_001120864.1. NM_001127392.2. [Q9Y2G1-1]
NP_037411.1. NM_013279.3. [Q9Y2G1-2]
UniGeneiHs.473109.

3D structure databases

ProteinModelPortaliQ9Y2G1.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107203. 1 interaction.
DIPiDIP-60483N.
STRINGi9606.ENSP00000278836.

PTM databases

PhosphoSiteiQ9Y2G1.

Polymorphism databases

DMDMi182637560.

Proteomic databases

MaxQBiQ9Y2G1.
PaxDbiQ9Y2G1.
PRIDEiQ9Y2G1.

Protocols and materials databases

DNASUi745.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000265460; ENSP00000265460; ENSG00000124920. [Q9Y2G1-2]
ENST00000278836; ENSP00000278836; ENSG00000124920. [Q9Y2G1-1]
GeneIDi745.
KEGGihsa:745.
UCSCiuc001nsc.1. human. [Q9Y2G1-1]
uc001nse.1. human. [Q9Y2G1-2]

Organism-specific databases

CTDi745.
GeneCardsiGC11P061521.
HGNCiHGNC:1181. MYRF.
HPAiHPA018310.
MIMi608329. gene.
neXtProtiNX_Q9Y2G1.
PharmGKBiPA25500.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG253930.
GeneTreeiENSGT00530000063626.
HOGENOMiHOG000111718.
InParanoidiQ9Y2G1.
OMAiSTNRSGP.
OrthoDBiEOG77M8N4.
PhylomeDBiQ9Y2G1.
TreeFamiTF312888.

Miscellaneous databases

GeneWikiiMyelin_gene_Regulatory_Factor.
GenomeRNAii745.
NextBioi3016.
SOURCEiSearch...

Gene expression databases

BgeeiQ9Y2G1.
CleanExiHS_C11orf9.
ExpressionAtlasiQ9Y2G1. baseline and differential.
GenevestigatoriQ9Y2G1.

Family and domain databases

Gene3Di2.60.40.1390. 1 hit.
InterProiIPR026933. MRF.
IPR026932. MRF_C1.
IPR025719. MRF_C2.
IPR024061. NDT80_DNA-bd_dom.
IPR008967. p53-like_TF_DNA-bd.
IPR030392. S74_ICA.
[Graphical view]
PANTHERiPTHR13029:SF16. PTHR13029:SF16. 1 hit.
PfamiPF13887. MRF_C1. 1 hit.
PF13888. MRF_C2. 1 hit.
PF05224. NDT80_PhoG. 1 hit.
[Graphical view]
SUPFAMiSSF49417. SSF49417. 1 hit.
PROSITEiPS51688. ICA. 1 hit.
PS51517. NDT80. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "cDNA cloning and genomic structure of a novel gene (C11orf9) localized to chromosome 11q12-->q13.1 which encodes a highly conserved, potential membrane-associated protein."
    Stoehr H., Marquardt A., White K., Weber B.H.F.
    Cytogenet. Cell Genet. 88:211-216(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), TISSUE SPECIFICITY.
  2. "Prediction of the coding sequences of unidentified human genes. XIII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
    Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
    DNA Res. 6:63-70(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Brain.
  3. "Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones."
    Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.
    DNA Res. 9:99-106(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: SEQUENCE REVISION.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "Transcript mapping of the human chromosome 11q12-q13.1 gene-rich region identifies several newly described conserved genes."
    Cooper P.R., Nowak N.J., Higgins M.J., Church D.M., Shows T.B.
    Genomics 49:419-429(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 476-660.
  6. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-123, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  7. "A bacteriophage tailspike domain promotes self-cleavage of a human membrane-bound transcription factor, the myelin regulatory factor MYRF."
    Li Z., Park Y., Marcotte E.M.
    PLoS Biol. 11:E1001624-E1001624(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, SUBUNIT, PROTEOLYTIC PROCESSING, GLYCOSYLATION, AUTOCATALYTIC CLEAVAGE, TOPOLOGY, MUTAGENESIS OF SER-587; ASP-588; LYS-592; SER-608; GLY-635; LEU-688 AND LEU-699, FUNCTION, DOMAIN.
+Additional computationally mapped references.

Entry informationi

Entry nameiMRF_HUMAN
AccessioniPrimary (citable) accession number: Q9Y2G1
Secondary accession number(s): O43582, Q9P1Q6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 26, 2008
Last sequence update: February 26, 2008
Last modified: February 4, 2015
This is version 95 of the entry and version 3 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 11
    Human chromosome 11: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. Peptidase families
    Classification of peptidase families and list of entries
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.