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Protein

Endoplasmic reticulum metallopeptidase 1

Gene

ERMP1

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

Functioni

Within the ovary, required for the organization of somatic cells and oocytes into discrete follicular structures.By similarity

Cofactori

Zn2+By similarityNote: Binds 2 Zn2+ ions per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi205 – 2051Zinc 1; catalyticBy similarity
Metal bindingi217 – 2171Zinc 1; catalyticBy similarity
Metal bindingi217 – 2171Zinc 2; catalyticBy similarity
Active sitei251 – 2511Proton acceptorBy similarity
Metal bindingi252 – 2521Zinc 2; catalyticBy similarity
Metal bindingi278 – 2781Zinc 1; catalyticBy similarity
Sitei353 – 3531Transition state stabilizerBy similarity
Metal bindingi354 – 3541Zinc 2; catalyticBy similarity

GO - Molecular functioni

  1. metal ion binding Source: UniProtKB-KW
  2. metallopeptidase activity Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Metalloprotease, Protease

Keywords - Ligandi

Metal-binding, Zinc

Protein family/group databases

MEROPSiM28.018.

Names & Taxonomyi

Protein namesi
Recommended name:
Endoplasmic reticulum metallopeptidase 1By similarityImported (EC:3.4.-.-Curated)
Alternative name(s):
Felix-inaBy similarity
Gene namesi
Name:ERMP1Imported
Synonyms:FXNABy similarity, KIAA18151 Publication
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 9

Organism-specific databases

HGNCiHGNC:23703. ERMP1.

Subcellular locationi

  1. Endoplasmic reticulum membrane By similarity; Multi-pass membrane protein Sequence Analysis

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 6363CytoplasmicCuratedAdd
BLAST
Transmembranei64 – 8421Helical; Name=1Sequence AnalysisAdd
BLAST
Topological domaini85 – 399315LumenalCuratedAdd
BLAST
Transmembranei400 – 42021Helical; Name=2Sequence AnalysisAdd
BLAST
Topological domaini421 – 45737CytoplasmicCuratedAdd
BLAST
Transmembranei458 – 47821Helical; Name=3Sequence AnalysisAdd
BLAST
Topological domaini479 – 48911LumenalCuratedAdd
BLAST
Transmembranei490 – 51021Helical; Name=4Sequence AnalysisAdd
BLAST
Topological domaini511 – 5199CytoplasmicCurated
Transmembranei520 – 54021Helical; Name=5Sequence AnalysisAdd
BLAST
Topological domaini541 – 5411LumenalCurated
Transmembranei542 – 56221Helical; Name=6Sequence AnalysisAdd
BLAST
Topological domaini563 – 57917CytoplasmicCuratedAdd
BLAST
Transmembranei580 – 60021Helical; Name=7Sequence AnalysisAdd
BLAST
Topological domaini601 – 62121LumenalCuratedAdd
BLAST
Transmembranei622 – 64221Helical; Name=8Sequence AnalysisAdd
BLAST
Topological domaini643 – 6519CytoplasmicCurated
Transmembranei652 – 67221Helical; Name=9Sequence AnalysisAdd
BLAST
Topological domaini673 – 904232LumenalCuratedAdd
BLAST

GO - Cellular componenti

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

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA162385366.

Polymorphism and mutation databases

BioMutaiERMP1.
DMDMi117949602.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 904904Endoplasmic reticulum metallopeptidase 1PRO_0000259492Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine1 Publication
Glycosylationi182 – 1821N-linked (GlcNAc...)PROSITE-ProRule annotation
Disulfide bondi204 ↔ 222By similarity
Glycosylationi730 – 7301N-linked (GlcNAc...)1 Publication

Keywords - PTMi

Acetylation, Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiQ7Z2K6.
PaxDbiQ7Z2K6.
PeptideAtlasiQ7Z2K6.
PRIDEiQ7Z2K6.

PTM databases

PhosphoSiteiQ7Z2K6.

Expressioni

Gene expression databases

BgeeiQ7Z2K6.
CleanExiHS_ERMP1.
ExpressionAtlasiQ7Z2K6. baseline and differential.
GenevestigatoriQ7Z2K6.

Organism-specific databases

HPAiHPA020584.

Interactioni

Protein-protein interaction databases

BioGridi123025. 15 interactions.
STRINGi9606.ENSP00000340427.

Structurei

3D structure databases

ProteinModelPortaliQ7Z2K6.
SMRiQ7Z2K6. Positions 185-373.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase M28 family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG2234.
GeneTreeiENSGT00530000063839.
HOGENOMiHOG000230679.
HOVERGENiHBG096075.
InParanoidiQ7Z2K6.
OMAiVHCGFLT.
OrthoDBiEOG78H3TS.
PhylomeDBiQ7Z2K6.
TreeFamiTF314836.

Family and domain databases

InterProiIPR007484. Peptidase_M28.
[Graphical view]
PfamiPF04389. Peptidase_M28. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q7Z2K6-1) [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
MEWGSESAAV RRHRVGVERR EGAAAAPPPE REARAQEPLV DGCSGGGRTR
60 70 80 90 100
KRSPGGSGGA SRGAGTGLSE VRAALGLALY LIALRTLVQL SLQQLVLRGA
110 120 130 140 150
AGHRGEFDAL QARDYLEHIT SIGPRTTGSP ENEILTVHYL LEQIKLIEVQ
160 170 180 190 200
SNSLHKISVD VQRPTGSFSI DFLGGFTSYY DNITNVVVKL EPRDGAQHAV
210 220 230 240 250
LANCHFDSVA NSPGASDDAV SCSVMLEVLR VLSTSSEALH HAVIFLFNGA
260 270 280 290 300
EENVLQASHG FITQHPWASL IRAFINLEAA GVGGKELVFQ TGPENPWLVQ
310 320 330 340 350
AYVSAAKHPF ASVVAQEVFQ SGIIPSDTDF RIYRDFGNIP GIDLAFIENG
360 370 380 390 400
YIYHTKYDTA DRILTDSIQR AGDNILAVLK HLATSDMLAA ASKYRHGNMV
410 420 430 440 450
FFDVLGLFVI AYPSRIGSII NYMVVMGVVL YLGKKFLQPK HKTGNYKKDF
460 470 480 490 500
LCGLGITLIS WFTSLVTVLI IAVFISLIGQ SLSWYNHFYV SVCLYGTATV
510 520 530 540 550
AKIILIHTLA KRFYYMNASA QYLGEVFFDI SLFVHCCFLV TLTYQGLCSA
560 570 580 590 600
FISAVWVAFP LLTKLCVHKD FKQHGAQGKF IAFYLLGMFI PYLYALYLIW
610 620 630 640 650
AVFEMFTPIL GRSGSEIPPD VVLASILAGC TMILSSYFIN FIYLAKSTKK
660 670 680 690 700
TMLTLTLVCA ITFLLVCSGT FFPYSSNPAN PKPKRVFLQH MTRTFHDLEG
710 720 730 740 750
NAVKRDSGIW INGFDYTGIS HITPHIPEIN DSIRAHCEEN APLCGFPWYL
760 770 780 790 800
PVHFLIRKNW YLPAPEVSPR NPPHFRLISK EQTPWDSIKL TFEATGPSHM
810 820 830 840 850
SFYVRAHKGS TLSQWSLGNG TPVTSKGGDY FVFYSHGLQA SAWQFWIEVQ
860 870 880 890 900
VSEEHPEGMV TVAIAAHYLS GEDKRSPQLD ALKEKFPDWT FPSAWVCTYD

LFVF
Length:904
Mass (Da):100,231
Last modified:October 31, 2006 - v2
Checksum:i3A723027C53092EF
GO
Isoform 2 (identifier: Q7Z2K6-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-224: Missing.
     576-904: Missing.

Note: No experimental confirmation available.

Show »
Length:351
Mass (Da):39,151
Checksum:iB02E3CEF1788BDFB
GO

Sequence cautioni

The sequence BAB15604.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti575 – 5751G → D in BAG52673 (PubMed:14702039).Curated
Sequence conflicti728 – 7281E → A in BAB15604 (PubMed:14702039).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti44 – 441S → N.
Corresponds to variant rs13284203 [ dbSNP | Ensembl ].
VAR_028945

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 224224Missing in isoform 2. 1 PublicationVSP_056121Add
BLAST
Alternative sequencei576 – 904329Missing in isoform 2. 1 PublicationVSP_056122Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK026962 mRNA. Translation: BAB15604.1. Different initiation.
AK093217 mRNA. Translation: BAG52673.1.
AK127218 mRNA. Translation: BAG54455.1.
AL136980 Genomic DNA. No translation available.
AL365360 Genomic DNA. No translation available.
BC031630 mRNA. Translation: AAH31630.2.
BC136771 mRNA. Translation: AAI36772.1.
BC136773 mRNA. Translation: AAI36774.1.
AB058718 mRNA. Translation: BAB47444.2.
CCDSiCCDS34983.1. [Q7Z2K6-1]
RefSeqiNP_079172.2. NM_024896.2. [Q7Z2K6-1]
UniGeneiHs.591078.

Genome annotation databases

EnsembliENST00000339450; ENSP00000340427; ENSG00000099219. [Q7Z2K6-1]
ENST00000462592; ENSP00000417160; ENSG00000099219. [Q7Z2K6-1]
GeneIDi79956.
KEGGihsa:79956.
UCSCiuc003zjm.1. human. [Q7Z2K6-1]

Polymorphism and mutation databases

BioMutaiERMP1.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK026962 mRNA. Translation: BAB15604.1. Different initiation.
AK093217 mRNA. Translation: BAG52673.1.
AK127218 mRNA. Translation: BAG54455.1.
AL136980 Genomic DNA. No translation available.
AL365360 Genomic DNA. No translation available.
BC031630 mRNA. Translation: AAH31630.2.
BC136771 mRNA. Translation: AAI36772.1.
BC136773 mRNA. Translation: AAI36774.1.
AB058718 mRNA. Translation: BAB47444.2.
CCDSiCCDS34983.1. [Q7Z2K6-1]
RefSeqiNP_079172.2. NM_024896.2. [Q7Z2K6-1]
UniGeneiHs.591078.

3D structure databases

ProteinModelPortaliQ7Z2K6.
SMRiQ7Z2K6. Positions 185-373.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi123025. 15 interactions.
STRINGi9606.ENSP00000340427.

Protein family/group databases

MEROPSiM28.018.

PTM databases

PhosphoSiteiQ7Z2K6.

Polymorphism and mutation databases

BioMutaiERMP1.
DMDMi117949602.

Proteomic databases

MaxQBiQ7Z2K6.
PaxDbiQ7Z2K6.
PeptideAtlasiQ7Z2K6.
PRIDEiQ7Z2K6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000339450; ENSP00000340427; ENSG00000099219. [Q7Z2K6-1]
ENST00000462592; ENSP00000417160; ENSG00000099219. [Q7Z2K6-1]
GeneIDi79956.
KEGGihsa:79956.
UCSCiuc003zjm.1. human. [Q7Z2K6-1]

Organism-specific databases

CTDi79956.
GeneCardsiGC09M005756.
H-InvDBHIX0007903.
HGNCiHGNC:23703. ERMP1.
HPAiHPA020584.
MIMi611156. gene.
neXtProtiNX_Q7Z2K6.
PharmGKBiPA162385366.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG2234.
GeneTreeiENSGT00530000063839.
HOGENOMiHOG000230679.
HOVERGENiHBG096075.
InParanoidiQ7Z2K6.
OMAiVHCGFLT.
OrthoDBiEOG78H3TS.
PhylomeDBiQ7Z2K6.
TreeFamiTF314836.

Miscellaneous databases

GenomeRNAii79956.
NextBioi69937.
PROiQ7Z2K6.
SOURCEiSearch...

Gene expression databases

BgeeiQ7Z2K6.
CleanExiHS_ERMP1.
ExpressionAtlasiQ7Z2K6. baseline and differential.
GenevestigatoriQ7Z2K6.

Family and domain databases

InterProiIPR007484. Peptidase_M28.
[Graphical view]
PfamiPF04389. Peptidase_M28. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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] (ISOFORMS 1 AND 2).
    Tissue: Hepatoma, Hippocampus and Testis.
  2. "DNA sequence and analysis of human chromosome 9."
    Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L.
    , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
    Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "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] (ISOFORM 1).
    Tissue: Brain.
  4. "Prediction of the coding sequences of unidentified human genes. XX. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
    Nagase T., Nakayama M., Nakajima D., Kikuno R., Ohara O.
    DNA Res. 8:85-95(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 24-904 (ISOFORM 1).
    Tissue: Brain.
  5. Ohara O., Nagase T., Kikuno R.
    Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION.
  6. "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-730.
    Tissue: Liver.
  7. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiERMP1_HUMAN
AccessioniPrimary (citable) accession number: Q7Z2K6
Secondary accession number(s): B2RNA4
, B3KSB1, Q8N5T5, Q9H5M1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 31, 2006
Last sequence update: October 31, 2006
Last modified: April 29, 2015
This is version 88 of the entry and version 2 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 9
    Human chromosome 9: 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.