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Protein

Signal peptide peptidase-like 2A

Gene

SPPL2A

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

Functioni

Intramembrane-cleaving aspartic protease (I-CLiP) that cleaves type II membrane signal peptides in the hydrophobic plane of the membrane. Functions in FASLG, ITM2B and TNF processing (PubMed:16829952, PubMed:16829951, PubMed:17557115, PubMed:17965014). Catalyzes the intramembrane cleavage of the anchored fragment of shed TNF-alpha (TNF), which promotes the release of the intracellular domain (ICD) for signaling to the nucleus (PubMed:16829952). Also responsible for the intramembrane cleavage of Fas antigen ligand FASLG, which promotes the release of the intracellular FasL domain (FasL ICD) (PubMed:17557115). May play a role in the regulation of innate and adaptive immunity (PubMed:16829952). Catalyzes the intramembrane cleavage of the simian foamy virus envelope glycoprotein gp130 independently of prior ectodomain shedding by furin or furin-like proprotein convertase (PC)-mediated cleavage proteolysis (PubMed:23132852).5 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei351 – 3511By similarity
Active sitei412 – 4121By similarity

GO - Molecular functioni

  • aspartic endopeptidase activity, intramembrane cleaving Source: UniProtKB
  • protein homodimerization activity Source: UniProtKB

GO - Biological processi

  • membrane protein ectodomain proteolysis Source: UniProtKB
  • membrane protein intracellular domain proteolysis Source: UniProtKB
  • membrane protein proteolysis Source: UniProtKB
  • regulation of immune response Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease

Protein family/group databases

MEROPSiA22.007.
TCDBi1.A.54.3.2. the presenilin er ca(2+) leak channel (presenilin) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Signal peptide peptidase-like 2A1 PublicationImported (EC:3.4.23.-)
Short name:
SPP-like 2A1 Publication
Short name:
SPPL2a1 Publication
Alternative name(s):
Intramembrane protease 31 Publication
Short name:
IMP-31 Publication
Presenilin-like protein 2
Gene namesi
Name:SPPL2A1 PublicationImported
Synonyms:IMP31 Publication, PSL2
ORF Names:PSEC0147
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 15

Organism-specific databases

HGNCiHGNC:30227. SPPL2A.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini26 – 172147Lumenal1 PublicationAdd
BLAST
Transmembranei173 – 19321HelicalSequence AnalysisAdd
BLAST
Topological domaini194 – 22027CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei221 – 24121HelicalSequence AnalysisAdd
BLAST
Topological domaini242 – 2476LumenalSequence Analysis
Transmembranei248 – 26821HelicalSequence AnalysisAdd
BLAST
Topological domaini269 – 28517CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei286 – 30621HelicalSequence AnalysisAdd
BLAST
Topological domaini307 – 3115LumenalSequence Analysis
Transmembranei312 – 33221HelicalSequence AnalysisAdd
BLAST
Topological domaini333 – 3408CytoplasmicSequence Analysis
Transmembranei341 – 36121HelicalSequence AnalysisAdd
BLAST
Topological domaini362 – 39938Lumenal1 PublicationAdd
BLAST
Transmembranei400 – 42021HelicalSequence AnalysisAdd
BLAST
Topological domaini421 – 43717CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei438 – 45821HelicalSequence AnalysisAdd
BLAST
Topological domaini459 – 4602LumenalSequence Analysis
Transmembranei461 – 48121HelicalSequence AnalysisAdd
BLAST
Topological domaini482 – 52039Cytoplasmic1 PublicationAdd
BLAST

GO - Cellular componenti

  • extracellular exosome Source: UniProtKB
  • Golgi-associated vesicle membrane Source: UniProtKB
  • integral component of cytoplasmic side of endoplasmic reticulum membrane Source: UniProtKB
  • integral component of lumenal side of endoplasmic reticulum membrane Source: UniProtKB
  • late endosome membrane Source: UniProtKB-SubCell
  • lysosomal membrane Source: UniProtKB
  • membrane Source: UniProtKB
  • plasma membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Endosome, Lysosome, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi412 – 4121D → A: Loss of intramembrane-cleaving activity toward FASLG, ITM2B, TNF and the simian foamy virus envelope glycoprotein gp130. 4 Publications

Polymorphism and mutation databases

BioMutaiSPPL2A.
DMDMi25008981.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 25251 PublicationAdd
BLAST
Chaini26 – 520495Signal peptide peptidase-like 2APRO_0000073910Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi58 – 581N-linked (GlcNAc...)Sequence Analysis
Glycosylationi66 – 661N-linked (GlcNAc...)Sequence Analysis
Glycosylationi74 – 741N-linked (GlcNAc...)Sequence Analysis
Glycosylationi116 – 1161N-linked (GlcNAc...)Sequence Analysis
Glycosylationi126 – 1261N-linked (GlcNAc...)Sequence Analysis
Glycosylationi149 – 1491N-linked (GlcNAc...)Sequence Analysis
Glycosylationi155 – 1551N-linked (GlcNAc...) (complex)1 Publication

Post-translational modificationi

Glycosylated.2 Publications

Keywords - PTMi

Glycoprotein

Proteomic databases

MaxQBiQ8TCT8.
PaxDbiQ8TCT8.
PeptideAtlasiQ8TCT8.
PRIDEiQ8TCT8.

PTM databases

PhosphoSiteiQ8TCT8.

Expressioni

Tissue specificityi

Ubiquitous.1 Publication

Gene expression databases

BgeeiQ8TCT8.
ExpressionAtlasiQ8TCT8. baseline and differential.
GenevisibleiQ8TCT8. HS.

Organism-specific databases

HPAiHPA036062.

Interactioni

Subunit structurei

Interacts with ITM2B (PubMed:17965014).1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
SGTAO437654EBI-750784,EBI-347996

Protein-protein interaction databases

BioGridi124328. 3 interactions.
IntActiQ8TCT8. 4 interactions.
MINTiMINT-1465822.
STRINGi9606.ENSP00000261854.

Structurei

3D structure databases

ProteinModelPortaliQ8TCT8.
SMRiQ8TCT8. Positions 68-163.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini63 – 15189PAAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi463 – 4653PAL
Motifi495 – 4984YXXo lysosomal targeting motif

Domaini

The PAL motif is required for normal active site conformation. The catalytic domains embedded in the membrane are in the opposite orientation to that of the presenilin protein family; therefore, it is predicted to cleave type II-oriented substrate peptides like the prototypic protease SPP. The C-terminal tail is necessary for lysosomal transport.By similarity

Sequence similaritiesi

Belongs to the peptidase A22B family.Curated

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG250196.
GeneTreeiENSGT00530000062920.
HOGENOMiHOG000231496.
HOVERGENiHBG024193.
InParanoidiQ8TCT8.
KOiK09596.
OMAiICCIMMV.
OrthoDBiEOG769ZJ4.
PhylomeDBiQ8TCT8.
TreeFamiTF319186.

Family and domain databases

InterProiIPR007369. Peptidase_A22B_SPP.
IPR006639. Preselin/SPP.
IPR003137. Protease-assoc_domain.
[Graphical view]
PANTHERiPTHR12174. PTHR12174. 1 hit.
PfamiPF02225. PA. 1 hit.
PF04258. Peptidase_A22B. 1 hit.
[Graphical view]
SMARTiSM00730. PSN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q8TCT8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGPQRRLSPA GAALLWGFLL QLTAAQEAIL HASGNGTTKD YCMLYNPYWT
60 70 80 90 100
ALPSTLENAT SISLMNLTST PLCNLSDIPP VGIKSKAVVV PWGSCHFLEK
110 120 130 140 150
ARIAQKGGAE AMLVVNNSVL FPPSGNRSEF PDVKILIAFI SYKDFRDMNQ
160 170 180 190 200
TLGDNITVKM YSPSWPNFDY TMVVIFVIAV FTVALGGYWS GLVELENLKA
210 220 230 240 250
VTTEDREMRK KKEEYLTFSP LTVVIFVVIC CVMMVLLYFF YKWLVYVMIA
260 270 280 290 300
IFCIASAMSL YNCLAALIHK IPYGQCTIAC RGKNMEVRLI FLSGLCIAVA
310 320 330 340 350
VVWAVFRNED RWAWILQDIL GIAFCLNLIK TLKLPNFKSC VILLGLLLLY
360 370 380 390 400
DVFFVFITPF ITKNGESIMV ELAAGPFGNN EKLPVVIRVP KLIYFSVMSV
410 420 430 440 450
CLMPVSILGF GDIIVPGLLI AYCRRFDVQT GSSYIYYVSS TVAYAIGMIL
460 470 480 490 500
TFVVLVLMKK GQPALLYLVP CTLITASVVA WRRKEMKKFW KGNSYQMMDH
510 520
LDCATNEENP VISGEQIVQQ
Length:520
Mass (Da):58,143
Last modified:November 8, 2002 - v2
Checksum:iA7A933A6504507DC
GO

Sequence cautioni

The sequence BAB55117.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence CAD13133.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti126 – 1261N → D in BAB55117 (PubMed:14702039).Curated
Sequence conflicti271 – 2711I → T in BAC11630 (PubMed:16303743).Curated
Sequence conflicti406 – 4061S → L in BAC11630 (PubMed:16303743).Curated
Sequence conflicti446 – 4461I → F in BAC11630 (PubMed:16303743).Curated
Sequence conflicti511 – 5111V → E in BAB55117 (PubMed:14702039).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti90 – 901V → I.
Corresponds to variant rs8034443 [ dbSNP | Ensembl ].
VAR_051790

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ345028 mRNA. Translation: CAC87789.1.
AY169314 mRNA. Translation: AAO12539.1.
AK027446 mRNA. Translation: BAB55117.1. Different initiation.
AK315651 mRNA. Translation: BAG38017.1.
AK075454 mRNA. Translation: BAC11630.1.
CH471082 Genomic DNA. Translation: EAW77410.1.
BC025740 mRNA. Translation: AAH25740.1.
AJ420896 mRNA. Translation: CAD13133.1. Different initiation.
CCDSiCCDS10138.1.
RefSeqiNP_116191.2. NM_032802.3.
UniGeneiHs.401537.

Genome annotation databases

EnsembliENST00000261854; ENSP00000261854; ENSG00000138600.
GeneIDi84888.
KEGGihsa:84888.
UCSCiuc001zyv.3. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ345028 mRNA. Translation: CAC87789.1.
AY169314 mRNA. Translation: AAO12539.1.
AK027446 mRNA. Translation: BAB55117.1. Different initiation.
AK315651 mRNA. Translation: BAG38017.1.
AK075454 mRNA. Translation: BAC11630.1.
CH471082 Genomic DNA. Translation: EAW77410.1.
BC025740 mRNA. Translation: AAH25740.1.
AJ420896 mRNA. Translation: CAD13133.1. Different initiation.
CCDSiCCDS10138.1.
RefSeqiNP_116191.2. NM_032802.3.
UniGeneiHs.401537.

3D structure databases

ProteinModelPortaliQ8TCT8.
SMRiQ8TCT8. Positions 68-163.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi124328. 3 interactions.
IntActiQ8TCT8. 4 interactions.
MINTiMINT-1465822.
STRINGi9606.ENSP00000261854.

Protein family/group databases

MEROPSiA22.007.
TCDBi1.A.54.3.2. the presenilin er ca(2+) leak channel (presenilin) family.

PTM databases

PhosphoSiteiQ8TCT8.

Polymorphism and mutation databases

BioMutaiSPPL2A.
DMDMi25008981.

Proteomic databases

MaxQBiQ8TCT8.
PaxDbiQ8TCT8.
PeptideAtlasiQ8TCT8.
PRIDEiQ8TCT8.

Protocols and materials databases

DNASUi84888.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000261854; ENSP00000261854; ENSG00000138600.
GeneIDi84888.
KEGGihsa:84888.
UCSCiuc001zyv.3. human.

Organism-specific databases

CTDi84888.
GeneCardsiGC15M050999.
HGNCiHGNC:30227. SPPL2A.
HPAiHPA036062.
MIMi608238. gene.
neXtProtiNX_Q8TCT8.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG250196.
GeneTreeiENSGT00530000062920.
HOGENOMiHOG000231496.
HOVERGENiHBG024193.
InParanoidiQ8TCT8.
KOiK09596.
OMAiICCIMMV.
OrthoDBiEOG769ZJ4.
PhylomeDBiQ8TCT8.
TreeFamiTF319186.

Miscellaneous databases

GeneWikiiSPPL2A.
GenomeRNAii84888.
NextBioi75209.
PROiQ8TCT8.
SOURCEiSearch...

Gene expression databases

BgeeiQ8TCT8.
ExpressionAtlasiQ8TCT8. baseline and differential.
GenevisibleiQ8TCT8. HS.

Family and domain databases

InterProiIPR007369. Peptidase_A22B_SPP.
IPR006639. Preselin/SPP.
IPR003137. Protease-assoc_domain.
[Graphical view]
PANTHERiPTHR12174. PTHR12174. 1 hit.
PfamiPF02225. PA. 1 hit.
PF04258. Peptidase_A22B. 1 hit.
[Graphical view]
SMARTiSM00730. PSN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Characterization of a new protein family with homology to presenilins."
    Irmler M., Tomiuk S., Korner M.R., Hofmann K., Conradt M.
    Submitted (SEP-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Novel class of polytopic proteins with domains associated with putative protease activity."
    Grigorenko A.P., Moliaka Y.K., Korovaitseva G.I., Rogaev E.I.
    Biochemistry (Mosc.) 67:826-834(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Blood.
  3. "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].
    Tissue: Synovium and Teratocarcinoma.
  4. "Signal sequence and keyword trap in silico for selection of full-length human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA libraries."
    Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J., Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S., Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y.
    , Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S., Isogai T.
    DNA Res. 12:117-126(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Placenta.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  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].
    Tissue: Pancreas.
  7. "Identification of signal peptide peptidase, a presenilin-type aspartic protease."
    Weihofen A., Binns K., Lemberg M.K., Ashman K., Martoglio B.
    Science 296:2215-2218(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 91-520.
    Tissue: Cervix carcinoma.
  8. "Consensus analysis of signal peptide peptidase and homologous human aspartic proteases reveals opposite topology of catalytic domains compared with presenilins."
    Friedmann E., Lemberg M.K., Weihofen A., Dev K.K., Dengler U., Rovelli G., Martoglio B.
    J. Biol. Chem. 279:50790-50798(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION, TOPOLOGY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  9. "SPPL2a and SPPL2b promote intramembrane proteolysis of TNFalpha in activated dendritic cells to trigger IL-12 production."
    Friedmann E., Hauben E., Maylandt K., Schleeger S., Vreugde S., Lichtenthaler S.F., Kuhn P.H., Stauffer D., Rovelli G., Martoglio B.
    Nat. Cell Biol. 8:843-848(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN CLEAVAGE OF TNF, SUBCELLULAR LOCATION, MUTAGENESIS OF ASP-412.
  10. "A gamma-secretase-like intramembrane cleavage of TNFalpha by the GxGD aspartyl protease SPPL2b."
    Fluhrer R., Grammer G., Israel L., Condron M.M., Haffner C., Friedmann E., Bohland C., Imhof A., Martoglio B., Teplow D.B., Haass C.
    Nat. Cell Biol. 8:894-896(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN CLEAVAGE OF TNF.
  11. Cited for: FUNCTION IN CLEAVAGE OF FASLG, MUTAGENESIS OF ASP-412.
  12. "Regulated intramembrane proteolysis of Bri2 (Itm2b) by ADAM10 and SPPL2a/SPPL2b."
    Martin L., Fluhrer R., Reiss K., Kremmer E., Saftig P., Haass C.
    J. Biol. Chem. 283:1644-1652(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN CLEAVAGE OF ITM2B, INTERACTION WITH ITM2B, MUTAGENESIS OF ASP-412.
  13. Cited for: GLYCOSYLATION AT ASN-155.
  14. Cited for: FUNCTION, MUTAGENESIS OF ASP-412.

Entry informationi

Entry nameiSPP2A_HUMAN
AccessioniPrimary (citable) accession number: Q8TCT8
Secondary accession number(s): B2RDS0, Q8TAW1, Q96SZ8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 8, 2002
Last sequence update: November 8, 2002
Last modified: July 22, 2015
This is version 115 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 15
    Human chromosome 15: 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.