Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(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)

Q8TCT8

- SPP2A_HUMAN

UniProt

Q8TCT8 - SPP2A_HUMAN

Protein

Signal peptide peptidase-like 2A

Gene

SPPL2A

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 109 (01 Oct 2014)
      Sequence version 2 (08 Nov 2002)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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. 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. Also responsible for the intramembrane cleavage of Fas antigen ligand FASLG, which promotes the release of the intracellular FasL domain (FasL ICD). May play a role in the regulation of innate and adaptive immunity.4 Publications

    Sites

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

    GO - Molecular functioni

    1. aspartic-type endopeptidase activity Source: InterPro
    2. protein binding Source: UniProtKB
    3. protein homodimerization activity Source: UniProtKB

    GO - Biological processi

    1. membrane protein ectodomain proteolysis Source: UniProtKB
    2. membrane protein intracellular domain proteolysis Source: UniProtKB
    3. regulation of immune response Source: UniProtKB

    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 2A (EC:3.4.23.-)
    Short name:
    SPP-like 2A
    Short name:
    SPPL2a
    Alternative name(s):
    Intramembrane protease 3
    Short name:
    IMP-3
    Presenilin-like protein 2
    Gene namesi
    Name:SPPL2A
    Synonyms:IMP3, PSL2
    ORF Names:PSEC0147
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 15

    Organism-specific databases

    HGNCiHGNC:30227. SPPL2A.

    Subcellular locationi

    Late endosome membrane By similarity; Multi-pass membrane protein By similarity. Lysosome membrane By similarity; Multi-pass membrane protein By similarity. Cell membrane 1 Publication
    Note: Colocalizes with palmitoylated and myristoylated proteins at the plasma membrane.

    GO - Cellular componenti

    1. Golgi-associated vesicle membrane Source: UniProtKB
    2. integral component of cytoplasmic side of endoplasmic reticulum membrane Source: UniProtKB
    3. integral component of lumenal side of endoplasmic reticulum membrane Source: UniProtKB
    4. late endosome membrane Source: UniProtKB-SubCell
    5. lysosomal membrane Source: UniProtKB
    6. plasma membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell membrane, Endosome, Lysosome, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi412 – 4121D → A: Loss of intramembrane-cleaving activity toward FASLG, ITM2B and TNF. 3 Publications

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2525Sequence AnalysisAdd
    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)2 Publications

    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

    ArrayExpressiQ8TCT8.
    BgeeiQ8TCT8.
    GenevestigatoriQ8TCT8.

    Organism-specific databases

    HPAiHPA036062.

    Interactioni

    Subunit structurei

    Interacts with ITM2B.1 Publication

    Protein-protein interaction databases

    BioGridi124328. 2 interactions.
    IntActiQ8TCT8. 4 interactions.
    MINTiMINT-1465822.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8TCT8.
    SMRiQ8TCT8. Positions 80-161.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini26 – 172147LumenalSequence AnalysisAdd
    BLAST
    Topological domaini194 – 22027CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini242 – 2476LumenalSequence Analysis
    Topological domaini269 – 28517CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini307 – 3115LumenalSequence Analysis
    Topological domaini333 – 3408CytoplasmicSequence Analysis
    Topological domaini362 – 39938LumenalSequence AnalysisAdd
    BLAST
    Topological domaini421 – 43717CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini459 – 4602LumenalSequence Analysis
    Topological domaini482 – 52039CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei173 – 19321HelicalSequence AnalysisAdd
    BLAST
    Transmembranei221 – 24121HelicalSequence AnalysisAdd
    BLAST
    Transmembranei248 – 26821HelicalSequence AnalysisAdd
    BLAST
    Transmembranei286 – 30621HelicalSequence AnalysisAdd
    BLAST
    Transmembranei312 – 33221HelicalSequence AnalysisAdd
    BLAST
    Transmembranei341 – 36121HelicalSequence AnalysisAdd
    BLAST
    Transmembranei400 – 42021HelicalSequence AnalysisAdd
    BLAST
    Transmembranei438 – 45821HelicalSequence AnalysisAdd
    BLAST
    Transmembranei461 – 48121HelicalSequence AnalysisAdd
    BLAST

    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 By similarity. 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.By similarity

    Sequence similaritiesi

    Belongs to the peptidase A22B family.Curated

    Keywords - Domaini

    Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG250196.
    HOGENOMiHOG000231496.
    HOVERGENiHBG024193.
    InParanoidiQ8TCT8.
    KOiK09596.
    OMAiSCTIAYA.
    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

    MGPQRRLSPA GAALLWGFLL QLTAAQEAIL HASGNGTTKD YCMLYNPYWT    50
    ALPSTLENAT SISLMNLTST PLCNLSDIPP VGIKSKAVVV PWGSCHFLEK 100
    ARIAQKGGAE AMLVVNNSVL FPPSGNRSEF PDVKILIAFI SYKDFRDMNQ 150
    TLGDNITVKM YSPSWPNFDY TMVVIFVIAV FTVALGGYWS GLVELENLKA 200
    VTTEDREMRK KKEEYLTFSP LTVVIFVVIC CVMMVLLYFF YKWLVYVMIA 250
    IFCIASAMSL YNCLAALIHK IPYGQCTIAC RGKNMEVRLI FLSGLCIAVA 300
    VVWAVFRNED RWAWILQDIL GIAFCLNLIK TLKLPNFKSC VILLGLLLLY 350
    DVFFVFITPF ITKNGESIMV ELAAGPFGNN EKLPVVIRVP KLIYFSVMSV 400
    CLMPVSILGF GDIIVPGLLI AYCRRFDVQT GSSYIYYVSS TVAYAIGMIL 450
    TFVVLVLMKK GQPALLYLVP CTLITASVVA WRRKEMKKFW KGNSYQMMDH 500
    LDCATNEENP VISGEQIVQQ 520
    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.
    The sequence CAD13133.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    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:
    EMBL
    GenBank
    DDBJ
    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.

    Polymorphism databases

    DMDMi25008981.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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.
    CCDSi CCDS10138.1.
    RefSeqi NP_116191.2. NM_032802.3.
    UniGenei Hs.401537.

    3D structure databases

    ProteinModelPortali Q8TCT8.
    SMRi Q8TCT8. Positions 80-161.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 124328. 2 interactions.
    IntActi Q8TCT8. 4 interactions.
    MINTi MINT-1465822.

    Protein family/group databases

    MEROPSi A22.007.
    TCDBi 1.A.54.3.2. the presenilin er ca(2+) leak channel (presenilin) family.

    PTM databases

    PhosphoSitei Q8TCT8.

    Polymorphism databases

    DMDMi 25008981.

    Proteomic databases

    MaxQBi Q8TCT8.
    PaxDbi Q8TCT8.
    PeptideAtlasi Q8TCT8.
    PRIDEi Q8TCT8.

    Protocols and materials databases

    DNASUi 84888.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000261854 ; ENSP00000261854 ; ENSG00000138600 .
    GeneIDi 84888.
    KEGGi hsa:84888.
    UCSCi uc001zyv.3. human.

    Organism-specific databases

    CTDi 84888.
    GeneCardsi GC15M050999.
    HGNCi HGNC:30227. SPPL2A.
    HPAi HPA036062.
    MIMi 608238. gene.
    neXtProti NX_Q8TCT8.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG250196.
    HOGENOMi HOG000231496.
    HOVERGENi HBG024193.
    InParanoidi Q8TCT8.
    KOi K09596.
    OMAi SCTIAYA.
    OrthoDBi EOG769ZJ4.
    PhylomeDBi Q8TCT8.
    TreeFami TF319186.

    Miscellaneous databases

    GeneWikii SPPL2A.
    GenomeRNAii 84888.
    NextBioi 75209.
    PROi Q8TCT8.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q8TCT8.
    Bgeei Q8TCT8.
    Genevestigatori Q8TCT8.

    Family and domain databases

    InterProi IPR007369. Peptidase_A22B_SPP.
    IPR006639. Preselin/SPP.
    IPR003137. Protease-assoc_domain.
    [Graphical view ]
    PANTHERi PTHR12174. PTHR12174. 1 hit.
    Pfami PF02225. PA. 1 hit.
    PF04258. Peptidase_A22B. 1 hit.
    [Graphical view ]
    SMARTi SM00730. PSN. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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, 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.

    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: October 1, 2014
    This is version 109 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