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Q8TCT7

- SPP2B_HUMAN

UniProt

Q8TCT7 - SPP2B_HUMAN

Protein

Signal peptide peptidase-like 2B

Gene

SPPL2B

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 118 (01 Oct 2014)
      Sequence version 2 (16 May 2006)
      Previous versions | rss
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    Functioni

    Intramembrane-cleaving aspartic protease (I-CLiP) that cleaves type II membrane signal peptides in the hydrophobic plane of the membrane. Functions in 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. May play a role in the regulation of innate and adaptive immunity.5 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei359 – 3591By similarity
    Active sitei421 – 4211By similarity

    GO - Molecular functioni

    1. aspartic endopeptidase activity, intramembrane cleaving Source: UniProtKB
    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

    MEROPSiA22.004.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Signal peptide peptidase-like 2B (EC:3.4.23.-)
    Short name:
    SPP-like 2B
    Short name:
    SPPL2b
    Alternative name(s):
    Intramembrane protease 4
    Short name:
    IMP-4
    Presenilin homologous protein 4
    Short name:
    PSH4
    Presenilin-like protein 1
    Gene namesi
    Name:SPPL2B
    Synonyms:IMP4, KIAA1532, PSL1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Unplaced

    Organism-specific databases

    HGNCiHGNC:30627. SPPL2B.

    Subcellular locationi

    Golgi apparatus membrane 2 Publications; Multi-pass membrane protein 2 Publications
    Note: targeted through the entire secretory pathway to endosomes/lysosomes.

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Golgi apparatus, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi421 – 4211D → A: Loss of intramembrane-cleaving activity toward ITM2B and TNF. 4 Publications

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2525Sequence AnalysisAdd
    BLAST
    Chaini26 – 592567Signal peptide peptidase-like 2BPRO_0000073909Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi97 – 971N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi129 – 1291N-linked (GlcNAc...)Sequence Analysis

    Post-translational modificationi

    Glycosylated.2 Publications

    Keywords - PTMi

    Glycoprotein

    Proteomic databases

    MaxQBiQ8TCT7.
    PaxDbiQ8TCT7.
    PRIDEiQ8TCT7.

    PTM databases

    PhosphoSiteiQ8TCT7.

    Expressioni

    Tissue specificityi

    Expressed predominantly in adrenal cortex and mammary gland.1 Publication

    Gene expression databases

    GenevestigatoriQ8TCT7.

    Interactioni

    Subunit structurei

    Monomer. Homodimer. Interacts with ITM2B and TNF.2 Publications

    Protein-protein interaction databases

    BioGridi121255. 1 interaction.
    IntActiQ8TCT7. 2 interactions.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8TCT7.
    SMRiQ8TCT7. Positions 82-159.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini26 – 174149LumenalSequence AnalysisAdd
    BLAST
    Topological domaini196 – 22126CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini245 – 2484LumenalSequence Analysis
    Topological domaini272 – 29322CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini315 – 3195LumenalSequence Analysis
    Topological domaini341 – 3488CytoplasmicSequence Analysis
    Topological domaini370 – 41243LumenalSequence AnalysisAdd
    BLAST
    Topological domaini434 – 44512CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini467 – 4704LumenalSequence Analysis
    Topological domaini492 – 592101CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei175 – 19521HelicalSequence AnalysisAdd
    BLAST
    Transmembranei222 – 24423HelicalSequence AnalysisAdd
    BLAST
    Transmembranei249 – 27123HelicalSequence AnalysisAdd
    BLAST
    Transmembranei294 – 31421HelicalSequence AnalysisAdd
    BLAST
    Transmembranei320 – 34021HelicalSequence AnalysisAdd
    BLAST
    Transmembranei349 – 36921HelicalSequence AnalysisAdd
    BLAST
    Transmembranei413 – 43321HelicalSequence AnalysisAdd
    BLAST
    Transmembranei446 – 46621HelicalSequence AnalysisAdd
    BLAST
    Transmembranei471 – 49121HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini71 – 14979PAAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi472 – 4743PAL

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi350 – 3578Poly-Leu
    Compositional biasi509 – 55143Pro-richAdd
    BLAST

    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.
    HOVERGENiHBG024193.
    InParanoidiQ8TCT7.
    KOiK09597.
    PhylomeDBiQ8TCT7.

    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]

    Sequences (4)i

    Sequence statusi: Complete.

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

    This entry describes 4 isoformsi produced by alternative splicing. Align

    Note: Experimental confirmation may be lacking for some isoforms.

    Isoform 1 (identifier: Q8TCT7-1) [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

    MAAAVAAALA RLLAAFLLLA AQVACEYGMV HVVSQAGGPE GKDYCILYNP    50
    QWAHLPHDLS KASFLQLRNW TASLLCSAAD LPARGFSNQI PLVARGNCTF 100
    YEKVRLAQGS GARGLLIVSR ERLVPPGGNK TQYDEIGIPV ALLSYKDMLD 150
    IFTRFGRTVR AALYAPKEPV LDYNMVIIFI MAVGTVAIGG YWAGSRDVKK 200
    RYMKHKRDDG PEKQEDEAVD VTPVMTCVFV VMCCSMLVLL YYFYDLLVYV 250
    VIGIFCLASA TGLYSCLAPC VRRLPFGKCR IPNNSLPYFH KRPQARMLLL 300
    ALFCVAVSVV WGVFRNEDQW AWVLQDALGI AFCLYMLKTI RLPTFKACTL 350
    LLLVLFLYDI FFVFITPFLT KSGSSIMVEV ATGPSDSATR EKLPMVLKVP 400
    RLNSSPLALC DRPFSLLGFG DILVPGLLVA YCHRFDIQVQ SSRVYFVACT 450
    IAYGVGLLVT FVALALMQRG QPALLYLVPC TLVTSCAVAL WRRELGVFWT 500
    GSGFAKVLPP SPWAPAPADG PQPPKDSATP LSPQPPSEEP ATSPWPAEQS 550
    PKSRTSEEMG AGAPMREPGS PAESEGRDQA QPSPVTQPGA SA 592
    Length:592
    Mass (Da):64,644
    Last modified:May 16, 2006 - v2
    Checksum:i0F49370F16D36AA0
    GO
    Isoform 2 (identifier: Q8TCT7-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         320-592: Missing.

    Show »
    Length:319
    Mass (Da):35,295
    Checksum:i5EFEEB110C4C7D7B
    GO
    Isoform 3 (identifier: Q8TCT7-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         280-291: Missing.
         320-592: Missing.

    Show »
    Length:307
    Mass (Da):33,827
    Checksum:i4AFCE5838F23543F
    GO
    Isoform 4 (identifier: Q8TCT7-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         506-511: KVLPPS → VNTSLL
         512-592: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:511
    Mass (Da):56,431
    Checksum:i6B496A9879E9D57F
    GO

    Sequence cautioni

    The sequence AAG45441.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.
    The sequence BAA96056.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.
    The sequence AAC05601.1 differs from that shown. Reason: Erroneous gene model prediction.

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti574 – 5741S → P.
    Corresponds to variant rs10402284 [ dbSNP | Ensembl ].
    VAR_059780

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei280 – 29112Missing in isoform 3. 1 PublicationVSP_005203Add
    BLAST
    Alternative sequencei320 – 592273Missing in isoform 2 and isoform 3. 2 PublicationsVSP_005204Add
    BLAST
    Alternative sequencei506 – 5116KVLPPS → VNTSLL in isoform 4. 1 PublicationVSP_009221
    Alternative sequencei512 – 59281Missing in isoform 4. 1 PublicationVSP_009222Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ345027 mRNA. Translation: CAC87788.1.
    AJ420897 mRNA. Translation: CAD13134.1.
    AY169315 mRNA. Translation: AAO12540.1.
    AB040965 mRNA. Translation: BAA96056.1. Different initiation.
    AC004410 Genomic DNA. Translation: AAC05601.1. Sequence problems.
    AC005258 Genomic DNA. Translation: AAG45441.1. Different initiation.
    CH471139 Genomic DNA. Translation: EAW69383.1.
    CH471139 Genomic DNA. Translation: EAW69388.1.
    BC001788 mRNA. Translation: AAH01788.2.
    BC028391 mRNA. Translation: AAH28391.2.
    BC093046 mRNA. Translation: AAH93046.1.
    AL365405 mRNA. Translation: CAB96951.1. Sequence problems.
    RefSeqiNP_001070706.1. NM_001077238.1. [Q8TCT7-4]
    NP_694533.1. NM_152988.2. [Q8TCT7-1]
    UniGeneiHs.744026.

    Genome annotation databases

    GeneIDi56928.
    KEGGihsa:56928.
    UCSCiuc002lvr.3. human. [Q8TCT7-4]
    uc002lvs.3. human. [Q8TCT7-1]

    Polymorphism databases

    DMDMi97537015.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ345027 mRNA. Translation: CAC87788.1 .
    AJ420897 mRNA. Translation: CAD13134.1 .
    AY169315 mRNA. Translation: AAO12540.1 .
    AB040965 mRNA. Translation: BAA96056.1 . Different initiation.
    AC004410 Genomic DNA. Translation: AAC05601.1 . Sequence problems.
    AC005258 Genomic DNA. Translation: AAG45441.1 . Different initiation.
    CH471139 Genomic DNA. Translation: EAW69383.1 .
    CH471139 Genomic DNA. Translation: EAW69388.1 .
    BC001788 mRNA. Translation: AAH01788.2 .
    BC028391 mRNA. Translation: AAH28391.2 .
    BC093046 mRNA. Translation: AAH93046.1 .
    AL365405 mRNA. Translation: CAB96951.1 . Sequence problems.
    RefSeqi NP_001070706.1. NM_001077238.1. [Q8TCT7-4 ]
    NP_694533.1. NM_152988.2. [Q8TCT7-1 ]
    UniGenei Hs.744026.

    3D structure databases

    ProteinModelPortali Q8TCT7.
    SMRi Q8TCT7. Positions 82-159.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 121255. 1 interaction.
    IntActi Q8TCT7. 2 interactions.

    Protein family/group databases

    MEROPSi A22.004.

    PTM databases

    PhosphoSitei Q8TCT7.

    Polymorphism databases

    DMDMi 97537015.

    Proteomic databases

    MaxQBi Q8TCT7.
    PaxDbi Q8TCT7.
    PRIDEi Q8TCT7.

    Protocols and materials databases

    DNASUi 56928.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 56928.
    KEGGi hsa:56928.
    UCSCi uc002lvr.3. human. [Q8TCT7-4 ]
    uc002lvs.3. human. [Q8TCT7-1 ]

    Organism-specific databases

    CTDi 56928.
    GeneCardsi GC19P002328.
    H-InvDB HIX0158528.
    HGNCi HGNC:30627. SPPL2B.
    MIMi 608239. gene.
    neXtProti NX_Q8TCT7.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG250196.
    HOVERGENi HBG024193.
    InParanoidi Q8TCT7.
    KOi K09597.
    PhylomeDBi Q8TCT7.

    Miscellaneous databases

    ChiTaRSi SPPL2B. human.
    GeneWikii SPPL2B.
    GenomeRNAii 56928.
    NextBioi 62462.
    PROi Q8TCT7.
    SOURCEi Search...

    Gene expression databases

    Genevestigatori Q8TCT7.

    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] (ISOFORM 1).
    2. Martoglio B.
      Submitted (NOV-2001) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    3. "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] (ISOFORM 1).
      Tissue: Blood.
    4. "Prediction of the coding sequences of unidentified human genes. XVII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
      Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.
      DNA Res. 7:143-150(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Brain.
    5. "The DNA sequence and biology of human chromosome 19."
      Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V.
      , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
      Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "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; 2 AND 4).
      Tissue: Brain, Eye and Testis.
    8. The European IMAGE consortium
      Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 201-318 (ISOFORM 3).
    9. "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.
    10. "Differential localization and identification of a critical aspartate suggest non-redundant proteolytic functions of the presenilin homologues SPPL2b and SPPL3."
      Krawitz P., Haffner C., Fluhrer R., Steiner H., Schmid B., Haass C.
      J. Biol. Chem. 280:39515-39523(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION, SUBCELLULAR LOCATION.
    11. "Intramembrane proteolytic cleavage by human signal peptide peptidase like 3 and malaria signal peptide peptidase."
      Nyborg A.C., Ladd T.B., Jansen K., Kukar T., Golde T.E.
      FASEB J. 20:1671-1679(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: HOMODIMERIZATION.
    12. "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.
    13. "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, INTERACTION WITH TNF, MUTAGENESIS OF ASP-421.
    14. "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, SUBCELLULAR LOCATION, INTERACTION WITH ITM2B, MUTAGENESIS OF ASP-421.
    15. "Substrate requirements for SPPL2b-dependent regulated intramembrane proteolysis."
      Martin L., Fluhrer R., Haass C.
      J. Biol. Chem. 284:5662-5670(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN CLEAVAGE OF ITM2B, MUTAGENESIS OF ASP-421.
    16. "The alpha-helical content of the transmembrane domain of the British dementia protein-2 (Bri2) determines its processing by signal peptide peptidase-like 2b (SPPL2b)."
      Fluhrer R., Martin L., Klier B., Haug-Kroper M., Grammer G., Nuscher B., Haass C.
      J. Biol. Chem. 287:5156-5163(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN CLEAVAGE OF ITM2B, MUTAGENESIS OF ASP-421.

    Entry informationi

    Entry nameiSPP2B_HUMAN
    AccessioniPrimary (citable) accession number: Q8TCT7
    Secondary accession number(s): D6W609
    , O60365, Q567S3, Q8IUH9, Q9BUY6, Q9H3M4, Q9NPN2, Q9P1Z6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 8, 2002
    Last sequence update: May 16, 2006
    Last modified: October 1, 2014
    This is version 118 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 19
      Human chromosome 19: 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