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Q8TCT7

- SPP2B_HUMAN

UniProt

Q8TCT7 - SPP2B_HUMAN

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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

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 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
Complete GO annotation...

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
Complete GO annotation...

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. 10 interactions.
IntActiQ8TCT7. 2 interactions.

Structurei

3D structure databases

ProteinModelPortaliQ8TCT7.
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.
GeneTreeiENSGT00530000062920.
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

        10         20         30         40         50
MAAAVAAALA RLLAAFLLLA AQVACEYGMV HVVSQAGGPE GKDYCILYNP
60 70 80 90 100
QWAHLPHDLS KASFLQLRNW TASLLCSAAD LPARGFSNQI PLVARGNCTF
110 120 130 140 150
YEKVRLAQGS GARGLLIVSR ERLVPPGGNK TQYDEIGIPV ALLSYKDMLD
160 170 180 190 200
IFTRFGRTVR AALYAPKEPV LDYNMVIIFI MAVGTVAIGG YWAGSRDVKK
210 220 230 240 250
RYMKHKRDDG PEKQEDEAVD VTPVMTCVFV VMCCSMLVLL YYFYDLLVYV
260 270 280 290 300
VIGIFCLASA TGLYSCLAPC VRRLPFGKCR IPNNSLPYFH KRPQARMLLL
310 320 330 340 350
ALFCVAVSVV WGVFRNEDQW AWVLQDALGI AFCLYMLKTI RLPTFKACTL
360 370 380 390 400
LLLVLFLYDI FFVFITPFLT KSGSSIMVEV ATGPSDSATR EKLPMVLKVP
410 420 430 440 450
RLNSSPLALC DRPFSLLGFG DILVPGLLVA YCHRFDIQVQ SSRVYFVACT
460 470 480 490 500
IAYGVGLLVT FVALALMQRG QPALLYLVPC TLVTSCAVAL WRRELGVFWT
510 520 530 540 550
GSGFAKVLPP SPWAPAPADG PQPPKDSATP LSPQPPSEEP ATSPWPAEQS
560 570 580 590
PKSRTSEEMG AGAPMREPGS PAESEGRDQA QPSPVTQPGA SA
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.
CCDSiCCDS74252.1. [Q8TCT7-1]
CCDS74253.1. [Q8TCT7-4]
RefSeqiNP_001070706.1. NM_001077238.1. [Q8TCT7-4]
NP_694533.1. NM_152988.2. [Q8TCT7-1]
UniGeneiHs.744026.

Genome annotation databases

EnsembliENST00000610743; ENSP00000478510; ENSG00000005206. [Q8TCT7-4]
ENST00000613503; ENSP00000478298; ENSG00000005206. [Q8TCT7-1]
ENST00000618220; ENSP00000480813; ENSG00000005206. [Q8TCT7-2]
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.
CCDSi CCDS74252.1. [Q8TCT7-1 ]
CCDS74253.1. [Q8TCT7-4 ]
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.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 121255. 10 interactions.
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

Ensembli ENST00000610743 ; ENSP00000478510 ; ENSG00000005206 . [Q8TCT7-4 ]
ENST00000613503 ; ENSP00000478298 ; ENSG00000005206 . [Q8TCT7-1 ]
ENST00000618220 ; ENSP00000480813 ; ENSG00000005206 . [Q8TCT7-2 ]
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.
GeneTreei ENSGT00530000062920.
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

« 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] (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 29, 2014
This is version 119 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