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Q8TCT9

- HM13_HUMAN

UniProt

Q8TCT9 - HM13_HUMAN

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Protein

Minor histocompatibility antigen H13

Gene
HM13, H13, IMP1, PSL3, SPP, MSTP086
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Catalyzes intramembrane proteolysis of some signal peptides after they have been cleaved from a preprotein, resulting in the release of the fragment from the ER membrane into the cytoplasm. Required to generate lymphocyte cell surface (HLA-E) epitopes derived from MHC class I signal peptides. May play a role in graft rejection By similarity. May be necessary for the removal of the signal peptide that remains attached to the hepatitis C virus core protein after the initial proteolytic processing of the polyprotein. Involved in the intramembrane cleavage of the integral membrane protein PSEN1.4 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei219 – 2191 By similarity
Active sitei265 – 2651 By similarity

GO - Molecular functioni

  1. aspartic endopeptidase activity, intramembrane cleaving Source: UniProtKB
  2. peptidase activity Source: UniProtKB
  3. protein binding Source: UniProtKB
  4. protein homodimerization activity Source: UniProtKB

GO - Biological processi

  1. membrane protein proteolysis Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease

Protein family/group databases

MEROPSiA22.003.

Names & Taxonomyi

Protein namesi
Recommended name:
Minor histocompatibility antigen H13 (EC:3.4.23.-)
Alternative name(s):
Intramembrane protease 1
Short name:
IMP-1
Short name:
IMPAS-1
Short name:
hIMP1
Presenilin-like protein 3
Signal peptide peptidase
Gene namesi
Name:HM13
Synonyms:H13, IMP1, PSL3, SPP
ORF Names:MSTP086
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 20

Organism-specific databases

HGNCiHGNC:16435. HM13.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 3131Lumenal Reviewed predictionAdd
BLAST
Transmembranei32 – 5221Helical; Reviewed predictionAdd
BLAST
Topological domaini53 – 7725Cytoplasmic Reviewed predictionAdd
BLAST
Transmembranei78 – 9821Helical; Reviewed predictionAdd
BLAST
Topological domaini99 – 1002Lumenal Reviewed prediction
Transmembranei101 – 12121Helical; Reviewed predictionAdd
BLAST
Topological domaini122 – 15736Cytoplasmic Reviewed predictionAdd
BLAST
Transmembranei158 – 17821Helical; Reviewed predictionAdd
BLAST
Topological domaini179 – 1813Lumenal Reviewed prediction
Transmembranei182 – 20221Helical; Reviewed predictionAdd
BLAST
Topological domaini203 – 2097Cytoplasmic Reviewed prediction
Transmembranei210 – 23021Helical; Reviewed predictionAdd
BLAST
Topological domaini231 – 25626Lumenal Reviewed predictionAdd
BLAST
Transmembranei257 – 27721Helical; Reviewed predictionAdd
BLAST
Topological domaini278 – 29013Cytoplasmic Reviewed predictionAdd
BLAST
Transmembranei291 – 31121Helical; Reviewed predictionAdd
BLAST
Topological domaini312 – 3143Lumenal Reviewed prediction
Transmembranei315 – 33521Helical; Reviewed predictionAdd
BLAST
Topological domaini336 – 37742Cytoplasmic Reviewed predictionAdd
BLAST

GO - Cellular componenti

  1. cell surface Source: UniProtKB
  2. endoplasmic reticulum 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. plasma membrane Source: UniProtKB-SubCell
  6. rough endoplasmic reticulum Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Endoplasmic reticulum, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi10 – 101N → Q: Abolishes N-glycosylation; when associated with Q-20. 1 Publication
Mutagenesisi20 – 201N → Q: Abolishes N-glycosylation; when associated with Q-10. 1 Publication
Mutagenesisi219 – 2191D → A: Abolishes proteolysis of PSEN1. 1 Publication
Mutagenesisi264 – 2641G → A: No effect on proteolysis of PSEN1. 1 Publication
Mutagenesisi265 – 2651D → A: No effect on inhibitor binding; abolishes catalytic activity. Abolishes proteolysis of PSEN1. 2 Publications
Mutagenesisi317 – 3171P → L: Abolishes proteolysis of PSEN1. 1 Publication

Organism-specific databases

PharmGKBiPA29314.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 377377Minor histocompatibility antigen H13PRO_0000073907Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi10 – 101N-linked (GlcNAc...)1 Publication
Glycosylationi20 – 201N-linked (GlcNAc...)1 Publication

Post-translational modificationi

N-glycosylated.1 Publication

Keywords - PTMi

Glycoprotein

Proteomic databases

MaxQBiQ8TCT9.
PaxDbiQ8TCT9.
PRIDEiQ8TCT9.

PTM databases

PhosphoSiteiQ8TCT9.

Expressioni

Tissue specificityi

Widely expressed with highest levels in kidney, liver, placenta, lung, leukocytes and small intestine and reduced expression in heart and skeletal muscle. Expressed abundantly in the CNS with highest levels in thalamus and medulla.2 Publications

Gene expression databases

BgeeiQ8TCT9.
GenevestigatoriQ8TCT9.

Organism-specific databases

HPAiHPA045089.

Interactioni

Subunit structurei

Interacts with RNF139.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
P4HBP072373EBI-347472,EBI-395883

Protein-protein interaction databases

BioGridi123505. 9 interactions.
IntActiQ8TCT9. 8 interactions.
MINTiMINT-3034232.

Structurei

3D structure databases

ProteinModelPortaliQ8TCT9.

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi317 – 3193PAL

Domaini

The first transmembrane domain may act as a type I signal anchor By similarity. The PAL motif is required for normal active site conformation By similarity.

Sequence similaritiesi

Belongs to the peptidase A22B family.

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG313636.
HOVERGENiHBG024161.
KOiK09595.
OMAiSSEMPET.
OrthoDBiEOG7Z3F4N.
PhylomeDBiQ8TCT9.
TreeFamiTF105854.

Family and domain databases

InterProiIPR007369. Peptidase_A22B_SPP.
IPR006639. Preselin/SPP.
[Graphical view]
PANTHERiPTHR12174. PTHR12174. 1 hit.
PfamiPF04258. Peptidase_A22B. 1 hit.
[Graphical view]
SMARTiSM00730. PSN. 1 hit.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q8TCT9-1) [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

MDSALSDPHN GSAEAGGPTN STTRPPSTPE GIALAYGSLL LMALLPIFFG    50
ALRSVRCARG KNASDMPETI TSRDAARFPI IASCTLLGLY LFFKIFSQEY 100
INLLLSMYFF VLGILALSHT ISPFMNKFFP ASFPNRQYQL LFTQGSGENK 150
EEIINYEFDT KDLVCLGLSS IVGVWYLLRK HWIANNLFGL AFSLNGVELL 200
HLNNVSTGCI LLGGLFIYDV FWVFGTNVMV TVAKSFEAPI KLVFPQDLLE 250
KGLEANNFAM LGLGDVVIPG IFIALLLRFD ISLKKNTHTY FYTSFAAYIF 300
GLGLTIFIMH IFKHAQPALL YLVPACIGFP VLVALAKGEV TEMFSYEESN 350
PKDPAAVTES KEGTEASASK GLEKKEK 377
Length:377
Mass (Da):41,488
Last modified:June 1, 2002 - v1
Checksum:i322D231B52B33118
GO
Isoform 2 (identifier: Q8TCT9-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     347-347: E → ESSAEILPHTPRLTHFPTVSGSPASLADSMQQKLAGPRRRRPQNPSAIYE

Show »
Length:426
Mass (Da):46,825
Checksum:i269AD5CC99982845
GO
Isoform 4 (identifier: Q8TCT9-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     348-377: ESNPKDPAAVTESKEGTEASASKGLEKKEK → SSAEILPHTP...RRRPQNPSAM

Show »
Length:394
Mass (Da):43,423
Checksum:i9BEC3A1C9B605D48
GO
Isoform 5 (identifier: Q8TCT9-5) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     181-222: Missing.

Note: No experimental confirmation available. Gene prediction based on EST data.

Show »
Length:335
Mass (Da):36,814
Checksum:iD22777AF67B3720B
GO

Sequence cautioni

The sequence BAC11138.1 differs from that shown. Reason: Intron retention.
The sequence AAQ13609.1 differs from that shown. Reason: Frameshift at positions 320, 329, 330 and 358.
The sequence CAI19152.1 differs from that shown. Reason: Erroneous gene model prediction.
The sequence CAI20173.1 differs from that shown. Reason: Erroneous gene model prediction.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti259 – 2591A → P.
Corresponds to variant rs1044419 [ dbSNP | Ensembl ].
VAR_014274

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei181 – 22242Missing in isoform 5. VSP_015082Add
BLAST
Alternative sequencei347 – 3471E → ESSAEILPHTPRLTHFPTVS GSPASLADSMQQKLAGPRRR RPQNPSAIYE in isoform 2. VSP_005196
Alternative sequencei348 – 37730ESNPK…EKKEK → SSAEILPHTPRLTHFPTVSG SPASLADSMQQKLAGPRRRR PQNPSAM in isoform 4. VSP_015083Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti132 – 1321S → N AA sequence 1 Publication
Sequence conflicti150 – 1501K → R in BAC11519. 1 Publication
Sequence conflicti159 – 1591D → A AA sequence 1 Publication
Sequence conflicti235 – 2351S → F in AAH08938. 1 Publication
Sequence conflicti235 – 2351S → F in AAH08959. 1 Publication
Sequence conflicti295 – 2951F → Y in AAQ13609. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AJ420895 mRNA. Translation: CAD13132.1.
AF515663 mRNA. Translation: AAN77099.1.
AY169310 mRNA. Translation: AAO12535.1.
AY169311 mRNA. Translation: AAO12536.1.
AY169312 mRNA. Translation: AAO12537.1.
DQ168450 mRNA. Translation: ABA56163.1.
AJ345029 mRNA. Translation: CAC87790.1.
AF483215 mRNA. Translation: AAM22076.1.
AF172086 mRNA. Translation: AAQ13609.1. Frameshift.
AK074686 mRNA. Translation: BAC11138.1. Sequence problems.
AK075283 mRNA. Translation: BAC11519.1.
AK314410 mRNA. Translation: BAG37032.1.
AL110115, AL121751 Genomic DNA. Translation: CAI20173.1. Sequence problems.
AL110115, AL121751 Genomic DNA. Translation: CAI20174.1.
AL110115, AL121751 Genomic DNA. Translation: CAI20175.2.
AL121751, AL110115 Genomic DNA. Translation: CAI19152.1. Sequence problems.
AL121751, AL110115 Genomic DNA. Translation: CAI19153.1.
AL121751, AL110115 Genomic DNA. Translation: CAI19154.2.
CH471077 Genomic DNA. Translation: EAW76436.1.
CH471077 Genomic DNA. Translation: EAW76437.1.
CH471077 Genomic DNA. Translation: EAW76435.1.
CH471077 Genomic DNA. Translation: EAW76438.1.
BC008938 mRNA. Translation: AAH08938.1.
BC008959 mRNA. Translation: AAH08959.1.
BC062595 mRNA. Translation: AAH62595.1.
CCDSiCCDS13182.1. [Q8TCT9-1]
CCDS13183.1. [Q8TCT9-4]
CCDS42861.1. [Q8TCT9-2]
RefSeqiNP_110416.1. NM_030789.3. [Q8TCT9-1]
NP_848695.1. NM_178580.2. [Q8TCT9-4]
NP_848696.1. NM_178581.2. [Q8TCT9-2]
NP_848697.1. NM_178582.2.
UniGeneiHs.373741.

Genome annotation databases

EnsembliENST00000335574; ENSP00000335294; ENSG00000101294. [Q8TCT9-4]
ENST00000340852; ENSP00000343032; ENSG00000101294. [Q8TCT9-1]
ENST00000376127; ENSP00000365296; ENSG00000101294. [Q8TCT9-5]
ENST00000398174; ENSP00000381237; ENSG00000101294. [Q8TCT9-2]
GeneIDi81502.
KEGGihsa:81502.
UCSCiuc002wwc.3. human. [Q8TCT9-2]
uc002wwd.3. human. [Q8TCT9-4]
uc002wwe.3. human. [Q8TCT9-1]

Polymorphism databases

DMDMi25008563.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AJ420895 mRNA. Translation: CAD13132.1 .
AF515663 mRNA. Translation: AAN77099.1 .
AY169310 mRNA. Translation: AAO12535.1 .
AY169311 mRNA. Translation: AAO12536.1 .
AY169312 mRNA. Translation: AAO12537.1 .
DQ168450 mRNA. Translation: ABA56163.1 .
AJ345029 mRNA. Translation: CAC87790.1 .
AF483215 mRNA. Translation: AAM22076.1 .
AF172086 mRNA. Translation: AAQ13609.1 . Frameshift.
AK074686 mRNA. Translation: BAC11138.1 . Sequence problems.
AK075283 mRNA. Translation: BAC11519.1 .
AK314410 mRNA. Translation: BAG37032.1 .
AL110115 , AL121751 Genomic DNA. Translation: CAI20173.1 . Sequence problems.
AL110115 , AL121751 Genomic DNA. Translation: CAI20174.1 .
AL110115 , AL121751 Genomic DNA. Translation: CAI20175.2 .
AL121751 , AL110115 Genomic DNA. Translation: CAI19152.1 . Sequence problems.
AL121751 , AL110115 Genomic DNA. Translation: CAI19153.1 .
AL121751 , AL110115 Genomic DNA. Translation: CAI19154.2 .
CH471077 Genomic DNA. Translation: EAW76436.1 .
CH471077 Genomic DNA. Translation: EAW76437.1 .
CH471077 Genomic DNA. Translation: EAW76435.1 .
CH471077 Genomic DNA. Translation: EAW76438.1 .
BC008938 mRNA. Translation: AAH08938.1 .
BC008959 mRNA. Translation: AAH08959.1 .
BC062595 mRNA. Translation: AAH62595.1 .
CCDSi CCDS13182.1. [Q8TCT9-1 ]
CCDS13183.1. [Q8TCT9-4 ]
CCDS42861.1. [Q8TCT9-2 ]
RefSeqi NP_110416.1. NM_030789.3. [Q8TCT9-1 ]
NP_848695.1. NM_178580.2. [Q8TCT9-4 ]
NP_848696.1. NM_178581.2. [Q8TCT9-2 ]
NP_848697.1. NM_178582.2.
UniGenei Hs.373741.

3D structure databases

ProteinModelPortali Q8TCT9.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 123505. 9 interactions.
IntActi Q8TCT9. 8 interactions.
MINTi MINT-3034232.

Protein family/group databases

MEROPSi A22.003.

PTM databases

PhosphoSitei Q8TCT9.

Polymorphism databases

DMDMi 25008563.

Proteomic databases

MaxQBi Q8TCT9.
PaxDbi Q8TCT9.
PRIDEi Q8TCT9.

Protocols and materials databases

DNASUi 81502.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000335574 ; ENSP00000335294 ; ENSG00000101294 . [Q8TCT9-4 ]
ENST00000340852 ; ENSP00000343032 ; ENSG00000101294 . [Q8TCT9-1 ]
ENST00000376127 ; ENSP00000365296 ; ENSG00000101294 . [Q8TCT9-5 ]
ENST00000398174 ; ENSP00000381237 ; ENSG00000101294 . [Q8TCT9-2 ]
GeneIDi 81502.
KEGGi hsa:81502.
UCSCi uc002wwc.3. human. [Q8TCT9-2 ]
uc002wwd.3. human. [Q8TCT9-4 ]
uc002wwe.3. human. [Q8TCT9-1 ]

Organism-specific databases

CTDi 81502.
GeneCardsi GC20P030106.
HGNCi HGNC:16435. HM13.
HPAi HPA045089.
MIMi 607106. gene.
neXtProti NX_Q8TCT9.
PharmGKBi PA29314.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG313636.
HOVERGENi HBG024161.
KOi K09595.
OMAi SSEMPET.
OrthoDBi EOG7Z3F4N.
PhylomeDBi Q8TCT9.
TreeFami TF105854.

Miscellaneous databases

ChiTaRSi HM13. human.
GeneWikii HM13.
GenomeRNAii 81502.
NextBioi 71746.
PROi Q8TCT9.
SOURCEi Search...

Gene expression databases

Bgeei Q8TCT9.
Genevestigatori Q8TCT9.

Family and domain databases

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

Publicationsi

« Hide 'large scale' publications
  1. "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] (ISOFORM 1), PROTEIN SEQUENCE OF 62-73; 128-136; 137-161; 242-251 AND 338-352, FUNCTION, GLYCOSYLATION, MUTAGENESIS OF ASN-10; ASN-20 AND ASP-265.
    Tissue: Cervix carcinoma.
  2. "Expression of the presenilin-like signal peptide peptidase (SPP) in mouse adult brain and during development."
    Urny J., Hermans-Borgmeyer I., Gercken G., Chica Schaller H.
    Gene Expr. Patterns 3:685-691(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
    Tissue: Placenta.
  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] (ISOFORMS 1; 2 AND 4), TISSUE SPECIFICITY.
    Tissue: Blood and Hippocampus.
  4. "Cell-surface expression of a new splice variant of the mouse signal peptide peptidase."
    Urny J., Hermans-Borgmeyer I., Schaller H.C.
    Biochim. Biophys. Acta 1759:159-165(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4).
  5. "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).
  6. "Genomic analysis of the H13 minor histocompatibility antigen gene."
    Brown A.C., Roopenian D.C.
    Submitted (FEB-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Aorta.
  8. "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] (ISOFORM 1).
    Tissue: Mammary gland, Retinoblastoma and Testis.
  9. "The DNA sequence and comparative analysis of human chromosome 20."
    Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E.
    , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.
    Nature 414:865-871(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  10. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  11. "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 and Muscle.
  12. "Intramembrane proteolysis of signal peptides: an essential step in the generation of HLA-E epitopes."
    Lemberg M.K., Bland F.A., Weihofen A., Braud V.M., Martoglio B.
    J. Immunol. 167:6441-6446(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  13. "Intramembrane proteolysis promotes trafficking of hepatitis C virus core protein to lipid droplets."
    McLauchlan J., Lemberg M.K., Hope G., Martoglio B.
    EMBO J. 21:3980-3988(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  14. "Impas 1 possesses endoproteolytic activity against multipass membrane protein substrate cleaving the presenilin 1 holoprotein."
    Moliaka Y.K., Grigorenko A., Madera D., Rogaev E.I.
    FEBS Lett. 557:185-192(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF ASP-219; GLY-264; ASP-265 AND PRO-317.
  15. "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: TOPOLOGY.
  16. "The TRC8 E3 ligase ubiquitinates MHC class I molecules before dislocation from the ER."
    Stagg H.R., Thomas M., van den Boomen D., Wiertz E.J., Drabkin H.A., Gemmill R.M., Lehner P.J.
    J. Cell Biol. 186:685-692(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RNF139.
  17. "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-10 AND ASN-20.
    Tissue: Liver.
  18. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiHM13_HUMAN
AccessioniPrimary (citable) accession number: Q8TCT9
Secondary accession number(s): B2RAY5
, E1P5L3, Q15K36, Q540H8, Q5JWP2, Q5JWP3, Q5JWP4, Q5JWP5, Q7Z4F2, Q86Y35, Q95H87, Q9H110, Q9H111
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 8, 2002
Last sequence update: June 1, 2002
Last modified: July 9, 2014
This is version 125 of the entry and version 1 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, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 20
    Human chromosome 20: 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

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