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Protein

Minor histocompatibility antigen H13

Gene

Hm13

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: 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. Involved in the intramembrane cleavage of the integral membrane protein PSEN1. Cleaves the integral membrane protein XBP1 isoform 1 in a DERL1/RNF139-dependent manner (By similarity). May play a role in graft rejection (PubMed:9354467).By similarity1 Publication

Sites

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

GO - Molecular functioni

GO - Biological processi

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):
Presenilin-like protein 3
Signal peptide peptidase
Gene namesi
Name:Hm13
Synonyms:H13, Psl3
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 2

Organism-specific databases

MGIiMGI:95886. H13.

Subcellular locationi

Isoform 4 :

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 3131LumenalBy similarityAdd
BLAST
Transmembranei32 – 5221HelicalSequence analysisAdd
BLAST
Topological domaini53 – 7725CytoplasmicSequence analysisAdd
BLAST
Transmembranei78 – 9821HelicalSequence analysisAdd
BLAST
Topological domaini99 – 1002LumenalSequence analysis
Transmembranei101 – 12121HelicalSequence analysisAdd
BLAST
Topological domaini122 – 15736CytoplasmicSequence analysisAdd
BLAST
Transmembranei158 – 17821HelicalSequence analysisAdd
BLAST
Topological domaini179 – 1813LumenalSequence analysis
Transmembranei182 – 20221HelicalSequence analysisAdd
BLAST
Topological domaini203 – 2097CytoplasmicSequence analysis
Transmembranei210 – 23021HelicalSequence analysisAdd
BLAST
Topological domaini231 – 25626LumenalBy similarityAdd
BLAST
Transmembranei257 – 27721HelicalSequence analysisAdd
BLAST
Topological domaini278 – 29013CytoplasmicSequence analysisAdd
BLAST
Transmembranei291 – 31121HelicalSequence analysisAdd
BLAST
Topological domaini312 – 3143LumenalSequence analysis
Transmembranei315 – 33521HelicalSequence analysisAdd
BLAST
Topological domaini336 – 37843CytoplasmicBy similarityAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Endoplasmic reticulum, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 378378Minor histocompatibility antigen H13PRO_0000073908Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi10 – 101N-linked (GlcNAc...)Sequence analysis
Glycosylationi20 – 201N-linked (GlcNAc...)Sequence analysis
Modified residuei368 – 3681PhosphoserineBy similarity

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

EPDiQ9D8V0.
MaxQBiQ9D8V0.
PRIDEiQ9D8V0.

PTM databases

iPTMnetiQ9D8V0.
PhosphoSiteiQ9D8V0.
SwissPalmiQ9D8V0.

Expressioni

Tissue specificityi

Widely expressed with highest levels in liver and kidney. In the brain, expressed predominantly in hippocampus, amygdala, piriform cortex, choroid plexus and arcuate nucleus of the hypothalamic area. Isoform 1 is more strongly expressed than isoform 4 in most tissues except brain and skeletal muscle where isoform 4 is the dominant isoform and in testis where isoform 1 and isoform 4 are expressed at similar levels. In the brain, isoform 4 is not detected in the choroid plexus.2 Publications

Developmental stagei

In the embryo, expression starts at day 6.5.1 Publication

Gene expression databases

BgeeiQ9D8V0.
CleanExiMM_H13.
ExpressionAtlasiQ9D8V0. baseline and differential.
GenevisibleiQ9D8V0. MM.

Interactioni

Subunit structurei

Monomer. Homodimer (By similarity). Interacts with RNF139 (PubMed:19720873). Interacts with DERL1 and XBP1 isoform 1 (By similarity).By similarity1 Publication

GO - Molecular functioni

Protein-protein interaction databases

MINTiMINT-1836977.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1INQX-ray2.20C169-177[»]
1JUFX-ray2.00C169-177[»]
ProteinModelPortaliQ9D8V0.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9D8V0.

Family & Domainsi

Motif

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

Domaini

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

Sequence similaritiesi

Belongs to the peptidase A22B family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

GeneTreeiENSGT00530000062920.
HOVERGENiHBG024161.
InParanoidiQ9D8V0.
KOiK09595.
OMAiDAKDLVC.
OrthoDBiEOG7Z3F4N.
PhylomeDBiQ9D8V0.
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. AlignAdd to basket

Isoform 1 (identifier: Q9D8V0-1) [UniParc]FASTAAdd to basket

Also known as: SPP-alpha

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
MDSAVSDPHN GSAEAGTPAN GTTRPPSTPE GIALAYGSLL LMALLPIFFG
60 70 80 90 100
ALRSVRCARG KSSSDMPETI TSRDAARFPI IASCTLLGLY LFFKIFSQEY
110 120 130 140 150
INLLLSMYFF VLGILALSHT ISPFMNKFFP ANFPNRQYQL LFTQGSGENK
160 170 180 190 200
EEIINYEFDT KDLVCLGLSS VVGVWYLLRK HWIANNLFGL AFSLNGVELL
210 220 230 240 250
HLNNVSTGCI LLGGLFIYDI FWVFGTNVMV TVAKSFEAPI KLVFPQDLLE
260 270 280 290 300
KGLEADNFAM LGLGDIVIPG IFIALLLRFD ISLKKNTHTY FYTSFAAYIF
310 320 330 340 350
GLGLTIFIMH IFKHAQPALL YLVPACIGFP VLVALAKGEV AEMFSYEESN
360 370
PKDPAAETES KEESTEASAS KRLEKKEK
Length:378
Mass (Da):41,748
Last modified:June 1, 2001 - v1
Checksum:iFB3B047323239A0D
GO
Isoform 2 (identifier: Q9D8V0-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     122-173: SPFMNKFFPA...VCLGLSSVVG → RSEGISRQPL...GNLPSRQHYT
     174-378: Missing.

Note: No experimental confirmation available.
Show »
Length:173
Mass (Da):18,706
Checksum:iA8592DD6E82FAA37
GO
Isoform 3 (identifier: Q9D8V0-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     119-151: HTISPFMNKFFPANFPNRQYQLLFTQGSGENKE → DDADSHALLQALTGWGWGGSLTLGSELIWPLCP
     181-193: HWIANNLFGLAFS → VSQSLRRRGGWAD

Show »
Length:378
Mass (Da):41,337
Checksum:iF6D4E61F39AC507C
GO
Isoform 4 (identifier: Q9D8V0-4) [UniParc]FASTAAdd to basket

Also known as: SPP-beta

The sequence of this isoform differs from the canonical sequence as follows:
     348-378: ESNPKDPAAETESKEESTEASASKRLEKKEK → SSAVILPHTP...RRRPQNPSAM

Show »
Length:394
Mass (Da):43,364
Checksum:i50072422E73F4D0F
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti42 – 421M → T in ABA56162 (PubMed:16730383).Curated
Sequence conflicti53 – 531R → P in CAC87793 (Ref. 3) Curated
Sequence conflicti53 – 531R → P in AAM22075 (Ref. 4) Curated
Sequence conflicti73 – 731R → Q in AAM22077 (Ref. 4) Curated
Sequence conflicti172 – 1721V → I in AAN77098 (PubMed:12972007).Curated
Sequence conflicti172 – 1721V → I in AAM22077 (Ref. 4) Curated
Sequence conflicti172 – 1721V → I in BAE34875 (PubMed:16141072).Curated
Sequence conflicti294 – 2941S → E in BAC25752 (PubMed:16141072).Curated
Sequence conflicti357 – 3571E → V in AAN77098 (PubMed:12972007).Curated
Sequence conflicti357 – 3571E → V in CAC87793 (Ref. 3) Curated
Sequence conflicti357 – 3571E → V in AAM22075 (Ref. 4) Curated
Sequence conflicti357 – 3571E → V in BAE34875 (PubMed:16141072).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei119 – 15133HTISP…GENKE → DDADSHALLQALTGWGWGGS LTLGSELIWPLCP in isoform 3. CuratedVSP_005201Add
BLAST
Alternative sequencei122 – 17352SPFMN…SSVVG → RSEGISRQPLKLLSQEPVQG LGWEHGLLCHSEPGLNPGCK IQGNLPSRQHYT in isoform 2. 1 PublicationVSP_005199Add
BLAST
Alternative sequencei174 – 378205Missing in isoform 2. 1 PublicationVSP_005200Add
BLAST
Alternative sequencei181 – 19313HWIAN…GLAFS → VSQSLRRRGGWAD in isoform 3. CuratedVSP_005202Add
BLAST
Alternative sequencei348 – 37831ESNPK…EKKEK → SSAVILPHTPRLTHFPTVSG SPASLADSMQQKLAGPRRRR PQNPSAM in isoform 4. 1 PublicationVSP_039805Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF515662 mRNA. Translation: AAN77098.1.
DQ168449 mRNA. Translation: ABA56162.1.
AJ345032 mRNA. Translation: CAC87793.1.
AF483214 mRNA. Translation: AAM22075.1.
AF483216 Genomic DNA. Translation: AAM22077.1.
AK004690 mRNA. Translation: BAB23476.1.
AK007664 mRNA. Translation: BAB25172.1.
AK012600 mRNA. No translation available.
AK019877 mRNA. Translation: BAB31897.1.
AK028109 mRNA. Translation: BAC25752.1.
AK049101 mRNA. Translation: BAC33543.1.
AK050664 mRNA. Translation: BAC34369.1.
AK080966 mRNA. Translation: BAC38098.1.
AK159176 mRNA. Translation: BAE34875.1.
AK169922 mRNA. Translation: BAE41461.1.
AL845162 Genomic DNA. Translation: CAM46159.1.
AL845162 Genomic DNA. Translation: CAM46160.1.
CH466551 Genomic DNA. Translation: EDL05980.1.
CH466551 Genomic DNA. Translation: EDL05981.1.
AF017785 mRNA. Translation: AAB81863.1.
BC034217 mRNA. No translation available.
CCDSiCCDS16896.1. [Q9D8V0-1]
CCDS50752.1. [Q9D8V0-4]
RefSeqiNP_001153023.1. NM_001159551.1. [Q9D8V0-4]
NP_001153025.1. NM_001159553.1. [Q9D8V0-2]
NP_034506.1. NM_010376.4. [Q9D8V0-1]
UniGeneiMm.277327.

Genome annotation databases

EnsembliENSMUST00000089059; ENSMUSP00000086460; ENSMUSG00000019188. [Q9D8V0-4]
ENSMUST00000125366; ENSMUSP00000120068; ENSMUSG00000019188. [Q9D8V0-1]
GeneIDi14950.
KEGGimmu:14950.
UCSCiuc008nfz.2. mouse. [Q9D8V0-2]
uc008ngb.2. mouse. [Q9D8V0-1]
uc008ngc.2. mouse. [Q9D8V0-4]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF515662 mRNA. Translation: AAN77098.1.
DQ168449 mRNA. Translation: ABA56162.1.
AJ345032 mRNA. Translation: CAC87793.1.
AF483214 mRNA. Translation: AAM22075.1.
AF483216 Genomic DNA. Translation: AAM22077.1.
AK004690 mRNA. Translation: BAB23476.1.
AK007664 mRNA. Translation: BAB25172.1.
AK012600 mRNA. No translation available.
AK019877 mRNA. Translation: BAB31897.1.
AK028109 mRNA. Translation: BAC25752.1.
AK049101 mRNA. Translation: BAC33543.1.
AK050664 mRNA. Translation: BAC34369.1.
AK080966 mRNA. Translation: BAC38098.1.
AK159176 mRNA. Translation: BAE34875.1.
AK169922 mRNA. Translation: BAE41461.1.
AL845162 Genomic DNA. Translation: CAM46159.1.
AL845162 Genomic DNA. Translation: CAM46160.1.
CH466551 Genomic DNA. Translation: EDL05980.1.
CH466551 Genomic DNA. Translation: EDL05981.1.
AF017785 mRNA. Translation: AAB81863.1.
BC034217 mRNA. No translation available.
CCDSiCCDS16896.1. [Q9D8V0-1]
CCDS50752.1. [Q9D8V0-4]
RefSeqiNP_001153023.1. NM_001159551.1. [Q9D8V0-4]
NP_001153025.1. NM_001159553.1. [Q9D8V0-2]
NP_034506.1. NM_010376.4. [Q9D8V0-1]
UniGeneiMm.277327.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1INQX-ray2.20C169-177[»]
1JUFX-ray2.00C169-177[»]
ProteinModelPortaliQ9D8V0.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

MINTiMINT-1836977.

Protein family/group databases

MEROPSiA22.003.

PTM databases

iPTMnetiQ9D8V0.
PhosphoSiteiQ9D8V0.
SwissPalmiQ9D8V0.

Proteomic databases

EPDiQ9D8V0.
MaxQBiQ9D8V0.
PRIDEiQ9D8V0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000089059; ENSMUSP00000086460; ENSMUSG00000019188. [Q9D8V0-4]
ENSMUST00000125366; ENSMUSP00000120068; ENSMUSG00000019188. [Q9D8V0-1]
GeneIDi14950.
KEGGimmu:14950.
UCSCiuc008nfz.2. mouse. [Q9D8V0-2]
uc008ngb.2. mouse. [Q9D8V0-1]
uc008ngc.2. mouse. [Q9D8V0-4]

Organism-specific databases

CTDi14950.
MGIiMGI:95886. H13.

Phylogenomic databases

GeneTreeiENSGT00530000062920.
HOVERGENiHBG024161.
InParanoidiQ9D8V0.
KOiK09595.
OMAiDAKDLVC.
OrthoDBiEOG7Z3F4N.
PhylomeDBiQ9D8V0.
TreeFamiTF105854.

Miscellaneous databases

EvolutionaryTraceiQ9D8V0.
PROiQ9D8V0.
SOURCEiSearch...

Gene expression databases

BgeeiQ9D8V0.
CleanExiMM_H13.
ExpressionAtlasiQ9D8V0. baseline and differential.
GenevisibleiQ9D8V0. MM.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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), SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
    Tissue: Placenta.
  2. "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), SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  3. "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).
    Strain: BALB/cJ.
  4. "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), NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 63-344.
    Strain: 129P3/J.
  5. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
    Strain: C57BL/6J.
    Tissue: Adipose tissue, Cerebellum, Embryo, Lung, Ovary, Pancreas, Thymus and Uterus.
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  7. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. "Minors held by majors: the H13 minor histocompatibility locus defined as a peptide/MHC class I complex."
    Mendoza L.M., Paz P., Zuberi A., Christianson G.J., Roopenian D.C., Shastri N.
    Immunity 7:461-472(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE OF 119-193 (ISOFORM 3), FUNCTION.
    Strain: BALB/cJ, C57BL/10, C57BL/6J and LP/J.
    Tissue: Thymic lymphoma.
  9. "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] OF 203-378 (ISOFORMS 1/3).
    Strain: FVB/N.
    Tissue: Mammary gland.
  10. "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.
  11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brown adipose tissue, Liver, Lung, Pancreas, Spleen and Testis.
  12. "How H13 histocompatibility peptides differing by a single methyl group and lacking conventional MHC binding anchor motifs determine self-nonself discrimination."
    Ostrov D.A., Roden M.M., Shi W., Palmieri E., Christianson G.J., Mendoza L., Villaflor G., Tilley D., Shastri N., Grey H., Almo S.C., Roopenian D.C., Nathenson S.G.
    J. Immunol. 168:283-289(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 169-177 IN COMPLEX WITH H2-D.

Entry informationi

Entry nameiHM13_MOUSE
AccessioniPrimary (citable) accession number: Q9D8V0
Secondary accession number(s): A3KGS1
, O19444, Q15K37, Q3TXP0, Q542R3, Q811Z6, Q8HWA9, Q8HWB5, Q9CQA4, Q9CSK9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 8, 2002
Last sequence update: June 1, 2001
Last modified: June 8, 2016
This is version 138 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. Peptidase families
    Classification of peptidase families and list of entries
  4. SIMILARITY comments
    Index of protein domains and families

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 one 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.