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Vacuolar protein sorting-associated protein 28 homolog (Caspase-activated DNase inhibitor that interacts with ASK1) (CIIA) (ESCRT-I complex subunit VPS28)

 VPS28_MOUSE             Reviewed;         221 AA.
Q9D1C8;
01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
01-JUN-2001, sequence version 1.
25-APR-2018, entry version 122.
RecName: Full=Vacuolar protein sorting-associated protein 28 homolog;
AltName: Full=Caspase-activated DNase inhibitor that interacts with ASK1;
Short=CIIA;
AltName: Full=ESCRT-I complex subunit VPS28;
Name=Vps28;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=BALB/cJ;
PubMed=14557248; DOI=10.1083/jcb.200303003;
Cho S.-G., Kim J.W., Lee Y.H., Hwang H.S., Kim M.S., Ryoo K.,
Kim M.J., Noh K.T., Kim E.K., Cho J.H., Yoon K.W., Cho E.G.,
Park H.S., Chi S.W., Lee M.J., Kang S.S., Ichijo H., Choi E.J.;
"Identification of a novel antiapoptotic protein that antagonizes ASK1
and CAD activities.";
J. Cell Biol. 163:71-81(2003).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J;
PubMed=16141072; DOI=10.1126/science.1112014;
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.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=FVB/N; TISSUE=Kidney;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
Pancreas, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- FUNCTION: Component of the ESCRT-I complex, a regulator of
vesicular trafficking process. {ECO:0000250}.
-!- SUBUNIT: Component of the ESCRT-I complex (endosomal sorting
complex required for transport I) which consists of TSG101, VPS28,
a VPS37 protein (VPS37A to -D) and MVB12A or MVB12B in a 1:1:1:1
stoichiometry. Interacts with TSG101, VPS37B, VPS37C, MVB12A and
MVB12B. Component of an ESCRT-I complex (endosomal sorting complex
required for transport I) which consists of TSG101, VPS28, VPS37A
and UBAP1 in a 1:1:1:1 stoichiometry. Interacts WITH VPS36; the
interaction mediates the association with the ESCRT-II complex.
Interacts with SNF8 and VPS25. Interacts with CEP55 (By
similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}. Late endosome
membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.
-!- SIMILARITY: Belongs to the VPS28 family. {ECO:0000255|PROSITE-
ProRule:PRU00642, ECO:0000255|PROSITE-ProRule:PRU00645}.
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EMBL; AF373710; AAN71982.1; -; mRNA.
EMBL; AK003699; BAB22945.1; -; mRNA.
EMBL; BC013535; AAH13535.1; -; mRNA.
CCDS; CCDS27579.1; -.
RefSeq; NP_001292597.1; NM_001305668.1.
RefSeq; NP_080118.1; NM_025842.4.
UniGene; Mm.30028; -.
ProteinModelPortal; Q9D1C8; -.
SMR; Q9D1C8; -.
BioGrid; 211806; 36.
IntAct; Q9D1C8; 36.
MINT; Q9D1C8; -.
STRING; 10090.ENSMUSP00000077856; -.
iPTMnet; Q9D1C8; -.
PhosphoSitePlus; Q9D1C8; -.
EPD; Q9D1C8; -.
MaxQB; Q9D1C8; -.
PaxDb; Q9D1C8; -.
PeptideAtlas; Q9D1C8; -.
PRIDE; Q9D1C8; -.
DNASU; 66914; -.
Ensembl; ENSMUST00000078803; ENSMUSP00000077856; ENSMUSG00000059323.
GeneID; 66914; -.
KEGG; mmu:66914; -.
UCSC; uc007wlc.2; mouse.
CTD; 51160; -.
MGI; MGI:1914164; Vps28.
eggNOG; KOG3284; Eukaryota.
eggNOG; ENOG4111IQ4; LUCA.
GeneTree; ENSGT00760000119090; -.
HOGENOM; HOG000203818; -.
HOVERGEN; HBG054248; -.
InParanoid; Q9D1C8; -.
KO; K12184; -.
OMA; KYRLDCP; -.
PhylomeDB; Q9D1C8; -.
TreeFam; TF313364; -.
ChiTaRS; Vps28; mouse.
PRO; PR:Q9D1C8; -.
Proteomes; UP000000589; Chromosome 15.
Bgee; ENSMUSG00000059323; -.
CleanEx; MM_VPS28; -.
ExpressionAtlas; Q9D1C8; baseline and differential.
Genevisible; Q9D1C8; MM.
GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
GO; GO:0005829; C:cytosol; ISO:MGI.
GO; GO:0005769; C:early endosome; ISO:MGI.
GO; GO:0005768; C:endosome; ISO:MGI.
GO; GO:0010008; C:endosome membrane; ISO:MGI.
GO; GO:0000813; C:ESCRT I complex; ISS:UniProtKB.
GO; GO:0031902; C:late endosome membrane; IEA:UniProtKB-SubCell.
GO; GO:0005886; C:plasma membrane; ISO:MGI.
GO; GO:0043130; F:ubiquitin binding; ISO:MGI.
GO; GO:0031397; P:negative regulation of protein ubiquitination; ISS:UniProtKB.
GO; GO:0045732; P:positive regulation of protein catabolic process; ISO:MGI.
GO; GO:2000397; P:positive regulation of ubiquitin-dependent endocytosis; ISO:MGI.
GO; GO:0043328; P:protein transport to vacuole involved in ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway; IBA:GO_Central.
GO; GO:0043162; P:ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway; ISS:UniProtKB.
Gene3D; 1.20.120.1130; -; 1.
Gene3D; 1.20.1440.200; -; 1.
InterPro; IPR037202; ESCRT_assembly_dom.
InterPro; IPR007143; Vps28.
InterPro; IPR017899; VPS28_C.
InterPro; IPR037206; VPS28_C_sf.
InterPro; IPR017898; VPS28_N.
InterPro; IPR038358; VPS28_N_sf.
PANTHER; PTHR12937; PTHR12937; 1.
Pfam; PF03997; VPS28; 1.
PIRSF; PIRSF017535; VPS28; 1.
SUPFAM; SSF140111; SSF140111; 1.
SUPFAM; SSF140427; SSF140427; 1.
PROSITE; PS51310; VPS28_C; 1.
PROSITE; PS51313; VPS28_N; 1.
1: Evidence at protein level;
Acetylation; Cell membrane; Complete proteome; Endosome; Membrane;
Protein transport; Reference proteome; Transport.
CHAIN 1 221 Vacuolar protein sorting-associated
protein 28 homolog.
/FTId=PRO_0000120952.
DOMAIN 13 120 VPS28 N-terminal. {ECO:0000255|PROSITE-
ProRule:PRU00645}.
DOMAIN 124 220 VPS28 C-terminal. {ECO:0000255|PROSITE-
ProRule:PRU00642}.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000250|UniProtKB:Q9UK41}.
SEQUENCE 221 AA; 25452 MW; DC144A4A27857245 CRC64;
MFHGIPATPG VGAPGNKPEL YEEVKLYKNA REREKYDNMA ELFAVVKTMQ ALEKAYIKDC
VTPNEYTAAC SRLLVQYKAA FRQVQGSEIS SIDEFCRKFR LDCPLAMERI KEDRPITIKD
DKGNLNRCIA DVVSLFITVM DKLRLEIRAM DEIQPDLREL METMHRMSHL PPDFEGRQTV
SQWLQTLSGM SASDELDDSQ VRQMLFDLES AYNAFNRFLH A


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