POMP_HUMAN
ID POMP_HUMAN Reviewed; 141 AA.
AC Q9Y244; A5HKJ2; D6MXU3; Q9HB69;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Proteasome maturation protein;
DE AltName: Full=Proteassemblin;
DE AltName: Full=Protein UMP1 homolog;
DE Short=hUMP1;
DE AltName: Full=Voltage-gated K channel beta subunit 4.1;
GN Name=POMP; Synonyms=C13orf12, UMP1; ORFNames=HSPC014, HSPC036, PNAS-110;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Heart;
RA Desir G.V., Tian S.;
RT "Identification of a novel Kv beta subunit.";
RL Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Heart;
RA Thomas D., Sullivan A.N., Goldstein S.A.;
RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], INVOLVEMENT IN KLICK, AND TISSUE SPECIFICITY.
RX PubMed=20226437; DOI=10.1016/j.ajhg.2010.02.018;
RA Dahlqvist J., Klar J., Tiwari N., Schuster J., Torma H., Badhai J.,
RA Pujol R., van Steensel M.A., Brinkhuizen T., Gijezen L., Chaves A.,
RA Tadini G., Vahlquist A., Dahl N.;
RT "A single-nucleotide deletion in the POMP 5' UTR causes a transcriptional
RT switch and altered epidermal proteasome distribution in KLICK
RT genodermatosis.";
RL Am. J. Hum. Genet. 86:596-603(2010).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Promyelocytic leukemia;
RA Yu W.-Q., Chai Y.-B., Sun B.-Z., Zhu F., Liu X.-S., Li Z., Lu F., Yan W.,
RA Yang H., Zhao Z.-L.;
RT "Human acute promyelocytic leukemia cell line NB4's apoptosis related
RT genes.";
RL Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Umbilical cord blood;
RX PubMed=11042152; DOI=10.1101/gr.140200;
RA Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G.,
RA Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W.,
RA Tao J., Huang Q.-H., Zhou J., Hu G.-X., Gu J., Chen S.-J., Chen Z.;
RT "Cloning and functional analysis of cDNAs with open reading frames for 300
RT previously undefined genes expressed in CD34+ hematopoietic stem/progenitor
RT cells.";
RL Genome Res. 10:1546-1560(2000).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Tongue;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057823; DOI=10.1038/nature02379;
RA Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L.,
RA Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S.,
RA Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Andrews D.T., Ashwell R.I.S., Babbage A.K., Bagguley C.L.,
RA Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P.,
RA Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P.,
RA Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C.,
RA Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P.,
RA Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L.,
RA Frankish A.G., Frankland J., French L., Garner P., Garnett J.,
RA Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M.,
RA Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D.,
RA Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D.,
RA Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S.,
RA Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S.,
RA Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R.,
RA Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W.,
RA Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P.,
RA Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L.,
RA Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R.,
RA Rogers J., Ross M.T.;
RT "The DNA sequence and analysis of human chromosome 13.";
RL Nature 428:522-528(2004).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Bone marrow, and Placenta;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [10]
RP PROTEIN SEQUENCE OF 69-79 AND 93-106, ASSOCIATION WITH PREPROTEASOME, AND
RP INDUCTION.
RX PubMed=10926487; DOI=10.1006/jmbi.2000.3959;
RA Witt E., Zantopf D., Schmidt M., Kraft R., Kloetzel P.-M., Krueger E.;
RT "Characterisation of the newly identified human Ump1 homologue POMP and
RT analysis of LMP7(beta 5i) incorporation into 20 S proteasomes.";
RL J. Mol. Biol. 301:1-9(2000).
RN [11]
RP ASSOCIATION WITH PREPROTEASOME.
RX PubMed=10891394; DOI=10.1006/mcbr.2000.0213;
RA Griffin T.A., Slack J.P., McCluskey T.S., Monaco J.J., Colbert R.A.;
RT "Identification of proteassemblin, a mammalian homologue of the yeast
RT protein, Ump1p, that is required for normal proteasome assembly.";
RL Mol. Cell Biol. Res. Commun. 3:212-217(2000).
RN [12]
RP ASSOCIATION WITH PREPROTEASOME, AND INDUCTION.
RX PubMed=10973495; DOI=10.1073/pnas.190268597;
RA Burri L., Hoeckendorff J., Boehm U., Klamp T., Dohmen R.J., Levy F.;
RT "Identification and characterization of a mammalian protein interacting
RT with 20S proteasome precursors.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:10348-10353(2000).
RN [13]
RP INTERACTION WITH PSMB1; PSMB4; PSMB5; PSMB6 AND PSMB9.
RX PubMed=14733938; DOI=10.1016/j.bbrc.2003.12.119;
RA Jayarapu K., Griffin T.A.;
RT "Protein-protein interactions among human 20S proteasome subunits and
RT proteassemblin.";
RL Biochem. Biophys. Res. Commun. 314:523-528(2004).
RN [14]
RP FUNCTION.
RX PubMed=16251969; DOI=10.1038/nature04106;
RA Hirano Y., Hendil K.B., Yashiroda H., Iemura S., Nagane R., Hioki Y.,
RA Natsume T., Tanaka K., Murata S.;
RT "A heterodimeric complex that promotes the assembly of mammalian 20S
RT proteasomes.";
RL Nature 437:1381-1385(2005).
RN [15]
RP FUNCTION, INDUCTION, AND INTERACTION WITH PSMB5 AND PSMB8.
RX PubMed=15944226; DOI=10.1073/pnas.0501711102;
RA Heink S., Ludwig D., Kloetzel P.-M., Krueger E.;
RT "IFN-gamma-induced immune adaptation of the proteasome system is an
RT accelerated and transient response.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:9241-9246(2005).
RN [16]
RP TETRAMERIZATION, AND SUBCELLULAR LOCATION.
RX PubMed=16624403; DOI=10.1016/j.ijbiomac.2006.03.015;
RA Hoefer M.M., Boneberg E.-M., Grotegut S., Kusch J., Illges H.;
RT "Possible tetramerisation of the proteasome maturation factor
RT POMP/proteassemblin/hUmp1 and its subcellular localisation.";
RL Int. J. Biol. Macromol. 38:259-267(2006).
RN [17]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=17948026; DOI=10.1038/sj.embor.7401091;
RA Fricke B., Heink S., Steffen J., Kloetzel P.M., Kruger E.;
RT "The proteasome maturation protein POMP facilitates major steps of 20S
RT proteasome formation at the endoplasmic reticulum.";
RL EMBO Rep. 8:1170-1175(2007).
RN [18]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [19]
RP INVOLVEMENT IN PRAAS2.
RX PubMed=26524591; DOI=10.1172/jci81260;
RA Brehm A., Liu Y., Sheikh A., Marrero B., Omoyinmi E., Zhou Q.,
RA Montealegre G., Biancotto A., Reinhardt A., Almeida de Jesus A.,
RA Pelletier M., Tsai W.L., Remmers E.F., Kardava L., Hill S., Kim H.,
RA Lachmann H.J., Megarbane A., Chae J.J., Brady J., Castillo R.D., Brown D.,
RA Casano A.V., Gao L., Chapelle D., Huang Y., Stone D., Chen Y., Sotzny F.,
RA Lee C.C., Kastner D.L., Torrelo A., Zlotogorski A., Moir S., Gadina M.,
RA McCoy P., Wesley R., Rother K., Hildebrand P.W., Brogan P., Krueger E.,
RA Aksentijevich I., Goldbach-Mansky R.;
RT "Additive loss-of-function proteasome subunit mutations in CANDLE/PRAAS
RT patients promote type I IFN production.";
RL J. Clin. Invest. 125:4196-4211(2015).
RN [20]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-39, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [21]
RP INVOLVEMENT IN PRAAS2.
RX PubMed=29805043; DOI=10.1016/j.ajhg.2018.04.010;
RG Undiagnosed Diseases Network members;
RA Poli M.C., Ebstein F., Nicholas S.K., de Guzman M.M., Forbes L.R.,
RA Chinn I.K., Mace E.M., Vogel T.P., Carisey A.F., Benavides F.,
RA Coban-Akdemir Z.H., Gibbs R.A., Jhangiani S.N., Muzny D.M.,
RA Carvalho C.M.B., Schady D.A., Jain M., Rosenfeld J.A., Emrick L.,
RA Lewis R.A., Lee B., Zieba B.A., Kuery S., Krueger E., Lupski J.R.,
RA Bostwick B.L., Orange J.S.;
RT "Heterozygous truncating variants in POMP escape nonsense-mediated decay
RT and cause a nique immune dysregulatory syndrome.";
RL Am. J. Hum. Genet. 102:1126-1142(2018).
CC -!- FUNCTION: Molecular chaperone essential for the assembly of standard
CC proteasomes and immunoproteasomes. Degraded after completion of
CC proteasome maturation. Mediates the association of 20S preproteasome
CC with the endoplasmic reticulum. {ECO:0000269|PubMed:15944226,
CC ECO:0000269|PubMed:16251969, ECO:0000269|PubMed:17948026}.
CC -!- SUBUNIT: Constituent of preproteasomes, but not of mature 20S
CC proteasomes. Within the preproteasome, may directly interact with
CC PSMB1/beta6, PSMB4/beta7, PSMB5/beta5, PSMB6/beta1 and PSMB9/beta1i.
CC Interaction with PSMB8/beta5i has been observed in PubMed:10973495, but
CC not in PubMed:10926487. Forms tetramers.
CC -!- INTERACTION:
CC Q9Y244; Q15777: MPPED2; NbExp=3; IntAct=EBI-696895, EBI-2350461;
CC Q9Y244; P20618: PSMB1; NbExp=3; IntAct=EBI-696895, EBI-372273;
CC Q9Y244; P49720: PSMB3; NbExp=3; IntAct=EBI-696895, EBI-603340;
CC Q9Y244; P28074: PSMB5; NbExp=3; IntAct=EBI-696895, EBI-357828;
CC Q9Y244; Q99436: PSMB7; NbExp=3; IntAct=EBI-696895, EBI-603319;
CC Q9Y244; P28065: PSMB9; NbExp=3; IntAct=EBI-696895, EBI-603300;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol. Nucleus. Microsome membrane.
CC -!- TISSUE SPECIFICITY: Strongly expressed from the basal layer to the
CC granular layer of healthy epidermis, whereas in KLICK patients there is
CC a gradual decrease of expression toward the granular layer.
CC {ECO:0000269|PubMed:20226437}.
CC -!- INDUCTION: By IFNG/IFN-gamma. {ECO:0000269|PubMed:10926487,
CC ECO:0000269|PubMed:10973495, ECO:0000269|PubMed:15944226}.
CC -!- DISEASE: Keratosis linearis with ichthyosis congenita and sclerosing
CC keratoderma (KLICK) [MIM:601952]: A keratinizing disorder characterized
CC by ichthyosis, palmoplantar keratoderma with constricting bands around
CC fingers, flexural deformities of fingers and keratotic papules in a
CC linear distribution on the flexural side of large joints. Histological
CC examination of the skin of affected individuals shows hypertrophy and
CC hyperplasia of the spinous, granular and horny epidermal layer.
CC {ECO:0000269|PubMed:20226437}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Proteasome-associated autoinflammatory syndrome 2 (PRAAS2)
CC [MIM:618048]: An autosomal dominant autoinflammatory disorder
CC characterized by onset in early infancy and severe inflammatory
CC neutrophilic dermatitis, autoimmunity, and variable immunodeficiency.
CC {ECO:0000269|PubMed:26524591, ECO:0000269|PubMed:29805043}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SIMILARITY: Belongs to the POMP/UMP1 family. {ECO:0000305}.
CC -!- CAUTION: Although this protein has been named voltage-gated K channel
CC beta subunit 4.1 in Ref.1 and Ref.2, there is no evidence that it may
CC play a role in ion transport. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG23819.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF262975; AAK58521.1; -; mRNA.
DR EMBL; EF535527; ABQ08566.1; -; mRNA.
DR EMBL; GU045555; ADE92939.1; -; mRNA.
DR EMBL; GU045556; ADE92940.1; -; mRNA.
DR EMBL; AF275807; AAG23819.1; ALT_FRAME; mRNA.
DR EMBL; AF077200; AAD26995.1; -; mRNA.
DR EMBL; AF125097; AAD39914.1; -; mRNA.
DR EMBL; AK312118; BAG35054.1; -; mRNA.
DR EMBL; AL359454; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471075; EAX08435.1; -; Genomic_DNA.
DR EMBL; BC014334; AAH14334.1; -; mRNA.
DR EMBL; BC003390; AAH03390.1; -; mRNA.
DR CCDS; CCDS9331.1; -.
DR RefSeq; NP_057016.1; NM_015932.5.
DR AlphaFoldDB; Q9Y244; -.
DR SMR; Q9Y244; -.
DR BioGRID; 119504; 66.
DR IntAct; Q9Y244; 50.
DR MINT; Q9Y244; -.
DR STRING; 9606.ENSP00000370222; -.
DR iPTMnet; Q9Y244; -.
DR PhosphoSitePlus; Q9Y244; -.
DR BioMuta; POMP; -.
DR DMDM; 74753466; -.
DR EPD; Q9Y244; -.
DR jPOST; Q9Y244; -.
DR MassIVE; Q9Y244; -.
DR MaxQB; Q9Y244; -.
DR PaxDb; Q9Y244; -.
DR PeptideAtlas; Q9Y244; -.
DR PRIDE; Q9Y244; -.
DR ProteomicsDB; 85643; -.
DR TopDownProteomics; Q9Y244; -.
DR Antibodypedia; 7516; 126 antibodies from 26 providers.
DR DNASU; 51371; -.
DR Ensembl; ENST00000380842.5; ENSP00000370222.4; ENSG00000132963.8.
DR GeneID; 51371; -.
DR KEGG; hsa:51371; -.
DR MANE-Select; ENST00000380842.5; ENSP00000370222.4; NM_015932.6; NP_057016.1.
DR UCSC; uc001usf.4; human.
DR CTD; 51371; -.
DR DisGeNET; 51371; -.
DR GeneCards; POMP; -.
DR HGNC; HGNC:20330; POMP.
DR HPA; ENSG00000132963; Low tissue specificity.
DR MalaCards; POMP; -.
DR MIM; 601952; phenotype.
DR MIM; 613386; gene.
DR MIM; 618048; phenotype.
DR neXtProt; NX_Q9Y244; -.
DR OpenTargets; ENSG00000132963; -.
DR Orphanet; 281201; Keratosis linearis-ichthyosis congenita-sclerosing keratoderma syndrome.
DR PharmGKB; PA134898606; -.
DR VEuPathDB; HostDB:ENSG00000132963; -.
DR eggNOG; KOG3061; Eukaryota.
DR GeneTree; ENSGT00390000010734; -.
DR HOGENOM; CLU_100687_3_0_1; -.
DR InParanoid; Q9Y244; -.
DR OMA; HHAMEVR; -.
DR OrthoDB; 1613776at2759; -.
DR PhylomeDB; Q9Y244; -.
DR TreeFam; TF323548; -.
DR PathwayCommons; Q9Y244; -.
DR SignaLink; Q9Y244; -.
DR BioGRID-ORCS; 51371; 375 hits in 1045 CRISPR screens.
DR ChiTaRS; POMP; human.
DR GeneWiki; POMP; -.
DR GenomeRNAi; 51371; -.
DR Pharos; Q9Y244; Tbio.
DR PRO; PR:Q9Y244; -.
DR Proteomes; UP000005640; Chromosome 13.
DR RNAct; Q9Y244; protein.
DR Bgee; ENSG00000132963; Expressed in heart right ventricle and 212 other tissues.
DR ExpressionAtlas; Q9Y244; baseline and differential.
DR Genevisible; Q9Y244; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0016607; C:nuclear speck; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0043248; P:proteasome assembly; IMP:UniProtKB.
DR InterPro; IPR008012; Ump1.
DR PANTHER; PTHR12828; PTHR12828; 1.
DR Pfam; PF05348; UMP1; 1.
PE 1: Evidence at protein level;
KW Chaperone; Cytoplasm; Direct protein sequencing; Endoplasmic reticulum;
KW Ichthyosis; Isopeptide bond; Membrane; Microsome; Nucleus;
KW Palmoplantar keratoderma; Reference proteome; Ubl conjugation.
FT CHAIN 1..141
FT /note="Proteasome maturation protein"
FT /id="PRO_0000247184"
FT MOTIF 68..72
FT /note="High-affinity association with the preproteasome"
FT CROSSLNK 39
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
SQ SEQUENCE 141 AA; 15789 MW; 2136624D232EF1C7 CRC64;
MNARGLGSEL KDSIPVTELS ASGPFESHDL LRKGFSCVKN ELLPSHPLEL SEKNFQLNQD
KMNFSTLRNI QGLFAPLKLQ MEFKAVQQVQ RLPFLSSSNL SLDVLRGNDE TIGFEDILND
PSQSEVMGEP HLMVEYKLGL L
