Full text data of POMP
POMP
(C13orf12, UMP1)
[Confidence: low (only semi-automatic identification from reviews)]
Proteasome maturation protein (Proteassemblin; Protein UMP1 homolog; hUMP1; Voltage-gated K channel beta subunit 4.1)
Proteasome maturation protein (Proteassemblin; Protein UMP1 homolog; hUMP1; Voltage-gated K channel beta subunit 4.1)
UniProt
Q9Y244
ID POMP_HUMAN Reviewed; 141 AA.
AC Q9Y244; A5HKJ2; D6MXU3; Q9HB69;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-NOV-1999, sequence version 1.
DT 22-JAN-2014, entry version 97.
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;
GN ORFNames=HSPC014, HSPC036, PNAS-110;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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
RP 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
RT transcriptional switch and altered epidermal proteasome distribution
RT in KLICK 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.,
RA Yan W., 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
RT 300 previously undefined genes expressed in CD34+ hematopoietic
RT stem/progenitor 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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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.,
RA Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T.,
RA Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R.,
RA Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S.,
RA 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.,
RA Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J.,
RA Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E.,
RA Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L.,
RA Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J.,
RA Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S.,
RA Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J.,
RA Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M.,
RA King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A.,
RA Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S.,
RA 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.,
RA Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S.,
RA Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A.,
RA Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B.,
RA Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L.,
RA Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R.M.,
RA Hubbard T., Sulston J.E., Beck S., Bentley D.R., 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.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA 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
RT project: 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,
RP AND 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
RT and 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
RT interacting 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.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: Molecular chaperone essential for the assembly of
CC standard proteasomes and immunoproteasomes. Degraded after
CC completion of proteasome maturation. Mediates the association of
CC 20S preproteasome with the endoplasmic reticulum.
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
CC PSMB9/beta1i. Interaction with PSMB8/beta5i has been observed in
CC PubMed:10973495, but not in PubMed:10926487. Forms tetramers.
CC -!- INTERACTION:
CC P28074:PSMB5; NbExp=3; IntAct=EBI-696895, EBI-357828;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol. Nucleus. Microsome
CC membrane.
CC -!- TISSUE SPECIFICITY: Strongly expressed from the basal layer to the
CC granular layer of healthy epidermis, whereas in KLICK patients
CC there is a gradual decrease of expression toward the granular
CC layer.
CC -!- INDUCTION: By IFNG/IFN-gamma.
CC -!- DISEASE: Keratosis linearis with ichthyosis congenita and
CC sclerosing keratoderma (KLICK) [MIM:601952]: A keratinizing
CC disorder characterized by ichthyosis, palmoplantar keratoderma
CC with constricting bands around fingers, flexural deformities of
CC fingers and keratotic papules in a linear distribution on the
CC flexural side of large joints. Histological examination of the
CC skin of affected individuals shows hypertrophy and hyperplasia of
CC the spinous, granular and horny epidermal layer. Note=The disease
CC is caused by mutations affecting the gene represented in this
CC entry.
CC -!- SIMILARITY: Belongs to the POMP/UMP1 family.
CC -!- CAUTION: Although this protein has been named voltage-gated K
CC channel beta subunit 4.1 in Ref.1 and Ref.2, there is no evidence
CC that it may play a role in ion transport.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG23819.1; Type=Frameshift; Positions=140;
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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; CAI17157.1; -; Genomic_DNA.
DR EMBL; CH471075; EAX08435.1; -; Genomic_DNA.
DR EMBL; BC014334; AAH14334.1; -; mRNA.
DR EMBL; BC003390; AAH03390.1; -; mRNA.
DR RefSeq; NP_057016.1; NM_015932.5.
DR UniGene; Hs.268742; -.
DR ProteinModelPortal; Q9Y244; -.
DR IntAct; Q9Y244; 27.
DR MINT; MINT-1695725; -.
DR STRING; 9606.ENSP00000370222; -.
DR PhosphoSite; Q9Y244; -.
DR DMDM; 74753466; -.
DR PaxDb; Q9Y244; -.
DR PRIDE; Q9Y244; -.
DR DNASU; 51371; -.
DR Ensembl; ENST00000380842; ENSP00000370222; ENSG00000132963.
DR GeneID; 51371; -.
DR KEGG; hsa:51371; -.
DR UCSC; uc001usf.3; human.
DR CTD; 51371; -.
DR GeneCards; GC13P029233; -.
DR HGNC; HGNC:20330; POMP.
DR HPA; HPA026995; -.
DR MIM; 601952; phenotype.
DR MIM; 613386; gene.
DR neXtProt; NX_Q9Y244; -.
DR Orphanet; 281201; Keratosis linearis-ichthyosis congenita-sclerosing keratoderma syndrome.
DR PharmGKB; PA134898606; -.
DR eggNOG; NOG248439; -.
DR HOGENOM; HOG000276894; -.
DR HOVERGEN; HBG057292; -.
DR InParanoid; Q9Y244; -.
DR KO; K11599; -.
DR OMA; DECIGFE; -.
DR OrthoDB; EOG715Q5T; -.
DR PhylomeDB; Q9Y244; -.
DR ChiTaRS; POMP; human.
DR GeneWiki; POMP; -.
DR GenomeRNAi; 51371; -.
DR NextBio; 54851; -.
DR PRO; PR:Q9Y244; -.
DR Bgee; Q9Y244; -.
DR CleanEx; HS_POMP; -.
DR Genevestigator; Q9Y244; -.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IDA:HPA.
DR GO; GO:0031090; C:organelle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000502; C:proteasome complex; IEA:UniProtKB-KW.
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; Complete proteome; Cytoplasm; Direct protein sequencing;
KW Endoplasmic reticulum; Ichthyosis; Membrane; Microsome; Nucleus;
KW Palmoplantar keratoderma; Proteasome; Reference proteome.
FT CHAIN 1 141 Proteasome maturation protein.
FT /FTId=PRO_0000247184.
FT MOTIF 68 72 High-affinity association with the
FT preproteasome.
SQ SEQUENCE 141 AA; 15789 MW; 2136624D232EF1C7 CRC64;
MNARGLGSEL KDSIPVTELS ASGPFESHDL LRKGFSCVKN ELLPSHPLEL SEKNFQLNQD
KMNFSTLRNI QGLFAPLKLQ MEFKAVQQVQ RLPFLSSSNL SLDVLRGNDE TIGFEDILND
PSQSEVMGEP HLMVEYKLGL L
//
ID POMP_HUMAN Reviewed; 141 AA.
AC Q9Y244; A5HKJ2; D6MXU3; Q9HB69;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-NOV-1999, sequence version 1.
DT 22-JAN-2014, entry version 97.
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;
GN ORFNames=HSPC014, HSPC036, PNAS-110;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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
RP 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
RT transcriptional switch and altered epidermal proteasome distribution
RT in KLICK 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.,
RA Yan W., 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
RT 300 previously undefined genes expressed in CD34+ hematopoietic
RT stem/progenitor 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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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.,
RA Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T.,
RA Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R.,
RA Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S.,
RA 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.,
RA Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J.,
RA Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E.,
RA Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L.,
RA Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J.,
RA Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S.,
RA Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J.,
RA Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M.,
RA King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A.,
RA Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S.,
RA 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.,
RA Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S.,
RA Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A.,
RA Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B.,
RA Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L.,
RA Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R.M.,
RA Hubbard T., Sulston J.E., Beck S., Bentley D.R., 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.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA 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
RT project: 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,
RP AND 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
RT and 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
RT interacting 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.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: Molecular chaperone essential for the assembly of
CC standard proteasomes and immunoproteasomes. Degraded after
CC completion of proteasome maturation. Mediates the association of
CC 20S preproteasome with the endoplasmic reticulum.
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
CC PSMB9/beta1i. Interaction with PSMB8/beta5i has been observed in
CC PubMed:10973495, but not in PubMed:10926487. Forms tetramers.
CC -!- INTERACTION:
CC P28074:PSMB5; NbExp=3; IntAct=EBI-696895, EBI-357828;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol. Nucleus. Microsome
CC membrane.
CC -!- TISSUE SPECIFICITY: Strongly expressed from the basal layer to the
CC granular layer of healthy epidermis, whereas in KLICK patients
CC there is a gradual decrease of expression toward the granular
CC layer.
CC -!- INDUCTION: By IFNG/IFN-gamma.
CC -!- DISEASE: Keratosis linearis with ichthyosis congenita and
CC sclerosing keratoderma (KLICK) [MIM:601952]: A keratinizing
CC disorder characterized by ichthyosis, palmoplantar keratoderma
CC with constricting bands around fingers, flexural deformities of
CC fingers and keratotic papules in a linear distribution on the
CC flexural side of large joints. Histological examination of the
CC skin of affected individuals shows hypertrophy and hyperplasia of
CC the spinous, granular and horny epidermal layer. Note=The disease
CC is caused by mutations affecting the gene represented in this
CC entry.
CC -!- SIMILARITY: Belongs to the POMP/UMP1 family.
CC -!- CAUTION: Although this protein has been named voltage-gated K
CC channel beta subunit 4.1 in Ref.1 and Ref.2, there is no evidence
CC that it may play a role in ion transport.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG23819.1; Type=Frameshift; Positions=140;
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
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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; CAI17157.1; -; Genomic_DNA.
DR EMBL; CH471075; EAX08435.1; -; Genomic_DNA.
DR EMBL; BC014334; AAH14334.1; -; mRNA.
DR EMBL; BC003390; AAH03390.1; -; mRNA.
DR RefSeq; NP_057016.1; NM_015932.5.
DR UniGene; Hs.268742; -.
DR ProteinModelPortal; Q9Y244; -.
DR IntAct; Q9Y244; 27.
DR MINT; MINT-1695725; -.
DR STRING; 9606.ENSP00000370222; -.
DR PhosphoSite; Q9Y244; -.
DR DMDM; 74753466; -.
DR PaxDb; Q9Y244; -.
DR PRIDE; Q9Y244; -.
DR DNASU; 51371; -.
DR Ensembl; ENST00000380842; ENSP00000370222; ENSG00000132963.
DR GeneID; 51371; -.
DR KEGG; hsa:51371; -.
DR UCSC; uc001usf.3; human.
DR CTD; 51371; -.
DR GeneCards; GC13P029233; -.
DR HGNC; HGNC:20330; POMP.
DR HPA; HPA026995; -.
DR MIM; 601952; phenotype.
DR MIM; 613386; gene.
DR neXtProt; NX_Q9Y244; -.
DR Orphanet; 281201; Keratosis linearis-ichthyosis congenita-sclerosing keratoderma syndrome.
DR PharmGKB; PA134898606; -.
DR eggNOG; NOG248439; -.
DR HOGENOM; HOG000276894; -.
DR HOVERGEN; HBG057292; -.
DR InParanoid; Q9Y244; -.
DR KO; K11599; -.
DR OMA; DECIGFE; -.
DR OrthoDB; EOG715Q5T; -.
DR PhylomeDB; Q9Y244; -.
DR ChiTaRS; POMP; human.
DR GeneWiki; POMP; -.
DR GenomeRNAi; 51371; -.
DR NextBio; 54851; -.
DR PRO; PR:Q9Y244; -.
DR Bgee; Q9Y244; -.
DR CleanEx; HS_POMP; -.
DR Genevestigator; Q9Y244; -.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IDA:HPA.
DR GO; GO:0031090; C:organelle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000502; C:proteasome complex; IEA:UniProtKB-KW.
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; Complete proteome; Cytoplasm; Direct protein sequencing;
KW Endoplasmic reticulum; Ichthyosis; Membrane; Microsome; Nucleus;
KW Palmoplantar keratoderma; Proteasome; Reference proteome.
FT CHAIN 1 141 Proteasome maturation protein.
FT /FTId=PRO_0000247184.
FT MOTIF 68 72 High-affinity association with the
FT preproteasome.
SQ SEQUENCE 141 AA; 15789 MW; 2136624D232EF1C7 CRC64;
MNARGLGSEL KDSIPVTELS ASGPFESHDL LRKGFSCVKN ELLPSHPLEL SEKNFQLNQD
KMNFSTLRNI QGLFAPLKLQ MEFKAVQQVQ RLPFLSSSNL SLDVLRGNDE TIGFEDILND
PSQSEVMGEP HLMVEYKLGL L
//
MIM
601952
*RECORD*
*FIELD* NO
601952
*FIELD* TI
#601952 KERATOSIS LINEARIS WITH ICHTHYOSIS CONGENITA AND SCLEROSING KERATODERMA
;;KLICK SYNDROME
read more*FIELD* TX
A number sign (#) is used with this entry because keratosis linearis
with ichthyosis congenita and sclerosing keratoderma (KLICK syndrome) is
caused by homozygous mutation in the POMP gene (613386).
CLINICAL FEATURES
Pujol et al. (1989) described 4 Spanish sibs with an autosomal recessive
keratinizing disorder thought to represent an entity that should be
classified among congenital syndromes. The most striking feature of the
patients' skin was the early appearance of linear hyperkeratosis without
evidence of Koebner phenomenon.
Vahlquist et al. (1997) described an isolated case of what was thought
to be the same disorder, which they referred to as KLICK syndrome
(keratosis linearis with ichthyosis congenita and sclerosing
keratoderma). The 32-year-old patient had a moderate, nonblistering
ichthyosis since birth and longstanding palmoplantar keratoderma with
pseudoainhum and a sclerosing flexion deformity of the fingers.
Longitudinal, noninflamed keratotic striae, which had appeared
spontaneously, were seen around his wrists, in the armfolds, and behind
the knees. The patient was otherwise physically and mentally healthy and
had no history of dental, nail, hair, or mucous membrane problems. The
parents were nonconsanguineous, and all 5 of his half sibs were healthy
and without skin symptoms. The condition improved on oral etretinate
therapy. On light microscopy, the involved epidermis showed marked
acanthosis with hypergranulosis and hyperkeratosis. Electron microscopy
disclosed numerous large keratohyaline granules in superficial
keratinocytes. Vahlquist et al. (1997) suggested that the condition is
due to a genetic defect in the formation of keratohyaline granules.
INHERITANCE
Vahlquist et al. (1997) suggested that KLICK syndrome is an autosomal
recessive disorder.
MAPPING
Dahlqvist et al. (2010) performed whole-genome SNP analysis on DNA from
3 Spanish sibs and 3 Swedish sporadic cases with KLICK syndrome and
identified a 1.5-Mb homozygous candidate region on chromosome 13q.
Microsatellite marker analysis further refined the critical region to an
approximately 0.8-Mb interval spanning 10 annotated genes and 2
pseudogenes.
MOLECULAR GENETICS
In 12 patients from 8 European families with KLICK syndrome mapping to
chromosome 13q, Dahlqvist et al. (2010) analyzed candidate genes and
identified homozygosity for a 1-bp deletion in the POMP gene
(613386.0001). Segregation analysis showed that the 6 available parents
were heterozygous and the 5 available healthy sibs were either
heterozygous or noncarriers for the deletion, which was not found in 280
Swedish control chromosomes. Immunohistochemical staining of patient
skin biopsies revealed an altered distribution of POMP and proteasome
subunits during formation of the horny layer, suggesting that KILCK
syndrome is caused by proteasome insufficiency at a specific stage of
epidermal differentiation.
*FIELD* RF
1. Dahlqvist, J.; Klar, J.; Tiwari, N.; Schuster, J.; Torma, H.; Badhai,
J.; Pujol, R.; van Steensel, M. A. M.; Brinkhuizen, T.; Gijezen, L.;
Chaves, A.; Tadini, G.; Vahlquist, A.; Dahl, N.: A single-nucleotide
deletion in the POMP 5-prime UTR causes a transcriptional switch and
altered epidermal proteasome distribution in KLICK genodermatosis. Am.
J. Hum. Genet. 86: 596-603, 2010. Note: Erratum: Am. J. Hum. Genet.
86: 655 only, 2010.
2. Pujol, R. M.; Moreno, A.; Alomar, A.; de Moragas, J. M.: Congenital
ichthyosiform dermatosis with linear keratotic flexural papules and
sclerosing palmoplantar keratoderma. Arch. Derm. 125: 103-106, 1989.
3. Vahlquist, A.; Ponten, F.; Pettersson, A.: Keratosis linearis
with ichthyosis congenita and sclerosing keratoderma (KLICK-syndrome):
a rare, autosomal recessive disorder of keratohyaline formation? Acta
Derm. Venereol. 77: 225-227, 1997.
*FIELD* CS
INHERITANCE:
Autosomal recessive
SKIN, NAILS, HAIR:
[Skin];
Ichthyosis, congenital, nonblistering;
Linear arrays of macular hyperkeratoses in flexural areas;
Honeycomb palmoplantar keratoderma;
Pseudoainhum;
HISTOLOGY:;
Acanthosis with hypergranulosis and hyperkeratosis in affected skin;
Parakeratosis;
Mild superficial perivascular lymphohistiocytic infiltrates;
ELECTRON MICROSCOPY:;
Numerous large keratohyaline granules in superficial keratinocytes;
[Nails];
Nail dystrophy with overcurvature
MOLECULAR BASIS:
Caused by mutation in the proteasome maturation protein gene (POMP,
613386.0001)
*FIELD* CN
Marla J. F. O'Neill - updated: 10/26/2011
Gary A. Bellus - revised: 4/13/2005
*FIELD* CD
John F. Jackson: 11/17/1998
*FIELD* ED
joanna: 10/26/2011
alopez: 1/24/2007
joanna: 4/13/2005
*FIELD* CN
Marla J. F. O'Neill - updated: 4/28/2010
*FIELD* CD
Victor A. McKusick: 8/22/1997
*FIELD* ED
carol: 04/28/2010
carol: 4/28/2010
carol: 7/25/2003
dholmes: 9/9/1997
jenny: 8/22/1997
*RECORD*
*FIELD* NO
601952
*FIELD* TI
#601952 KERATOSIS LINEARIS WITH ICHTHYOSIS CONGENITA AND SCLEROSING KERATODERMA
;;KLICK SYNDROME
read more*FIELD* TX
A number sign (#) is used with this entry because keratosis linearis
with ichthyosis congenita and sclerosing keratoderma (KLICK syndrome) is
caused by homozygous mutation in the POMP gene (613386).
CLINICAL FEATURES
Pujol et al. (1989) described 4 Spanish sibs with an autosomal recessive
keratinizing disorder thought to represent an entity that should be
classified among congenital syndromes. The most striking feature of the
patients' skin was the early appearance of linear hyperkeratosis without
evidence of Koebner phenomenon.
Vahlquist et al. (1997) described an isolated case of what was thought
to be the same disorder, which they referred to as KLICK syndrome
(keratosis linearis with ichthyosis congenita and sclerosing
keratoderma). The 32-year-old patient had a moderate, nonblistering
ichthyosis since birth and longstanding palmoplantar keratoderma with
pseudoainhum and a sclerosing flexion deformity of the fingers.
Longitudinal, noninflamed keratotic striae, which had appeared
spontaneously, were seen around his wrists, in the armfolds, and behind
the knees. The patient was otherwise physically and mentally healthy and
had no history of dental, nail, hair, or mucous membrane problems. The
parents were nonconsanguineous, and all 5 of his half sibs were healthy
and without skin symptoms. The condition improved on oral etretinate
therapy. On light microscopy, the involved epidermis showed marked
acanthosis with hypergranulosis and hyperkeratosis. Electron microscopy
disclosed numerous large keratohyaline granules in superficial
keratinocytes. Vahlquist et al. (1997) suggested that the condition is
due to a genetic defect in the formation of keratohyaline granules.
INHERITANCE
Vahlquist et al. (1997) suggested that KLICK syndrome is an autosomal
recessive disorder.
MAPPING
Dahlqvist et al. (2010) performed whole-genome SNP analysis on DNA from
3 Spanish sibs and 3 Swedish sporadic cases with KLICK syndrome and
identified a 1.5-Mb homozygous candidate region on chromosome 13q.
Microsatellite marker analysis further refined the critical region to an
approximately 0.8-Mb interval spanning 10 annotated genes and 2
pseudogenes.
MOLECULAR GENETICS
In 12 patients from 8 European families with KLICK syndrome mapping to
chromosome 13q, Dahlqvist et al. (2010) analyzed candidate genes and
identified homozygosity for a 1-bp deletion in the POMP gene
(613386.0001). Segregation analysis showed that the 6 available parents
were heterozygous and the 5 available healthy sibs were either
heterozygous or noncarriers for the deletion, which was not found in 280
Swedish control chromosomes. Immunohistochemical staining of patient
skin biopsies revealed an altered distribution of POMP and proteasome
subunits during formation of the horny layer, suggesting that KILCK
syndrome is caused by proteasome insufficiency at a specific stage of
epidermal differentiation.
*FIELD* RF
1. Dahlqvist, J.; Klar, J.; Tiwari, N.; Schuster, J.; Torma, H.; Badhai,
J.; Pujol, R.; van Steensel, M. A. M.; Brinkhuizen, T.; Gijezen, L.;
Chaves, A.; Tadini, G.; Vahlquist, A.; Dahl, N.: A single-nucleotide
deletion in the POMP 5-prime UTR causes a transcriptional switch and
altered epidermal proteasome distribution in KLICK genodermatosis. Am.
J. Hum. Genet. 86: 596-603, 2010. Note: Erratum: Am. J. Hum. Genet.
86: 655 only, 2010.
2. Pujol, R. M.; Moreno, A.; Alomar, A.; de Moragas, J. M.: Congenital
ichthyosiform dermatosis with linear keratotic flexural papules and
sclerosing palmoplantar keratoderma. Arch. Derm. 125: 103-106, 1989.
3. Vahlquist, A.; Ponten, F.; Pettersson, A.: Keratosis linearis
with ichthyosis congenita and sclerosing keratoderma (KLICK-syndrome):
a rare, autosomal recessive disorder of keratohyaline formation? Acta
Derm. Venereol. 77: 225-227, 1997.
*FIELD* CS
INHERITANCE:
Autosomal recessive
SKIN, NAILS, HAIR:
[Skin];
Ichthyosis, congenital, nonblistering;
Linear arrays of macular hyperkeratoses in flexural areas;
Honeycomb palmoplantar keratoderma;
Pseudoainhum;
HISTOLOGY:;
Acanthosis with hypergranulosis and hyperkeratosis in affected skin;
Parakeratosis;
Mild superficial perivascular lymphohistiocytic infiltrates;
ELECTRON MICROSCOPY:;
Numerous large keratohyaline granules in superficial keratinocytes;
[Nails];
Nail dystrophy with overcurvature
MOLECULAR BASIS:
Caused by mutation in the proteasome maturation protein gene (POMP,
613386.0001)
*FIELD* CN
Marla J. F. O'Neill - updated: 10/26/2011
Gary A. Bellus - revised: 4/13/2005
*FIELD* CD
John F. Jackson: 11/17/1998
*FIELD* ED
joanna: 10/26/2011
alopez: 1/24/2007
joanna: 4/13/2005
*FIELD* CN
Marla J. F. O'Neill - updated: 4/28/2010
*FIELD* CD
Victor A. McKusick: 8/22/1997
*FIELD* ED
carol: 04/28/2010
carol: 4/28/2010
carol: 7/25/2003
dholmes: 9/9/1997
jenny: 8/22/1997
MIM
613386
*RECORD*
*FIELD* NO
613386
*FIELD* TI
*613386 PROTEASOME MATURATION PROTEIN; POMP
;;UMP1, YEAST, HOMOLOG OF; UMP1;;
PROTEASSEMBLIN
read more*FIELD* TX
DESCRIPTION
The 20S proteasome is the proteolytically active component of the larger
26S proteasome complex. The 20S subunit has a 4-ring structure, with 2
outer rings formed by 7 alpha subunits (e.g., PSMA1; 602854) and 2 inner
rings formed by 7 beta subunits (e.g., PSMB1; 602017). Assembly of this
structure occurs via distinct intermediates of approximately 13S and
16S. POMP associates specifically with these precursor intermediates and
facilitates the sequential assembly of beta subunits onto the preformed
alpha subunit rings (Witt et al., 2000; Fricke et al., 2007).
CLONING
By sequencing peptides derived from a subunit of the 16S proteasome
intermediate in a human B-cell line, followed by database analysis, Witt
et al. (2000) identified POMP. The deduced 141-amino acid protein has a
calculated molecular mass of 15.8 kD. Human, rat, and mouse POMP share
over 90% amino acid identity. By 2-dimensional gel electrophoresis, POMP
had an apparent molecular mass of 16 kD.
By gel filtration under nondenaturing conditions, Hoefer et al. (2006)
found that, following removal of the GST tag, recombinant human POMP
eluted at an apparent molecular mass of about 64 kD, suggesting that
native POMP forms tetramers. Fractionation of 2 human B-lymphoid cell
lines and immunoprecipitation showed that POMP was enriched in the
cytosolic fraction. Immunohistochemical analysis of HEK293 cells also
showed nuclear punctate staining, in addition to more diffuse nuclear
and cytoplasmic staining.
MAPPING
Hartz (2010) mapped the POMP gene to chromosome 13q12.3 based on an
alignment of the POMP sequence (GenBank GENBANK AF077200) with the
genomic sequence (GRCh37).
GENE FUNCTION
By Western blot analysis of HeLa cell lysates and immunoprecipitation
analysis, Witt et al. (2000) confirmed that POMP associated specifically
with proteasome precursor complexes, but not with the mature 20S
proteasome.
Chondrogianni and Gonos (2007) found that overexpression of POMP in
human embryonic fibroblasts increased the level of functional proteasome
and enhanced the capacity of fibroblasts to cope with various oxidative
stressors.
Using precursor complex-specific antibodies, Fricke et al. (2007) showed
that the main steps in 20S core complex formation occurred at the
endoplasmic reticulum (ER). POMP associated with microsomal membranes
and was easily solubilized, suggesting that it is a peripheral membrane
protein. Protein-interaction assays revealed that POMP bound all beta
subunits proforms, including immunosubunits (e.g., PSMB9; 177045). POMP
also interacted directly with the alpha-3 (PSMA3; 176843), -4 (PSMA4;
176846), and -7 (PSMA7; 606607) subunits. POMP interacted in vitro with
the alpha(1-7) ring complex and incorporated beta subunits in a stepwise
fashion at the ER. Depletion of POMP abolished the association of beta
subunit proforms with the ER, suggesting that POMP mediates the
association of pre20S with the ER. Fricke et al. (2007) proposed a model
for proteasome assembly where alpha ring assembly is facilitated by PACs
(see PAC1, or PSMG1; 605296) and targeted to the ER either by PAC1 or by
interaction with POMP. There, POMP recruits the remaining beta subunits
into the nascent complex and supports final proteasome maturation.
MOLECULAR GENETICS
In 12 patients from 8 European families with keratosis linearis with
ichthyosis congenita and sclerosing keratoderma (KLICK syndrome; 601952)
mapping to chromosome 13q, Dahlqvist et al. (2010) analyzed candidate
genes and identified homozygosity for a 1-bp deletion in the POMP gene
(613386.0001). The deletion is included in POMP transcript variants with
long 5-prime UTRs and was associated with a marked increase in these
transcript variants in keratinocytes from KLICK patients.
Immunohistochemical analysis of patient skin biopsies revealed an
altered epidermal distribution of POMP, the proteasome subunit proteins
alpha-7 (606607) and beta-5 (600306), and the endoplasmic reticulum
stress marker CHOP (126337). In addition, staining of filaggrin
(135940), which in normal samples was restricted to the outermost cells
of the granular layer and the most basal cells of the horny layer,
occurred almost exclusively in the horny layer in patient skin biopsies,
in a broad and inconsistent manner. Dahlqvist et al. (2010) concluded
that the proteasome has a prominent role in the terminal differentiation
of the human epidermis.
*FIELD* AV
.0001
KERATOSIS LINEARIS WITH ICHTHYOSIS CONGENITA AND SCLEROSING KERATODERMA
POMP, 1-BP DEL, -95C
In 12 patients from 8 European families with keratosis linearis with
ichthyosis congenita and sclerosing keratoderma (KLICK syndrome;
601952), Dahlqvist et al. (2010) identified homozygosity for a 1-bp
deletion (-95delC) within a highly conserved 19-bp sequence in the
5-prime region of the POMP gene. Segregation analysis showed that the 6
available parents were heterozygous and the 5 available healthy sibs
were either heterozygous or noncarriers for the deletion, which was not
found in 280 Swedish control chromosomes. Haplotype analysis in the 8
affected probands formed at least 5 different haplotypes, suggesting
that the -95delC variant is a recurrent rather than a founder mutation.
The deletion is included in POMP transcript variants with long 5-prime
UTRs, and levels of the longer transcripts were significantly increased
in patients compared to controls in both nondifferentiated and
differentiated keratinocytes. Immunohistochemical analysis of skin
biopsies revealed an altered epidermal distribution of POMP and the
proteasome subunits alpha-7 and beta-5 (600306), with decreased staining
in the granular layer of patients compared to controls.
*FIELD* RF
1. Chondrogianni, N.; Gonos, E. S.: Overexpression of hUMP1/POMP
proteasome accessory protein enhances proteasome-mediated antioxidant
defence. Exp. Gerontol. 42: 899-903, 2007.
2. Dahlqvist, J.; Klar, J.; Tiwari, N.; Schuster, J.; Torma, H.; Badhai,
J.; Pujol, R.; van Steensel, M. A. M.; Brinkhuizen, T.; Gijezen, L.;
Chaves, A.; Tadini, G.; Vahlquist, A.; Dahl, N.: A single-nucleotide
deletion in the POMP 5-prime UTR causes a transcriptional switch and
altered epidermal proteasome distribution in KLICK genodermatosis. Am.
J. Hum. Genet. 86: 596-603, 2010. Note: Erratum: Am. J. Hum. Genet.
86: 655 only, 2010.
3. Fricke, B.; Heink, S.; Steffen, J.; Kloetzel, P.-M.; Kruger, E.
: The proteasome maturation protein POMP facilitates major steps of
20S proteasome formation at the endoplasmic reticulum. EMBO J. 8:
1170-1175, 2007.
4. Hartz, P. A.: Personal Communication. Baltimore, Md. 4/27/2010.
5. Hoefer, M. M.; Boneberg, E.-M.; Grotegut, S.; Kusch, J.; Illges,
H.: Possible tetramerisation of the proteasome maturation factor
POMP/proteassemblin/hUmp1 and its subcellular localisation. Int.
J. Biol. Macromol. 38: 259-267, 2006.
6. Witt, E.; Zantopf, D.; Schmidt, M.; Kraft, R.; Kloetzel, P.-M.;
Kruger, E.: Characterisation of the newly identified human Ump1 homologue
POMP and analysis of LMP7(beta-5i) incorporation into 20 S proteasomes. J.
Molec. Biol. 301: 1-9, 2000.
*FIELD* CN
Ada Hamosh - updated: 4/30/2010
Marla J. F. O'Neill - updated: 4/28/2010
*FIELD* CD
Patricia A. Hartz: 4/27/2010
*FIELD* ED
carol: 05/23/2012
terry: 12/6/2010
mgross: 4/30/2010
terry: 4/30/2010
carol: 4/28/2010
mgross: 4/27/2010
*RECORD*
*FIELD* NO
613386
*FIELD* TI
*613386 PROTEASOME MATURATION PROTEIN; POMP
;;UMP1, YEAST, HOMOLOG OF; UMP1;;
PROTEASSEMBLIN
read more*FIELD* TX
DESCRIPTION
The 20S proteasome is the proteolytically active component of the larger
26S proteasome complex. The 20S subunit has a 4-ring structure, with 2
outer rings formed by 7 alpha subunits (e.g., PSMA1; 602854) and 2 inner
rings formed by 7 beta subunits (e.g., PSMB1; 602017). Assembly of this
structure occurs via distinct intermediates of approximately 13S and
16S. POMP associates specifically with these precursor intermediates and
facilitates the sequential assembly of beta subunits onto the preformed
alpha subunit rings (Witt et al., 2000; Fricke et al., 2007).
CLONING
By sequencing peptides derived from a subunit of the 16S proteasome
intermediate in a human B-cell line, followed by database analysis, Witt
et al. (2000) identified POMP. The deduced 141-amino acid protein has a
calculated molecular mass of 15.8 kD. Human, rat, and mouse POMP share
over 90% amino acid identity. By 2-dimensional gel electrophoresis, POMP
had an apparent molecular mass of 16 kD.
By gel filtration under nondenaturing conditions, Hoefer et al. (2006)
found that, following removal of the GST tag, recombinant human POMP
eluted at an apparent molecular mass of about 64 kD, suggesting that
native POMP forms tetramers. Fractionation of 2 human B-lymphoid cell
lines and immunoprecipitation showed that POMP was enriched in the
cytosolic fraction. Immunohistochemical analysis of HEK293 cells also
showed nuclear punctate staining, in addition to more diffuse nuclear
and cytoplasmic staining.
MAPPING
Hartz (2010) mapped the POMP gene to chromosome 13q12.3 based on an
alignment of the POMP sequence (GenBank GENBANK AF077200) with the
genomic sequence (GRCh37).
GENE FUNCTION
By Western blot analysis of HeLa cell lysates and immunoprecipitation
analysis, Witt et al. (2000) confirmed that POMP associated specifically
with proteasome precursor complexes, but not with the mature 20S
proteasome.
Chondrogianni and Gonos (2007) found that overexpression of POMP in
human embryonic fibroblasts increased the level of functional proteasome
and enhanced the capacity of fibroblasts to cope with various oxidative
stressors.
Using precursor complex-specific antibodies, Fricke et al. (2007) showed
that the main steps in 20S core complex formation occurred at the
endoplasmic reticulum (ER). POMP associated with microsomal membranes
and was easily solubilized, suggesting that it is a peripheral membrane
protein. Protein-interaction assays revealed that POMP bound all beta
subunits proforms, including immunosubunits (e.g., PSMB9; 177045). POMP
also interacted directly with the alpha-3 (PSMA3; 176843), -4 (PSMA4;
176846), and -7 (PSMA7; 606607) subunits. POMP interacted in vitro with
the alpha(1-7) ring complex and incorporated beta subunits in a stepwise
fashion at the ER. Depletion of POMP abolished the association of beta
subunit proforms with the ER, suggesting that POMP mediates the
association of pre20S with the ER. Fricke et al. (2007) proposed a model
for proteasome assembly where alpha ring assembly is facilitated by PACs
(see PAC1, or PSMG1; 605296) and targeted to the ER either by PAC1 or by
interaction with POMP. There, POMP recruits the remaining beta subunits
into the nascent complex and supports final proteasome maturation.
MOLECULAR GENETICS
In 12 patients from 8 European families with keratosis linearis with
ichthyosis congenita and sclerosing keratoderma (KLICK syndrome; 601952)
mapping to chromosome 13q, Dahlqvist et al. (2010) analyzed candidate
genes and identified homozygosity for a 1-bp deletion in the POMP gene
(613386.0001). The deletion is included in POMP transcript variants with
long 5-prime UTRs and was associated with a marked increase in these
transcript variants in keratinocytes from KLICK patients.
Immunohistochemical analysis of patient skin biopsies revealed an
altered epidermal distribution of POMP, the proteasome subunit proteins
alpha-7 (606607) and beta-5 (600306), and the endoplasmic reticulum
stress marker CHOP (126337). In addition, staining of filaggrin
(135940), which in normal samples was restricted to the outermost cells
of the granular layer and the most basal cells of the horny layer,
occurred almost exclusively in the horny layer in patient skin biopsies,
in a broad and inconsistent manner. Dahlqvist et al. (2010) concluded
that the proteasome has a prominent role in the terminal differentiation
of the human epidermis.
*FIELD* AV
.0001
KERATOSIS LINEARIS WITH ICHTHYOSIS CONGENITA AND SCLEROSING KERATODERMA
POMP, 1-BP DEL, -95C
In 12 patients from 8 European families with keratosis linearis with
ichthyosis congenita and sclerosing keratoderma (KLICK syndrome;
601952), Dahlqvist et al. (2010) identified homozygosity for a 1-bp
deletion (-95delC) within a highly conserved 19-bp sequence in the
5-prime region of the POMP gene. Segregation analysis showed that the 6
available parents were heterozygous and the 5 available healthy sibs
were either heterozygous or noncarriers for the deletion, which was not
found in 280 Swedish control chromosomes. Haplotype analysis in the 8
affected probands formed at least 5 different haplotypes, suggesting
that the -95delC variant is a recurrent rather than a founder mutation.
The deletion is included in POMP transcript variants with long 5-prime
UTRs, and levels of the longer transcripts were significantly increased
in patients compared to controls in both nondifferentiated and
differentiated keratinocytes. Immunohistochemical analysis of skin
biopsies revealed an altered epidermal distribution of POMP and the
proteasome subunits alpha-7 and beta-5 (600306), with decreased staining
in the granular layer of patients compared to controls.
*FIELD* RF
1. Chondrogianni, N.; Gonos, E. S.: Overexpression of hUMP1/POMP
proteasome accessory protein enhances proteasome-mediated antioxidant
defence. Exp. Gerontol. 42: 899-903, 2007.
2. Dahlqvist, J.; Klar, J.; Tiwari, N.; Schuster, J.; Torma, H.; Badhai,
J.; Pujol, R.; van Steensel, M. A. M.; Brinkhuizen, T.; Gijezen, L.;
Chaves, A.; Tadini, G.; Vahlquist, A.; Dahl, N.: A single-nucleotide
deletion in the POMP 5-prime UTR causes a transcriptional switch and
altered epidermal proteasome distribution in KLICK genodermatosis. Am.
J. Hum. Genet. 86: 596-603, 2010. Note: Erratum: Am. J. Hum. Genet.
86: 655 only, 2010.
3. Fricke, B.; Heink, S.; Steffen, J.; Kloetzel, P.-M.; Kruger, E.
: The proteasome maturation protein POMP facilitates major steps of
20S proteasome formation at the endoplasmic reticulum. EMBO J. 8:
1170-1175, 2007.
4. Hartz, P. A.: Personal Communication. Baltimore, Md. 4/27/2010.
5. Hoefer, M. M.; Boneberg, E.-M.; Grotegut, S.; Kusch, J.; Illges,
H.: Possible tetramerisation of the proteasome maturation factor
POMP/proteassemblin/hUmp1 and its subcellular localisation. Int.
J. Biol. Macromol. 38: 259-267, 2006.
6. Witt, E.; Zantopf, D.; Schmidt, M.; Kraft, R.; Kloetzel, P.-M.;
Kruger, E.: Characterisation of the newly identified human Ump1 homologue
POMP and analysis of LMP7(beta-5i) incorporation into 20 S proteasomes. J.
Molec. Biol. 301: 1-9, 2000.
*FIELD* CN
Ada Hamosh - updated: 4/30/2010
Marla J. F. O'Neill - updated: 4/28/2010
*FIELD* CD
Patricia A. Hartz: 4/27/2010
*FIELD* ED
carol: 05/23/2012
terry: 12/6/2010
mgross: 4/30/2010
terry: 4/30/2010
carol: 4/28/2010
mgross: 4/27/2010