PIP30_MOUSE
ID PIP30_MOUSE Reviewed; 254 AA.
AC Q91WE2; Q3U9X3; Q8R0C9;
DT 26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=PSME3-interacting protein {ECO:0000305};
DE AltName: Full=NEFA-interacting nuclear protein NIP30 {ECO:0000303|PubMed:26497270};
DE AltName: Full=PA28G-interacting protein {ECO:0000250|UniProtKB:Q9GZU8};
GN Name=Psme3ip1 {ECO:0000312|MGI:MGI:1919637};
GN Synonyms=Fam192a {ECO:0000312|MGI:MGI:1919637},
GN Nip30 {ECO:0000303|PubMed:26497270};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Diencephalon;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Eye, Liver, and Retina;
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 [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Heart, Liver, Lung, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [4]
RP TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, INDUCTION DURING MUSCLE ATROPHY,
RP INDUCTION BY MYOD1, AND SUBCELLULAR LOCATION.
RX PubMed=26497270; DOI=10.1016/j.gene.2015.10.046;
RA Waddell D.S., Duffin P.J., Haddock A.N., Triplett V.E., Saredy J.J.,
RA Kakareka K.M., Eldredge J.T.;
RT "Isolation, expression analysis and characterization of NEFA-interacting
RT nuclear protein 30 and RING finger and SPRY domain containing 1 in skeletal
RT muscle.";
RL Gene 576:319-332(2016).
CC -!- FUNCTION: Promotes the association of the proteasome activator complex
CC subunit PSME3 with the 20S proteasome and regulates its activity.
CC Inhibits PSME3-mediated degradation of some proteasome substrates,
CC probably by affecting their diffusion rate into the catalytic chamber
CC of the proteasome. Also inhibits the interaction of PSME3 with COIL,
CC inhibits accumulation of PSME3 in Cajal bodies and positively regulates
CC the number of Cajal bodies in the nucleus.
CC {ECO:0000250|UniProtKB:Q9GZU8}.
CC -!- SUBUNIT: Interacts (via C-terminus) with both free and 20S proteasome-
CC bound forms of the proteasome activator complex subunit PSME3/PA28G;
CC the interaction is direct. {ECO:0000250|UniProtKB:Q9GZU8}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:26497270}.
CC -!- TISSUE SPECIFICITY: Expressed in skeletal muscle.
CC {ECO:0000269|PubMed:26497270}.
CC -!- DEVELOPMENTAL STAGE: Shows relatively constant expression in both
CC proliferating myoblasts and in differentiated myotubes, when assayed in
CC C2C12 cell line (at protein level). {ECO:0000269|PubMed:26497270}.
CC -!- INDUCTION: Up-regulated in response to denervation-induced skeletal
CC muscle atrophy. Induced by MYOD1. {ECO:0000269|PubMed:26497270}.
CC -!- PTM: Phosphorylation by CK2 stabilizes the interaction with PSME3.
CC {ECO:0000250|UniProtKB:Q9GZU8}.
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DR EMBL; AK033988; BAC28539.1; -; mRNA.
DR EMBL; AK151603; BAE30543.1; -; mRNA.
DR EMBL; AK050704; BAC34387.1; -; mRNA.
DR EMBL; BC016088; AAH16088.1; -; mRNA.
DR EMBL; BC023158; AAH23158.1; -; mRNA.
DR EMBL; BC025472; AAH25472.1; -; mRNA.
DR EMBL; BC027060; AAH27060.1; -; mRNA.
DR EMBL; BC040818; AAH40818.1; -; mRNA.
DR CCDS; CCDS40439.1; -.
DR RefSeq; NP_082497.2; NM_028221.4.
DR RefSeq; XP_006530603.1; XM_006530540.2.
DR RefSeq; XP_006530604.1; XM_006530541.2.
DR RefSeq; XP_006530605.1; XM_006530542.2.
DR RefSeq; XP_011246558.1; XM_011248256.2.
DR AlphaFoldDB; Q91WE2; -.
DR SMR; Q91WE2; -.
DR BioGRID; 221800; 9.
DR STRING; 10090.ENSMUSP00000034226; -.
DR iPTMnet; Q91WE2; -.
DR PhosphoSitePlus; Q91WE2; -.
DR EPD; Q91WE2; -.
DR MaxQB; Q91WE2; -.
DR PaxDb; Q91WE2; -.
DR PeptideAtlas; Q91WE2; -.
DR PRIDE; Q91WE2; -.
DR ProteomicsDB; 275991; -.
DR Antibodypedia; 28815; 55 antibodies from 19 providers.
DR DNASU; 102122; -.
DR Ensembl; ENSMUST00000034226; ENSMUSP00000034226; ENSMUSG00000031774.
DR GeneID; 102122; -.
DR KEGG; mmu:102122; -.
DR UCSC; uc009mwn.2; mouse.
DR CTD; 80011; -.
DR MGI; MGI:1919637; Psme3ip1.
DR VEuPathDB; HostDB:ENSMUSG00000031774; -.
DR eggNOG; KOG4036; Eukaryota.
DR GeneTree; ENSGT00500000044916; -.
DR HOGENOM; CLU_081950_0_0_1; -.
DR InParanoid; Q91WE2; -.
DR OMA; VDAHKMN; -.
DR OrthoDB; 1321801at2759; -.
DR PhylomeDB; Q91WE2; -.
DR TreeFam; TF314540; -.
DR BioGRID-ORCS; 102122; 1 hit in 74 CRISPR screens.
DR ChiTaRS; Fam192a; mouse.
DR PRO; PR:Q91WE2; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q91WE2; protein.
DR Bgee; ENSMUSG00000031774; Expressed in animal zygote and 282 other tissues.
DR ExpressionAtlas; Q91WE2; baseline and differential.
DR Genevisible; Q91WE2; MM.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:1901799; P:negative regulation of proteasomal protein catabolic process; ISS:UniProtKB.
DR GO; GO:0032091; P:negative regulation of protein binding; ISS:UniProtKB.
DR InterPro; IPR039845; FAM192A.
DR InterPro; IPR019331; FAM192A/Fyv6_N.
DR PANTHER; PTHR13495; PTHR13495; 1.
DR Pfam; PF10187; FAM192A_Fyv6_N; 1.
PE 1: Evidence at protein level;
KW Acetylation; Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..254
FT /note="PSME3-interacting protein"
FT /id="PRO_0000096848"
FT REGION 22..53
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 154..198
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 201..254
FT /note="Interaction with PSME3"
FT /evidence="ECO:0000250|UniProtKB:Q9GZU8"
FT COMPBIAS 162..180
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q9GZU8"
FT MOD_RES 17
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9GZU8"
FT MOD_RES 138
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9GZU8"
FT MOD_RES 222
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9GZU8"
FT MOD_RES 228
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9GZU8"
FT CONFLICT 4
FT /note="E -> G (in Ref. 1; BAE30543)"
FT /evidence="ECO:0000305"
FT CONFLICT 98
FT /note="E -> D (in Ref. 2; AAH27060)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 254 AA; 28702 MW; 82CC62DE8ED636EC CRC64;
MDGEDDSNLV IKKRFVSEAE LDERRKRRQE EWEKVRKPED PKECPEEAYD PRSLYERLQE
QKDRKQQEYE EQFKFKNMVR GLDEDETNFL DEVSRQQELI EKQRREEELE ELKEYRSNLN
KVGISAENKE VEKKLAVKPI ETKNKFSQAK LLAGAVKHKS SESGNSVKRL KPDPDPDDKA
QEAPSCMSLG SSSLSGPPSI HCPSAAVCIG ILPGLGAYSG SSDSESSSDS EGTINATGKI
VSSIFRTNTF LEAP
