PIP30_HUMAN
ID PIP30_HUMAN Reviewed; 254 AA.
AC Q9GZU8;
DT 26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=PSME3-interacting protein {ECO:0000305};
DE AltName: Full=NEFA-interacting nuclear protein NIP30 {ECO:0000250|UniProtKB:Q91WE2};
DE AltName: Full=PA28G-interacting protein {ECO:0000303|PubMed:29934401};
GN Name=PSME3IP1 {ECO:0000312|HGNC:HGNC:29856};
GN Synonyms=C16orf94 {ECO:0000312|HGNC:HGNC:29856}, FAM192A,
GN NIP30 {ECO:0000250|UniProtKB:Q91WE2}, PIP30 {ECO:0000303|PubMed:29934401};
GN ORFNames=CDA018, CDA10;
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].
RA Barnikol-Watanabe S., Barnikol H.U., Kroll K., Hirschfeld G., Schwarzer C.;
RL Submitted (MAR-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Pheochromocytoma;
RA Li Y., Huang Q., Peng Y., Song H., Yu Y., Xu S., Ren S., Chen Z., Han Z.;
RT "A novel gene expressed in human pheochromocytoma.";
RL Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Ovary;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lymph node;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Colon, and Eye;
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 [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-139, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [8]
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 [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [12]
RP FUNCTION, INTERACTION WITH PSME3, SUBCELLULAR LOCATION, PHOSPHORYLATION AT
RP SER-222 AND SER-228, MUTAGENESIS OF SER-222; 223-ASP--GLU-225;
RP 229-ASP--GLU-231 AND SER-228, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=29934401; DOI=10.1073/pnas.1722299115;
RA Jonik-Nowak B., Menneteau T., Fesquet D., Baldin V., Bonne-Andrea C.,
RA Mechali F., Fabre B., Boisguerin P., de Rossi S., Henriquet C.,
RA Pugniere M., Ducoux-Petit M., Burlet-Schiltz O., Lamond A.I., Fort P.,
RA Boulon S., Bousquet M.P., Coux O.;
RT "PIP30/FAM192A is a novel regulator of the nuclear proteasome activator
RT PA28gamma.";
RL Proc. Natl. Acad. Sci. U.S.A. 115:E6477-E6486(2018).
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:0000269|PubMed:29934401}.
CC -!- SUBUNIT: Interacts (via C-terminus) with both free and 20S proteasome-
CC bound forms of the proteasome activator complex subunit PSME3; the
CC interaction is direct. {ECO:0000269|PubMed:29934401}.
CC -!- INTERACTION:
CC Q9GZU8; Q12933: TRAF2; NbExp=3; IntAct=EBI-2371956, EBI-355744;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:29934401}.
CC -!- PTM: Phosphorylation by CK2 stabilizes the interaction with PSME3.
CC {ECO:0000269|PubMed:29934401}.
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DR EMBL; AF356585; AAK43697.1; -; mRNA.
DR EMBL; AF212249; AAK14932.1; -; mRNA.
DR EMBL; AF271785; AAG44796.1; -; mRNA.
DR EMBL; AK023291; BAB14512.1; -; mRNA.
DR EMBL; AK025452; BAB15136.1; -; mRNA.
DR EMBL; AL834421; CAD39082.1; -; mRNA.
DR EMBL; BC020536; AAH20536.1; -; mRNA.
DR EMBL; BC071952; AAH71952.1; -; mRNA.
DR CCDS; CCDS42168.1; -.
DR RefSeq; NP_079222.1; NM_024946.2.
DR RefSeq; XP_005256217.1; XM_005256160.2.
DR RefSeq; XP_005256220.1; XM_005256163.2.
DR RefSeq; XP_005256221.1; XM_005256164.3.
DR RefSeq; XP_005256222.1; XM_005256165.2.
DR RefSeq; XP_011521645.1; XM_011523343.2.
DR RefSeq; XP_016879171.1; XM_017023682.1.
DR RefSeq; XP_016879172.1; XM_017023683.1.
DR RefSeq; XP_016879173.1; XM_017023684.1.
DR RefSeq; XP_016879174.1; XM_017023685.1.
DR RefSeq; XP_016879175.1; XM_017023686.1.
DR RefSeq; XP_016879176.1; XM_017023687.1.
DR RefSeq; XP_016879177.1; XM_017023688.1.
DR RefSeq; XP_016879178.1; XM_017023689.1.
DR RefSeq; XP_016879179.1; XM_017023690.1.
DR RefSeq; XP_016879180.1; XM_017023691.1.
DR RefSeq; XP_016879181.1; XM_017023692.1.
DR RefSeq; XP_016879182.1; XM_017023693.1.
DR RefSeq; XP_016879183.1; XM_017023694.1.
DR RefSeq; XP_016879184.1; XM_017023695.1.
DR RefSeq; XP_016879185.1; XM_017023696.1.
DR RefSeq; XP_016879186.1; XM_017023697.1.
DR RefSeq; XP_016879187.1; XM_017023698.1.
DR RefSeq; XP_016879188.1; XM_017023699.1.
DR RefSeq; XP_016879189.1; XM_017023700.1.
DR RefSeq; XP_016879190.1; XM_017023701.1.
DR RefSeq; XP_016879191.1; XM_017023702.1.
DR RefSeq; XP_016879192.1; XM_017023703.1.
DR RefSeq; XP_016879193.1; XM_017023704.1.
DR AlphaFoldDB; Q9GZU8; -.
DR SMR; Q9GZU8; -.
DR BioGRID; 123067; 123.
DR IntAct; Q9GZU8; 44.
DR MINT; Q9GZU8; -.
DR STRING; 9606.ENSP00000335808; -.
DR GlyGen; Q9GZU8; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9GZU8; -.
DR PhosphoSitePlus; Q9GZU8; -.
DR BioMuta; FAM192A; -.
DR DMDM; 46577123; -.
DR EPD; Q9GZU8; -.
DR jPOST; Q9GZU8; -.
DR MassIVE; Q9GZU8; -.
DR MaxQB; Q9GZU8; -.
DR PaxDb; Q9GZU8; -.
DR PeptideAtlas; Q9GZU8; -.
DR PRIDE; Q9GZU8; -.
DR ProteomicsDB; 80152; -.
DR Antibodypedia; 28815; 55 antibodies from 19 providers.
DR DNASU; 80011; -.
DR Ensembl; ENST00000309137.13; ENSP00000335808.6; ENSG00000172775.17.
DR Ensembl; ENST00000389447.9; ENSP00000374098.5; ENSG00000172775.17.
DR Ensembl; ENST00000564108.5; ENSP00000456211.1; ENSG00000172775.17.
DR Ensembl; ENST00000567439.5; ENSP00000457850.1; ENSG00000172775.17.
DR Ensembl; ENST00000569266.5; ENSP00000457740.1; ENSG00000172775.17.
DR GeneID; 80011; -.
DR KEGG; hsa:80011; -.
DR MANE-Select; ENST00000309137.13; ENSP00000335808.6; NM_024946.4; NP_079222.1.
DR UCSC; uc021tiy.1; human.
DR CTD; 80011; -.
DR GeneCards; PSME3IP1; -.
DR HGNC; HGNC:29856; PSME3IP1.
DR HPA; ENSG00000172775; Low tissue specificity.
DR MIM; 617766; gene.
DR neXtProt; NX_Q9GZU8; -.
DR OpenTargets; ENSG00000172775; -.
DR VEuPathDB; HostDB:ENSG00000172775; -.
DR eggNOG; KOG4036; Eukaryota.
DR GeneTree; ENSGT00500000044916; -.
DR InParanoid; Q9GZU8; -.
DR OMA; VDAHKMN; -.
DR OrthoDB; 1321801at2759; -.
DR PhylomeDB; Q9GZU8; -.
DR TreeFam; TF314540; -.
DR PathwayCommons; Q9GZU8; -.
DR SignaLink; Q9GZU8; -.
DR BioGRID-ORCS; 80011; 7 hits in 1078 CRISPR screens.
DR ChiTaRS; FAM192A; human.
DR GeneWiki; NIP30; -.
DR GenomeRNAi; 80011; -.
DR Pharos; Q9GZU8; Tdark.
DR PRO; PR:Q9GZU8; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; Q9GZU8; protein.
DR Bgee; ENSG00000172775; Expressed in calcaneal tendon and 192 other tissues.
DR ExpressionAtlas; Q9GZU8; baseline and differential.
DR Genevisible; Q9GZU8; HS.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:1901799; P:negative regulation of proteasomal protein catabolic process; IMP:UniProtKB.
DR GO; GO:0032091; P:negative regulation of protein binding; IMP: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_0000096847"
FT REGION 22..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 155..195
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 201..254
FT /note="Interaction with PSME3"
FT /evidence="ECO:0000269|PubMed:29934401"
FT COMPBIAS 163..183
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378"
FT MOD_RES 17
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 139
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 222
FT /note="Phosphoserine; by CK2"
FT /evidence="ECO:0000269|PubMed:29934401"
FT MOD_RES 228
FT /note="Phosphoserine; by CK2"
FT /evidence="ECO:0000269|PubMed:29934401"
FT MUTAGEN 222
FT /note="S->A: Reduces phosphorylation by CK2 and interaction
FT with PSME3; when associated with A-228."
FT /evidence="ECO:0000269|PubMed:29934401"
FT MUTAGEN 223..225
FT /note="DSE->KSK: Abolishes phosphorylation by CK2, strongly
FT reduces interaction with PSME3 and abolishes effect on
FT proteasome activity."
FT /evidence="ECO:0000269|PubMed:29934401"
FT MUTAGEN 228
FT /note="S->A: Reduces phosphorylation by CK2 and interaction
FT with PSME3; when associated with A-222."
FT /evidence="ECO:0000269|PubMed:29934401"
FT MUTAGEN 229..231
FT /note="DSE->KSK: Strongly reduces phosphorylation by CK2
FT and interaction with PSME3."
FT /evidence="ECO:0000269|PubMed:29934401"
SQ SEQUENCE 254 AA; 28912 MW; 725D2AD4AB3AD5DA CRC64;
MDGGDDGNLI IKKRFVSEAE LDERRKRRQE EWEKVRKPED PEECPEEVYD PRSLYERLQE
QKDRKQQEYE EQFKFKNMVR GLDEDETNFL DEVSRQQELI EKQRREEELK ELKEYRNNLK
KVGISQENKK EVEKKLTVKP IETKNKFSQA KLLAGAVKHK SSESGNSVKR LKPDPEPDDK
NQEPSSCKSL GNTSLSGPSI HCPSAAVCIG ILPGLGAYSG SSDSESSSDS EGTINATGKI
VSSIFRTNTF LEAP
