PO121_MOUSE
ID PO121_MOUSE Reviewed; 1200 AA.
AC Q8K3Z9; Q7TSH5;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 2.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Nuclear envelope pore membrane protein POM 121;
DE AltName: Full=Nucleoporin Nup121;
DE AltName: Full=Pore membrane protein of 121 kDa;
GN Name=Pom121; Synonyms=Nup121;
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 [MRNA].
RA Tassabehji M., Cunliffe P.;
RT "Identification of mouse genes mapping to the Williams syndrome critical
RT region.";
RL Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-319; SER-322; SER-325;
RP SER-408 AND SER-409, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-244; SER-319; SER-322;
RP SER-325; SER-370; SER-409; SER-412; SER-413; SER-416 AND SER-417, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Kidney, Liver, Lung, Pancreas, Spleen,
RC 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).
CC -!- FUNCTION: Essential component of the nuclear pore complex (NPC). The
CC repeat-containing domain may be involved in anchoring components of the
CC pore complex to the pore membrane. When overexpressed in cells induces
CC the formation of cytoplasmic annulate lamellae (AL) (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nuclear pore complex {ECO:0000250}.
CC Nucleus membrane {ECO:0000250}; Single-pass membrane protein
CC {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250}; Single-
CC pass membrane protein {ECO:0000250}. Note=Stably associated with the
CC NPC throughout interphase and the endoplasmic reticulum during
CC metaphase. {ECO:0000250}.
CC -!- DOMAIN: Contains F-X-F-G repeats.
CC -!- PTM: Proteolytically cleaved by caspase-3 during apoptosis.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the POM121 family. {ECO:0000305}.
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DR EMBL; AF516680; AAM64199.1; -; mRNA.
DR EMBL; BC053101; AAH53101.1; -; mRNA.
DR CCDS; CCDS51662.1; -.
DR RefSeq; NP_683734.2; NM_148932.2.
DR AlphaFoldDB; Q8K3Z9; -.
DR SMR; Q8K3Z9; -.
DR BioGRID; 223706; 1.
DR ComplexPortal; CPX-4474; Nuclear pore complex.
DR STRING; 10090.ENSMUSP00000106801; -.
DR iPTMnet; Q8K3Z9; -.
DR PhosphoSitePlus; Q8K3Z9; -.
DR SwissPalm; Q8K3Z9; -.
DR EPD; Q8K3Z9; -.
DR jPOST; Q8K3Z9; -.
DR MaxQB; Q8K3Z9; -.
DR PaxDb; Q8K3Z9; -.
DR PRIDE; Q8K3Z9; -.
DR ProteomicsDB; 289468; -.
DR Ensembl; ENSMUST00000111171; ENSMUSP00000106801; ENSMUSG00000053293.
DR GeneID; 107939; -.
DR KEGG; mmu:107939; -.
DR UCSC; uc008zyi.1; mouse.
DR CTD; 9883; -.
DR MGI; MGI:2137624; Pom121.
DR VEuPathDB; HostDB:ENSMUSG00000053293; -.
DR eggNOG; ENOG502R5GW; Eukaryota.
DR GeneTree; ENSGT00940000153253; -.
DR HOGENOM; CLU_011366_0_0_1; -.
DR InParanoid; Q8K3Z9; -.
DR OMA; MPCPQFG; -.
DR OrthoDB; 355024at2759; -.
DR PhylomeDB; Q8K3Z9; -.
DR TreeFam; TF323517; -.
DR Reactome; R-MMU-159227; Transport of the SLBP independent Mature mRNA.
DR Reactome; R-MMU-159230; Transport of the SLBP Dependant Mature mRNA.
DR Reactome; R-MMU-159231; Transport of Mature mRNA Derived from an Intronless Transcript.
DR Reactome; R-MMU-159236; Transport of Mature mRNA derived from an Intron-Containing Transcript.
DR Reactome; R-MMU-170822; Regulation of Glucokinase by Glucokinase Regulatory Protein.
DR Reactome; R-MMU-191859; snRNP Assembly.
DR Reactome; R-MMU-3108214; SUMOylation of DNA damage response and repair proteins.
DR Reactome; R-MMU-3232142; SUMOylation of ubiquitinylation proteins.
DR Reactome; R-MMU-3301854; Nuclear Pore Complex (NPC) Disassembly.
DR Reactome; R-MMU-3371453; Regulation of HSF1-mediated heat shock response.
DR Reactome; R-MMU-4085377; SUMOylation of SUMOylation proteins.
DR Reactome; R-MMU-4551638; SUMOylation of chromatin organization proteins.
DR Reactome; R-MMU-4570464; SUMOylation of RNA binding proteins.
DR Reactome; R-MMU-4615885; SUMOylation of DNA replication proteins.
DR Reactome; R-MMU-5578749; Transcriptional regulation by small RNAs.
DR Reactome; R-MMU-9615933; Postmitotic nuclear pore complex (NPC) reformation.
DR BioGRID-ORCS; 107939; 5 hits in 73 CRISPR screens.
DR ChiTaRS; Pom121; mouse.
DR PRO; PR:Q8K3Z9; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q8K3Z9; protein.
DR Bgee; ENSMUSG00000053293; Expressed in respiratory primordium and 242 other tissues.
DR ExpressionAtlas; Q8K3Z9; baseline and differential.
DR Genevisible; Q8K3Z9; MM.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005635; C:nuclear envelope; ISO:MGI.
DR GO; GO:0031965; C:nuclear membrane; ISO:MGI.
DR GO; GO:0005643; C:nuclear pore; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0008139; F:nuclear localization sequence binding; IBA:GO_Central.
DR GO; GO:0017056; F:structural constituent of nuclear pore; ISO:MGI.
DR GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR GO; GO:0006999; P:nuclear pore organization; ISO:MGI.
DR GO; GO:0006913; P:nucleocytoplasmic transport; IC:ComplexPortal.
DR GO; GO:0006606; P:protein import into nucleus; IBA:GO_Central.
DR GO; GO:0006405; P:RNA export from nucleus; IBA:GO_Central.
DR InterPro; IPR026054; Nucleoporin.
DR InterPro; IPR026090; POM121.
DR PANTHER; PTHR23193; PTHR23193; 1.
DR PANTHER; PTHR23193:SF43; PTHR23193:SF43; 1.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; Membrane; mRNA transport; Nuclear pore complex;
KW Nucleus; Phosphoprotein; Protein transport; Reference proteome; Repeat;
KW Translocation; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..1200
FT /note="Nuclear envelope pore membrane protein POM 121"
FT /id="PRO_0000204907"
FT TRANSMEM 57..77
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..56
FT /note="Cisternal side"
FT /evidence="ECO:0000255"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 76..1200
FT /note="Pore side"
FT /evidence="ECO:0000255"
FT REGION 91..167
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 177..196
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 294..328
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 345..509
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 530..627
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 640..692
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 706..744
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1075..1151
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1173..1200
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 294..322
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 364..422
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 456..482
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 563..589
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 712..742
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 531..532
FT /note="Cleavage; by caspase-3"
FT /evidence="ECO:0000250"
FT MOD_RES 83
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A8CG34"
FT MOD_RES 244
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 319
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 322
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 325
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 345
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96HA1"
FT MOD_RES 355
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P52591"
FT MOD_RES 367
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A8CG34"
FT MOD_RES 370
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 408
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355"
FT MOD_RES 409
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 412
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 413
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 416
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 417
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CONFLICT 500
FT /note="Missing (in Ref. 1; AAM64199)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1200 AA; 121022 MW; C15B5D6C204D445E CRC64;
MSPAAAAADG GERRRPPLGG REGRSRARGY GGPAGAAALG LALLGLALYL VPAAAALAWL
AVGASAAWWG LSREPRGPRA LSSFVRDARR HPRPALTASP PPAKSPVNGS LCEPRSPLGG
PDPAELLLMG SYLGKPGPPE PALRQDPRER PGRRPPARSP PPASAVQRVH HVYPALPTPL
LRPSRRPPHR DCGPLSSRFV ITPRRRYPIQ QAQYSLLGAL PTVCWNGGHK KAVLSPRNSR
MVCSPVTVRI APPDSKLFRS SMSEQILDTT LSSPSSNAPD PCAKETVLNA LKEKKKRTVA
EEDQLHLDGQ ENKRRRHDSG GSGHSAFEPL VANGVPAAFV PKPGSLKRSL ASQSSDDHLN
KRSRTSSVSS LASACTGGIP SSSRNAITSS YSSTRGISQL WKRSGPTSSP FSSPASSRSQ
TPERPAKKTR EEEPCQQSSS SPPLVTDKES PGEKVTDTTT GKQQSSWTSP PTPGSSGQRK
RKIQLLPSRR GDQLTLPPPP ELGYSITAED LDMERKASLQ WFNKVLEDKP DDASASATDG
PPSTSPPFTF TLPAVGPAAS PASLPAPSSN PLLESLKKMQ ESPAPSSSEP AEAATVAAPS
PPKTPSLLAP LVSPLAGPLA STSSDSKPAA TFLGLASASS ITPLTDSKSS GVSQAEQSVS
TPASTASSPT PKPSMLFGML SPPASSSSLA TPAPACASPM FKPIFPATPK SESDSPLPSS
SSAATTASSS TAPPTAASTT PTFKPIFDKM EPFTAMPLST PFSLKQTTAT ATTTATSAPL
FTGLGTATST VASGTAASAS KPVFGFGVTT AASTASSTMT STSQSVLFGG APPVTTSSSA
PALASIFQFG KPLAPAASAA GTSFSQPLAS STQTAASNSG FSGFGSTLTT STSAPATTSQ
PTLTFSNTVT PTFNIPFSSS AKPALPTYPG ANSQPTFGAT DGATKPALAP SFGSSFTFGN
SVASAPSAAP APATFGSAAQ PAFGGLKAAA STFGAPASTQ PAFGSTTSVF SFGSATTSGF
GAAATAATTT QTTNSGSSSS LFGSSAPSPF TFGGSAAPAG SGGFGLSATP GTSSTSGTFS
FGSGQSGTPG TTTSFGSLSQ NTLGAPSQGS PFAFSVGSTP ESKPVFGGTS TPTFGQSAPA
PGVGTTGSSL SFGASSTPAQ GFVGVGPFGS AAPSFSIGAG SKTPGARQRL QARRQHTRKK
