P121C_HUMAN
ID P121C_HUMAN Reviewed; 1229 AA.
AC A8CG34; A0A075B7F8; A0A087WY75; O75115; Q9Y2N3; Q9Y4S7;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 28-MAR-2018, sequence version 3.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Nuclear envelope pore membrane protein POM 121C;
DE AltName: Full=Nuclear pore membrane protein 121-2;
DE Short=POM121-2;
DE AltName: Full=Pore membrane protein of 121 kDa C;
GN Name=POM121C;
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 [LARGE SCALE GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Leiomyosarcoma;
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 NUCLEOTIDE SEQUENCE [MRNA] OF 1-398, IDENTIFICATION BY MASS SPECTROMETRY,
RP FUNCTION, AND SUBCELLULAR LOCATION.
RC TISSUE=Cervix;
RX PubMed=17900573; DOI=10.1016/j.febslet.2007.09.021;
RA Funakoshi T., Maeshima K., Yahata K., Sugano S., Imamoto F., Imamoto N.;
RT "Two distinct human POM121 genes: requirement for the formation of nuclear
RT pore complexes.";
RL FEBS Lett. 581:4910-4916(2007).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-370, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-322 AND SER-348, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-81 AND SER-373, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and 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).
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).
CC {ECO:0000269|PubMed:17900573}.
CC -!- INTERACTION:
CC A8CG34; Q14974: KPNB1; NbExp=2; IntAct=EBI-2880179, EBI-286758;
CC -!- SUBCELLULAR LOCATION: Nucleus, nuclear pore complex
CC {ECO:0000269|PubMed:17900573}. Nucleus membrane
CC {ECO:0000269|PubMed:17900573}; Single-pass membrane protein
CC {ECO:0000269|PubMed:17900573}. Endoplasmic reticulum membrane
CC {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. Note=Stably
CC associated with the NPC throughout interphase and the endoplasmic
CC reticulum during metaphase. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=A8CG34-1; Sequence=Displayed;
CC Name=2;
CC IsoId=A8CG34-2; Sequence=VSP_040759;
CC -!- DOMAIN: Contains F-X-F-G repeats.
CC -!- SIMILARITY: Belongs to the POM121 family. {ECO:0000305}.
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DR EMBL; AC006014; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC211429; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC082993; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AB354586; BAF80888.1; -; mRNA.
DR CCDS; CCDS47617.1; -. [A8CG34-2]
DR PIR; T12551; T12551.
DR AlphaFoldDB; A8CG34; -.
DR IntAct; A8CG34; 21.
DR MINT; A8CG34; -.
DR STRING; 9606.ENSP00000481575; -.
DR TCDB; 1.I.1.1.3; the nuclear pore complex (npc) family.
DR GlyGen; A8CG34; 30 sites, 2 O-linked glycans (30 sites).
DR iPTMnet; A8CG34; -.
DR PhosphoSitePlus; A8CG34; -.
DR SwissPalm; A8CG34; -.
DR BioMuta; POM121C; -.
DR EPD; A8CG34; -.
DR jPOST; A8CG34; -.
DR MassIVE; A8CG34; -.
DR MaxQB; A8CG34; -.
DR PaxDb; A8CG34; -.
DR PeptideAtlas; A8CG34; -.
DR PRIDE; A8CG34; -.
DR ProteomicsDB; 1822; -. [A8CG34-1]
DR ProteomicsDB; 1823; -. [A8CG34-2]
DR Antibodypedia; 74341; 7 antibodies from 3 providers.
DR DNASU; 100101267; -.
DR Ensembl; ENST00000607367.5; ENSP00000476236.2; ENSG00000272391.6. [A8CG34-1]
DR Ensembl; ENST00000615331.5; ENSP00000481575.1; ENSG00000272391.6. [A8CG34-2]
DR MANE-Select; ENST00000615331.5; ENSP00000481575.1; NM_001099415.3; NP_001092885.2. [A8CG34-2]
DR GeneCards; POM121C; -.
DR HGNC; HGNC:34005; POM121C.
DR HPA; ENSG00000272391; Low tissue specificity.
DR MIM; 615754; gene.
DR neXtProt; NX_A8CG34; -.
DR OpenTargets; ENSG00000272391; -.
DR VEuPathDB; HostDB:ENSG00000272391; -.
DR eggNOG; ENOG502R5GW; Eukaryota.
DR GeneTree; ENSGT00940000153253; -.
DR InParanoid; A8CG34; -.
DR OMA; MPCPQFG; -.
DR PhylomeDB; A8CG34; -.
DR TreeFam; TF323517; -.
DR PathwayCommons; A8CG34; -.
DR Reactome; R-HSA-1169408; ISG15 antiviral mechanism.
DR Reactome; R-HSA-159227; Transport of the SLBP independent Mature mRNA.
DR Reactome; R-HSA-159230; Transport of the SLBP Dependant Mature mRNA.
DR Reactome; R-HSA-159231; Transport of Mature mRNA Derived from an Intronless Transcript.
DR Reactome; R-HSA-159236; Transport of Mature mRNA derived from an Intron-Containing Transcript.
DR Reactome; R-HSA-165054; Rev-mediated nuclear export of HIV RNA.
DR Reactome; R-HSA-168271; Transport of Ribonucleoproteins into the Host Nucleus.
DR Reactome; R-HSA-168276; NS1 Mediated Effects on Host Pathways.
DR Reactome; R-HSA-168325; Viral Messenger RNA Synthesis.
DR Reactome; R-HSA-168333; NEP/NS2 Interacts with the Cellular Export Machinery.
DR Reactome; R-HSA-170822; Regulation of Glucokinase by Glucokinase Regulatory Protein.
DR Reactome; R-HSA-180746; Nuclear import of Rev protein.
DR Reactome; R-HSA-180910; Vpr-mediated nuclear import of PICs.
DR Reactome; R-HSA-191859; snRNP Assembly.
DR Reactome; R-HSA-3108214; SUMOylation of DNA damage response and repair proteins.
DR Reactome; R-HSA-3232142; SUMOylation of ubiquitinylation proteins.
DR Reactome; R-HSA-3301854; Nuclear Pore Complex (NPC) Disassembly.
DR Reactome; R-HSA-3371453; Regulation of HSF1-mediated heat shock response.
DR Reactome; R-HSA-4085377; SUMOylation of SUMOylation proteins.
DR Reactome; R-HSA-4551638; SUMOylation of chromatin organization proteins.
DR Reactome; R-HSA-4570464; SUMOylation of RNA binding proteins.
DR Reactome; R-HSA-4615885; SUMOylation of DNA replication proteins.
DR Reactome; R-HSA-5578749; Transcriptional regulation by small RNAs.
DR Reactome; R-HSA-5619107; Defective TPR may confer susceptibility towards thyroid papillary carcinoma (TPC).
DR Reactome; R-HSA-6784531; tRNA processing in the nucleus.
DR Reactome; R-HSA-9609690; HCMV Early Events.
DR Reactome; R-HSA-9610379; HCMV Late Events.
DR Reactome; R-HSA-9705671; SARS-CoV-2 activates/modulates innate and adaptive immune responses.
DR SignaLink; A8CG34; -.
DR BioGRID-ORCS; 100101267; 219 hits in 998 CRISPR screens.
DR ChiTaRS; POM121C; human.
DR GenomeRNAi; 100101267; -.
DR Pharos; A8CG34; Tdark.
DR PRO; PR:A8CG34; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; A8CG34; protein.
DR Bgee; ENSG00000272391; Expressed in islet of Langerhans and 99 other tissues.
DR ExpressionAtlas; A8CG34; baseline and differential.
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; TAS:Reactome.
DR GO; GO:0031965; C:nuclear membrane; IDA:HPA.
DR GO; GO:0005643; C:nuclear pore; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0008139; F:nuclear localization sequence binding; IBA:GO_Central.
DR GO; GO:0017056; F:structural constituent of nuclear pore; IBA:GO_Central.
DR GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
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 Alternative splicing; Endoplasmic reticulum; Membrane; mRNA transport;
KW Nuclear pore complex; Nucleus; Phosphoprotein; Protein transport;
KW Reference proteome; Repeat; Translocation; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..1229
FT /note="Nuclear envelope pore membrane protein POM 121C"
FT /id="PRO_0000204906"
FT TRANSMEM 41..61
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..398
FT /note="Required for targeting to the nucleus and nuclear
FT pore complex"
FT REGION 1..40
FT /note="Cisternal side"
FT /evidence="ECO:0000255"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 62..1229
FT /note="Pore side"
FT /evidence="ECO:0000255"
FT REGION 90..200
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 296..507
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 579..747
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 936..966
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1202..1229
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 296..325
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 367..425
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 426..440
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 464..484
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 656..698
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 726..747
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 81
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 322
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 328
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96HA1"
FT MOD_RES 348
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 370
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 373
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..242
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_040759"
FT VARIANT 379
FT /note="T -> A (in dbSNP:rs427206)"
FT /id="VAR_045906"
FT VARIANT 1165
FT /note="Q -> L (in dbSNP:rs365436)"
FT /id="VAR_045907"
FT CONFLICT 166
FT /note="Q -> P (in Ref. 3; BAF80888)"
FT /evidence="ECO:0000305"
FT CONFLICT 965
FT /note="T -> A (in Ref. 2; BC082993)"
FT /evidence="ECO:0000305"
FT CONFLICT 979..980
FT /note="Missing (in Ref. 2; BC082993)"
FT /evidence="ECO:0000305"
FT CONFLICT 984
FT /note="T -> A (in Ref. 2; BC082993)"
FT /evidence="ECO:0000305"
FT CONFLICT 991
FT /note="A -> P (in Ref. 2; BC082993)"
FT /evidence="ECO:0000305"
FT CONFLICT 1025
FT /note="A -> T (in Ref. 2; BC082993)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1229 AA; 125092 MW; 34B3F575435758D2 CRC64;
MSPAAAAAGA GERRRPIASV RDGRGRGCGG PAGAALLGLS LVGLLLYLVP AAAALAWLAV
GTTAAWWGLS REPRGSRPLS SFVQKARHRR TLFASPPAKS TANGNLLEPR TLLEGPDPAE
LLLMGSYLGK PGPPQPAPAP EGQDLRNRPG RRPPARPAPR STPPSQPTHR VHHFYPSLPT
PLLRPSGRPS PRDRGTLPDR FVITPRRRYP IHQTQYSCPG VLPTVCWNGY HKKAVLSPRN
SRMVCSPVTV RIAPPDRRFS RSAIPEQIIS STLSSPSSNA PDPCAKETVL SALKEKKKKR
TVEEEDQIFL DGQENKRRRH DSSGSGHSAF EPLVASGVPA SFVPKPGSLK RGLNSQSSDD
HLNKRSRSSS MSSLTGAYTS GIPSSSRNAI TSSYSSTRGI SQLWKRNGPS SSPFSSPASS
RSQTPERPAK KIREEELCHH SSSSTPLAAD KESQGEKAAD TTPRKKQNSN SQSTPGSSGQ
RKRKVQLLPS RRGEQLTLPP PPQLGYSITA EDLDLEKKAS LQWFNQALED KSDAASNSVT
ETPPTTQPSF TFTLPAAATA SPPTSLLAPS TNPLLESLKK MQTPPSLPPC PESAGAATTE
ALSPPKTPSL LPPLGLSQSG PPGLLPSPSF DSKPPTTLLG LIPAPSMVPA TDTKAPPTLQ
AETATKPQAT SAPSPAPKQS FLFGTQNTSP SSPAAPAASS ASPMFKPIFT APPKSEKEGL
TPPGPSVSAT APSSSSLPTT TSTTAPTFQP VFSSMGPPAS VPLPAPFFKQ TTTPATAPTT
TAPLFTGLAS ATSAVAPITS ASPSTDSASK PAFGFGINSV SSSSVSTTTS TATAASQPFL
FGAPQASAAS FTPAMGSIFQ FGKPPALPTT TTVTTFSQSL PTAVPTATSS SAADFSGFGS
TLATSAPATS SQPTLTFSNT STPTFNIPFG SSAKSPLPSY PGANPQPAFG AAEGQPPGAA
KPALTPSFGS SFTFGNSAAP APATAPTPAP ASTIKIVPAH VPTPIQPTFG GATHSAFGLK
ATASAFGAPA SSQPAFGGST AVFSFGAATS SGFGATTQTA SSGSSSSVFG STTPSPFTFG
GSAAPAGSGS FGINVATPGS SATTGAFSFG AGQSGSTATS TPFTGGLGQN ALGTTGQSTP
FAFNVGSTTE SKPVFGGTAT PTFGQNTPAP GVGTSGSSLS FGASSAPAQG FVGVGPFGSA
APSFSIGAGS KTPGARQRLQ ARRQHTRKK
