ID   P121A_HUMAN             Reviewed;        1249 AA.
AC   Q96HA1; A6NFS9; A8CDT4; A8K933; A8MXF9; O75115; Q96DI0; Q9H9X1; Q9Y2N3;
AC   Q9Y4S7;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   02-SEP-2008, sequence version 2.
DT   27-MAR-2024, entry version 170.
DE   RecName: Full=Nuclear envelope pore membrane protein POM 121;
DE   AltName: Full=Nuclear envelope pore membrane protein POM 121A;
DE   AltName: Full=Nucleoporin Nup121;
DE   AltName: Full=Pore membrane protein of 121 kDa;
GN   Name=POM121; Synonyms=KIAA0618, NUP121, POM121A;
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 MRNA] (ISOFORM 3).
RC   TISSUE=Brain;
RX   PubMed=9734811; DOI=10.1093/dnares/5.3.169;
RA   Ishikawa K., Nagase T., Suyama M., Miyajima N., Tanaka A., Kotani H.,
RA   Nomura N., Ohara O.;
RT   "Prediction of the coding sequences of unidentified human genes. X. The
RT   complete sequences of 100 new cDNA clones from brain which can code for
RT   large proteins in vitro.";
RL   DNA Res. 5:169-176(1998).
RN   [2]
RP   SEQUENCE REVISION.
RA   Ohara O., Suyama M., Nagase T., Ishikawa K.;
RL   Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Teratocarcinoma, and Testis;
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 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   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Lymph, and Skin;
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   NUCLEOTIDE SEQUENCE [MRNA] OF 1-285 (ISOFORM 1), IDENTIFICATION BY MASS
RP   SPECTROMETRY, 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   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1150-1249 (ISOFORM 1).
RC   TISSUE=Uterus;
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   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-351, AND IDENTIFICATION BY
RP   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   [9]
RP   IDENTIFICATION BY MASS 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   [10]
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   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-371, AND IDENTIFICATION BY
RP   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   [12]
RP   IDENTIFICATION BY 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).
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       Q96HA1; O95994: AGR2; NbExp=4; IntAct=EBI-739990, EBI-712648;
CC       Q96HA1; Q8TAP6: CEP76; NbExp=3; IntAct=EBI-739990, EBI-742887;
CC       Q96HA1; P51116: FXR2; NbExp=4; IntAct=EBI-739990, EBI-740459;
CC       Q96HA1; Q9NSC5: HOMER3; NbExp=3; IntAct=EBI-739990, EBI-748420;
CC       Q96HA1; Q6ZW49-2: PAXIP1; NbExp=3; IntAct=EBI-739990, EBI-10236271;
CC       Q96HA1; Q93062: RBPMS; NbExp=4; IntAct=EBI-739990, EBI-740322;
CC       Q96HA1; Q8IYF3: TEX11; NbExp=4; IntAct=EBI-739990, EBI-742397;
CC       Q96HA1-2; O95994: AGR2; NbExp=3; IntAct=EBI-11956563, EBI-712648;
CC       Q96HA1-2; Q10567-3: AP1B1; NbExp=3; IntAct=EBI-11956563, EBI-11978055;
CC       Q96HA1-2; P63010-2: AP2B1; NbExp=3; IntAct=EBI-11956563, EBI-11529439;
CC       Q96HA1-2; P54253: ATXN1; NbExp=3; IntAct=EBI-11956563, EBI-930964;
CC       Q96HA1-2; Q8N9W6-4: BOLL; NbExp=3; IntAct=EBI-11956563, EBI-11983447;
CC       Q96HA1-2; Q2TAC2-2: CCDC57; NbExp=3; IntAct=EBI-11956563, EBI-10961624;
CC       Q96HA1-2; P40199: CEACAM6; NbExp=3; IntAct=EBI-11956563, EBI-4314501;
CC       Q96HA1-2; Q8TAP6: CEP76; NbExp=3; IntAct=EBI-11956563, EBI-742887;
CC       Q96HA1-2; Q9Y2V7: COG6; NbExp=3; IntAct=EBI-11956563, EBI-3866319;
CC       Q96HA1-2; A1KXE4-2: FAM168B; NbExp=3; IntAct=EBI-11956563, EBI-12193763;
CC       Q96HA1-2; Q08379: GOLGA2; NbExp=3; IntAct=EBI-11956563, EBI-618309;
CC       Q96HA1-2; Q9NSC5: HOMER3; NbExp=3; IntAct=EBI-11956563, EBI-748420;
CC       Q96HA1-2; P0C870: JMJD7; NbExp=3; IntAct=EBI-11956563, EBI-9090173;
CC       Q96HA1-2; O60684: KPNA6; NbExp=3; IntAct=EBI-11956563, EBI-359923;
CC       Q96HA1-2; O60711: LPXN; NbExp=3; IntAct=EBI-11956563, EBI-744222;
CC       Q96HA1-2; Q9Y5V3: MAGED1; NbExp=3; IntAct=EBI-11956563, EBI-716006;
CC       Q96HA1-2; Q5VZ52: MORN5; NbExp=3; IntAct=EBI-11956563, EBI-12835568;
CC       Q96HA1-2; P25963: NFKBIA; NbExp=3; IntAct=EBI-11956563, EBI-307386;
CC       Q96HA1-2; Q7L8S5: OTUD6A; NbExp=3; IntAct=EBI-11956563, EBI-11960139;
CC       Q96HA1-2; Q96R06: SPAG5; NbExp=3; IntAct=EBI-11956563, EBI-413317;
CC       Q96HA1-2; P40763: STAT3; NbExp=3; IntAct=EBI-11956563, EBI-518675;
CC       Q96HA1-2; Q9UBB9: TFIP11; NbExp=3; IntAct=EBI-11956563, EBI-1105213;
CC       Q96HA1-2; Q12933: TRAF2; NbExp=3; IntAct=EBI-11956563, EBI-355744;
CC       Q96HA1-2; Q13114: TRAF3; NbExp=3; IntAct=EBI-11956563, EBI-357631;
CC       Q96HA1-2; P36406: TRIM23; NbExp=3; IntAct=EBI-11956563, EBI-740098;
CC       Q96HA1-2; P14373: TRIM27; NbExp=3; IntAct=EBI-11956563, EBI-719493;
CC       Q96HA1-2; P0CI25: TRIM49; NbExp=3; IntAct=EBI-11956563, EBI-6427421;
CC       Q96HA1-2; Q15654: TRIP6; NbExp=3; IntAct=EBI-11956563, EBI-742327;
CC       Q96HA1-2; Q9UHD9: UBQLN2; NbExp=3; IntAct=EBI-11956563, EBI-947187;
CC       Q96HA1-2; Q9H0C1: ZMYND12; NbExp=3; IntAct=EBI-11956563, EBI-12030590;
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=3;
CC       Name=1;
CC         IsoId=Q96HA1-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q96HA1-2; Sequence=VSP_035010;
CC       Name=3;
CC         IsoId=Q96HA1-3; Sequence=VSP_035010, VSP_035011;
CC   -!- DOMAIN: Contains F-X-F-G repeats.
CC   -!- SIMILARITY: Belongs to the POM121 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAA31593.2; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=BAB14097.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AB014518; BAA31593.2; ALT_INIT; mRNA.
DR   EMBL; AK022555; BAB14097.1; ALT_INIT; mRNA.
DR   EMBL; AK292548; BAF85237.1; -; mRNA.
DR   EMBL; AC005488; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC001518; AAH01518.2; -; mRNA.
DR   EMBL; BC008794; AAH08794.1; -; mRNA.
DR   EMBL; AB289621; BAF80887.1; -; mRNA.
DR   EMBL; AL080109; CAB45713.1; -; mRNA.
DR   EMBL; AL713666; CAD28472.1; -; mRNA.
DR   CCDS; CCDS5542.1; -. [Q96HA1-2]
DR   CCDS; CCDS59059.1; -. [Q96HA1-3]
DR   CCDS; CCDS94112.1; -. [Q96HA1-1]
DR   RefSeq; NP_001244119.1; NM_001257190.2. [Q96HA1-3]
DR   RefSeq; NP_742017.1; NM_172020.4. [Q96HA1-2]
DR   RefSeq; XP_005250783.1; XM_005250726.3.
DR   RefSeq; XP_006716259.1; XM_006716196.3.
DR   RefSeq; XP_016868342.1; XM_017012853.1.
DR   RefSeq; XP_016868343.1; XM_017012854.1.
DR   PDB; 5T6W; X-ray; 1.90 A; C=418-427.
DR   PDBsum; 5T6W; -.
DR   AlphaFoldDB; Q96HA1; -.
DR   SMR; Q96HA1; -.
DR   BioGRID; 115214; 199.
DR   ComplexPortal; CPX-873; Nuclear pore complex.
DR   IntAct; Q96HA1; 79.
DR   MINT; Q96HA1; -.
DR   STRING; 9606.ENSP00000378687; -.
DR   TCDB; 1.I.1.1.3; the nuclear pore complex (npc) family.
DR   GlyConnect; 2909; 1 O-GlcNAc glycan (3 sites).
DR   GlyCosmos; Q96HA1; 26 sites, 1 glycan.
DR   GlyGen; Q96HA1; 24 sites, 1 O-linked glycan (24 sites).
DR   iPTMnet; Q96HA1; -.
DR   PhosphoSitePlus; Q96HA1; -.
DR   SwissPalm; Q96HA1; -.
DR   BioMuta; POM121; -.
DR   DMDM; 205829302; -.
DR   EPD; Q96HA1; -.
DR   jPOST; Q96HA1; -.
DR   MassIVE; Q96HA1; -.
DR   MaxQB; Q96HA1; -.
DR   PaxDb; 9606-ENSP00000378687; -.
DR   PeptideAtlas; Q96HA1; -.
DR   ProteomicsDB; 2321; -.
DR   ProteomicsDB; 76715; -. [Q96HA1-1]
DR   ProteomicsDB; 76716; -. [Q96HA1-2]
DR   ProteomicsDB; 76717; -. [Q96HA1-3]
DR   Pumba; Q96HA1; -.
DR   Antibodypedia; 53550; 85 antibodies from 23 providers.
DR   DNASU; 9883; -.
DR   Ensembl; ENST00000395270.5; ENSP00000378687.1; ENSG00000196313.13. [Q96HA1-3]
DR   Ensembl; ENST00000434423.5; ENSP00000405562.2; ENSG00000196313.13. [Q96HA1-1]
DR   Ensembl; ENST00000627934.3; ENSP00000486504.1; ENSG00000196313.13. [Q96HA1-2]
DR   GeneID; 9883; -.
DR   KEGG; hsa:9883; -.
DR   MANE-Select; ENST00000434423.5; ENSP00000405562.2; NM_001387691.1; NP_001374620.1.
DR   UCSC; uc003twk.3; human. [Q96HA1-1]
DR   AGR; HGNC:19702; -.
DR   CTD; 9883; -.
DR   DisGeNET; 9883; -.
DR   GeneCards; POM121; -.
DR   HGNC; HGNC:19702; POM121.
DR   HPA; ENSG00000196313; Low tissue specificity.
DR   MIM; 615753; gene.
DR   neXtProt; NX_Q96HA1; -.
DR   OpenTargets; ENSG00000196313; -.
DR   PharmGKB; PA134987951; -.
DR   VEuPathDB; HostDB:ENSG00000196313; -.
DR   eggNOG; ENOG502R5GW; Eukaryota.
DR   GeneTree; ENSGT00940000153253; -.
DR   HOGENOM; CLU_011366_0_0_1; -.
DR   InParanoid; Q96HA1; -.
DR   OMA; CAREACI; -.
DR   OrthoDB; 3094378at2759; -.
DR   PhylomeDB; Q96HA1; -.
DR   TreeFam; TF323517; -.
DR   PathwayCommons; Q96HA1; -.
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-9615933; Postmitotic nuclear pore complex (NPC) reformation.
DR   Reactome; R-HSA-9705671; SARS-CoV-2 activates/modulates innate and adaptive immune responses.
DR   SignaLink; Q96HA1; -.
DR   SIGNOR; Q96HA1; -.
DR   BioGRID-ORCS; 9883; 49 hits in 1118 CRISPR screens.
DR   ChiTaRS; POM121; human.
DR   GeneWiki; POM121; -.
DR   GenomeRNAi; 9883; -.
DR   Pharos; Q96HA1; Tbio.
DR   PRO; PR:Q96HA1; -.
DR   Proteomes; UP000005640; Chromosome 7.
DR   RNAct; Q96HA1; Protein.
DR   Bgee; ENSG00000196313; Expressed in granulocyte and 136 other cell types or tissues.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005635; C:nuclear envelope; IDA:ComplexPortal.
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:0006913; P:nucleocytoplasmic transport; NAS: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   PANTHER; PTHR23193:SF5; NUCLEAR ENVELOPE PORE MEMBRANE PROTEIN POM 121; 1.
DR   PANTHER; PTHR23193; NUCLEAR PORE COMPLEX PROTEIN NUP; 1.
DR   Pfam; PF15229; POM121; 1.
DR   Genevisible; Q96HA1; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Endoplasmic reticulum; Membrane;
KW   mRNA transport; Nuclear pore complex; Nucleus; Phosphoprotein;
KW   Protein transport; Reference proteome; Repeat; Translocation;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..1249
FT                   /note="Nuclear envelope pore membrane protein POM 121"
FT                   /id="PRO_0000346773"
FT   TRANSMEM        35..55
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          1..285
FT                   /note="Required for targeting to the nucleus and nuclear
FT                   pore complex"
FT   REGION          1..34
FT                   /note="Cisternal side"
FT                   /evidence="ECO:0000255"
FT   REGION          1..27
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          56..1249
FT                   /note="Pore side"
FT                   /evidence="ECO:0000255"
FT   REGION          136..220
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          319..530
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          602..776
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          959..986
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1226..1249
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        168..193
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        319..348
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        390..448
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        449..463
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        487..507
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        679..718
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        751..776
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         94
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:A8CG34"
FT   MOD_RES         345
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:A8CG34"
FT   MOD_RES         351
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648"
FT   MOD_RES         371
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21406692"
FT   MOD_RES         393
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:A8CG34"
FT   MOD_RES         396
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:A8CG34"
FT   VAR_SEQ         1..265
FT                   /note="Missing (in isoform 2 and isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:14702039,
FT                   ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:9734811"
FT                   /id="VSP_035010"
FT   VAR_SEQ         1219..1249
FT                   /note="SAALSFSIGAGSKTPGARQRLQARRQHTRKK -> NTFAHQQEHSPRKGPNN
FT                   LSKRKLLPAVRAQGLPRRGQASSFPTRKE (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:9734811"
FT                   /id="VSP_035011"
FT   VARIANT         1215
FT                   /note="A -> G (in dbSNP:rs3177261)"
FT                   /id="VAR_045905"
FT   CONFLICT        689
FT                   /note="K -> E (in Ref. 3; BAF85237)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        904
FT                   /note="H -> P (in Ref. 3; BAB14097)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        971
FT                   /note="A -> T (in Ref. 3; BAB14097)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1021
FT                   /note="Y -> H (in Ref. 3; BAB14097)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1113
FT                   /note="I -> T (in Ref. 3; BAF85237)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        Q96HA1-3:985
FT                   /note="L -> P (in Ref. 1; BAA31593)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1249 AA;  127720 MW;  EDBA86CA5D658F61 CRC64;
     MSPAAAAAGA GERRRPIASV RDGRGRGCGG PARAVLLGLS LVGLLLYLVP AAAALAWLTV
     GATAAWWGLS REPRGSRPLS SFVRKARHRR PLSSFVRKAR HRRTLFASPL AKSTANGNLL
     EPRTLLEGPD PAELLLMGSY LGKPGPPQPA AAPEGQDLRD RPGRRPPARP APRSPPPRSP
     PPRSPPPSPP THRAHHVYPS LPTPLLRPSR RPSPRDCGTL PNRFVITPRR RYPIHQAQYS
     CLGVLPTVCW NGYHKKAVLS PRNSRMVCSP VTVRIAPPDR RFSRSAIPEQ IISSTLSSPS
     SNAPDPCAKE TVLSALKEKE KKRTVEEEDQ IFLDGQENKR RRHDSSGSGH SAFEPLVANG
     VPASFVPKPG SLKRGLNSQS SDDHLNKRSR SSSMSSLTGA YASGIPSSSR NAITSSYSST
     RGISQLWKRN GPSSSPFSSP ASSRSQTPER PAKKIREEEL CHHSSSSTPL AADRESQGEK
     AADTTPRKKQ NSNSQSTPGS SGQRKRKVQL LPSRRGEQLT LPPPPQLGYS ITAEDLDLEK
     KASLQWFNQA LEDKSDAASN SVTETPPITQ PSFTFTLPAA APASPPTSLL APSTNPLLES
     LKKMQTPPSL PPCPESAGAA TTEALSPPKT PSLLPPLGLS QSGPPGLLPS PSFDSKPPTT
     LLGLIPAPSM VPATDTKAPP TLQAETATKP QATSAPSPAP KQSFLFGTQN TSPSSPAAPA
     ASSAPPMFKP IFTAPPKSEK EGPTPPGPSV TATAPSSSSL PTTTSTTAPT FQPVFSSMGP
     PASVPLPAPF FKQTTTPATA PTTTAPLFTG LASATSAVAP ITSASPSTDS ASKPAFGFGI
     NSVSSSSVST TTSTATAASQ PFLFGAPQAS AASFTPAMGS IFQFGKPPAL PTTTTVTTFS
     QSLHTAVPTA TSSSAADFSG FGSTLATSAP ATSSQPTLTF SNTSTPTFNI PFGSSAKSPL
     PSYPGANPQP AFGAAEGQPP GAAKPALAPS FGSSFTFGNS AAPAAAPTPA PPSMIKVVPA
     YVPTPIHPIF GGATHSAFGL KATASAFGAP ASSQPAFGGS TAVFFGAATS SGFGATTQTA
     SSGSSSSVFG STTPSPFTFG GSAAPAGSGS FGINVATPGS STTTGAFSFG AGQSGSTATS
     TPFAGGLGQN ALGTTGQSTP FAFNVSSTTE SKPVFGGTAT PTFGLNTPAP GVGTSGSSLS
     FGASSAPAQG FVGVAPFGSA ALSFSIGAGS KTPGARQRLQ ARRQHTRKK
//