NEMP1_HUMAN
ID NEMP1_HUMAN Reviewed; 444 AA.
AC O14524; Q17R72; Q68DH0; Q6IQ25;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 2.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Nuclear envelope integral membrane protein 1;
DE Flags: Precursor;
GN Name=NEMP1; Synonyms=KIAA0286, TMEM194, TMEM194A;
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 1).
RC TISSUE=Brain;
RX PubMed=9179496; DOI=10.1093/dnares/4.1.53;
RA Ohara O., Nagase T., Ishikawa K., Nakajima D., Ohira M., Seki N.,
RA Nomura N.;
RT "Construction and characterization of human brain cDNA libraries suitable
RT for analysis of cDNA clones encoding relatively large proteins.";
RL DNA Res. 4:53-59(1997).
RN [2]
RP SEQUENCE REVISION.
RX PubMed=12168954; DOI=10.1093/dnares/9.3.99;
RA Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
RT "Construction of expression-ready cDNA clones for KIAA genes: manual
RT curation of 330 KIAA cDNA clones.";
RL DNA Res. 9:99-106(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Amygdala;
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] (ISOFORM 2).
RC TISSUE=Endometrial tumor;
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] (ISOFORMS 1 AND 2).
RC TISSUE=Placenta;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-368, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-368, 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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-424 AND SER-425, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
CC -!- SUBUNIT: Homooligomer. Interacts with RAN-GTP.
CC {ECO:0000250|UniProtKB:B9X187, ECO:0000250|UniProtKB:Q6ZQE4}.
CC -!- INTERACTION:
CC O14524-2; Q15848: ADIPOQ; NbExp=3; IntAct=EBI-10969203, EBI-10827839;
CC O14524-2; Q96PS8: AQP10; NbExp=3; IntAct=EBI-10969203, EBI-12820279;
CC O14524-2; P07306: ASGR1; NbExp=3; IntAct=EBI-10969203, EBI-1172335;
CC O14524-2; Q6PL45-2: BRICD5; NbExp=3; IntAct=EBI-10969203, EBI-12244618;
CC O14524-2; P01031: C5; NbExp=3; IntAct=EBI-10969203, EBI-8558308;
CC O14524-2; P60033: CD81; NbExp=3; IntAct=EBI-10969203, EBI-712921;
CC O14524-2; Q9BXN2-6: CLEC7A; NbExp=3; IntAct=EBI-10969203, EBI-11989440;
CC O14524-2; A0PK11: CLRN2; NbExp=3; IntAct=EBI-10969203, EBI-12813623;
CC O14524-2; Q8TBE1: CNIH3; NbExp=3; IntAct=EBI-10969203, EBI-12208021;
CC O14524-2; P29400-2: COL4A5; NbExp=3; IntAct=EBI-10969203, EBI-12211159;
CC O14524-2; Q07325: CXCL9; NbExp=3; IntAct=EBI-10969203, EBI-3911467;
CC O14524-2; Q96IV6: FAXDC2; NbExp=3; IntAct=EBI-10969203, EBI-12142299;
CC O14524-2; Q9NPR9: GPR108; NbExp=3; IntAct=EBI-10969203, EBI-11343451;
CC O14524-2; Q02747: GUCA2A; NbExp=3; IntAct=EBI-10969203, EBI-12244272;
CC O14524-2; Q9Y5U4: INSIG2; NbExp=3; IntAct=EBI-10969203, EBI-8503746;
CC O14524-2; P54315: PNLIPRP1; NbExp=3; IntAct=EBI-10969203, EBI-8652812;
CC O14524-2; Q5QGT7: RTP2; NbExp=3; IntAct=EBI-10969203, EBI-10244780;
CC O14524-2; Q14162: SCARF1; NbExp=3; IntAct=EBI-10969203, EBI-12056025;
CC O14524-2; Q8N6R1: SERP2; NbExp=3; IntAct=EBI-10969203, EBI-749270;
CC O14524-2; Q86Y82: STX12; NbExp=3; IntAct=EBI-10969203, EBI-2691717;
CC O14524-2; Q9Y6G1: TMEM14A; NbExp=3; IntAct=EBI-10969203, EBI-2800360;
CC O14524-2; Q8NBD8: TMEM229B; NbExp=3; IntAct=EBI-10969203, EBI-12195227;
CC O14524-2; Q69YG0: TMEM42; NbExp=3; IntAct=EBI-10969203, EBI-12038591;
CC O14524-2; Q8N661: TMEM86B; NbExp=3; IntAct=EBI-10969203, EBI-2548832;
CC O14524-2; Q5BJF2: TMEM97; NbExp=3; IntAct=EBI-10969203, EBI-12111910;
CC O14524-2; Q71RG4: TMUB2; NbExp=3; IntAct=EBI-10969203, EBI-2820477;
CC O14524-2; Q86UF1: TSPAN33; NbExp=3; IntAct=EBI-10969203, EBI-12045841;
CC O14524-2; Q5BVD1: TTMP; NbExp=3; IntAct=EBI-10969203, EBI-10243654;
CC O14524-2; O75841: UPK1B; NbExp=3; IntAct=EBI-10969203, EBI-12237619;
CC O14524-2; Q15836: VAMP3; NbExp=3; IntAct=EBI-10969203, EBI-722343;
CC -!- SUBCELLULAR LOCATION: Nucleus inner membrane
CC {ECO:0000250|UniProtKB:Q6ZQE4}; Multi-pass membrane protein
CC {ECO:0000255}; Nucleoplasmic side {ECO:0000250|UniProtKB:B9X187}.
CC Nucleus envelope {ECO:0000250|UniProtKB:Q6ZQE4}. Note=Colocalizes with
CC lamins and RAN-GTP at the nuclear envelope.
CC {ECO:0000250|UniProtKB:Q6ZQE4}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O14524-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O14524-2; Sequence=VSP_011896;
CC -!- DOMAIN: The transmembrane domains are required and sufficient for its
CC oligomerization. {ECO:0000250|UniProtKB:B9X187}.
CC -!- PTM: Phosphorylation may regulate its interaction with RAN-GTP.
CC {ECO:0000250|UniProtKB:Q6ZQE4}.
CC -!- SIMILARITY: Belongs to the NEMP family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH71597.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAA22955.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB006624; BAA22955.2; ALT_INIT; mRNA.
DR EMBL; CR749406; CAH18250.1; -; mRNA.
DR EMBL; AK294566; BAG57761.1; -; mRNA.
DR EMBL; BC071597; AAH71597.1; ALT_INIT; mRNA.
DR EMBL; BC117436; AAI17437.1; -; mRNA.
DR EMBL; BC126300; AAI26301.1; -; mRNA.
DR CCDS; CCDS31841.1; -. [O14524-2]
DR CCDS; CCDS44927.1; -. [O14524-1]
DR RefSeq; NP_001124435.1; NM_001130963.1. [O14524-1]
DR RefSeq; NP_056072.2; NM_015257.2. [O14524-2]
DR AlphaFoldDB; O14524; -.
DR BioGRID; 116898; 88.
DR IntAct; O14524; 59.
DR MINT; O14524; -.
DR STRING; 9606.ENSP00000300128; -.
DR TCDB; 9.B.368.1.1; the tmem194a (tmem194a) family.
DR GlyConnect; 1577; 1 N-Linked glycan (1 site).
DR GlyGen; O14524; 1 site, 1 N-linked glycan (1 site).
DR iPTMnet; O14524; -.
DR PhosphoSitePlus; O14524; -.
DR BioMuta; NEMP1; -.
DR EPD; O14524; -.
DR jPOST; O14524; -.
DR MassIVE; O14524; -.
DR MaxQB; O14524; -.
DR PaxDb; O14524; -.
DR PeptideAtlas; O14524; -.
DR PRIDE; O14524; -.
DR ProteomicsDB; 48069; -. [O14524-1]
DR ProteomicsDB; 48070; -. [O14524-2]
DR Antibodypedia; 16059; 29 antibodies from 15 providers.
DR DNASU; 23306; -.
DR Ensembl; ENST00000300128.9; ENSP00000300128.4; ENSG00000166881.10. [O14524-1]
DR Ensembl; ENST00000379391.7; ENSP00000368701.3; ENSG00000166881.10. [O14524-2]
DR GeneID; 23306; -.
DR KEGG; hsa:23306; -.
DR MANE-Select; ENST00000300128.9; ENSP00000300128.4; NM_001130963.2; NP_001124435.1.
DR UCSC; uc001smx.4; human. [O14524-1]
DR CTD; 23306; -.
DR DisGeNET; 23306; -.
DR GeneCards; NEMP1; -.
DR HGNC; HGNC:29001; NEMP1.
DR HPA; ENSG00000166881; Low tissue specificity.
DR MIM; 616496; gene.
DR neXtProt; NX_O14524; -.
DR OpenTargets; ENSG00000166881; -.
DR PharmGKB; PA162406290; -.
DR VEuPathDB; HostDB:ENSG00000166881; -.
DR eggNOG; KOG3817; Eukaryota.
DR GeneTree; ENSGT00390000002174; -.
DR HOGENOM; CLU_025225_0_0_1; -.
DR InParanoid; O14524; -.
DR OMA; MAGCMKM; -.
DR OrthoDB; 536946at2759; -.
DR PhylomeDB; O14524; -.
DR TreeFam; TF314831; -.
DR PathwayCommons; O14524; -.
DR SignaLink; O14524; -.
DR BioGRID-ORCS; 23306; 16 hits in 1081 CRISPR screens.
DR ChiTaRS; NEMP1; human.
DR GenomeRNAi; 23306; -.
DR Pharos; O14524; Tdark.
DR PRO; PR:O14524; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; O14524; protein.
DR Bgee; ENSG00000166881; Expressed in oocyte and 145 other tissues.
DR ExpressionAtlas; O14524; baseline and differential.
DR Genevisible; O14524; HS.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005635; C:nuclear envelope; ISS:UniProtKB.
DR GO; GO:0005637; C:nuclear inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0071763; P:nuclear membrane organization; IMP:FlyBase.
DR InterPro; IPR019358; NEMP_fam.
DR PANTHER; PTHR13598; PTHR13598; 1.
DR Pfam; PF10225; NEMP; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Glycoprotein; Membrane; Nucleus; Phosphoprotein;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..43
FT /evidence="ECO:0000255"
FT CHAIN 44..444
FT /note="Nuclear envelope integral membrane protein 1"
FT /id="PRO_0000050744"
FT TRANSMEM 161..181
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 186..206
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 216..236
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 245..265
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 289..309
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 186..297
FT /note="A; required for its colocalization with lamins at
FT the nuclear envelope"
FT /evidence="ECO:0000250|UniProtKB:Q6ZQE4"
FT REGION 336..444
FT /note="Required for nuclear localization"
FT /evidence="ECO:0000250|UniProtKB:Q6ZQE4"
FT REGION 336..405
FT /note="B; required for interaction with RAN-GTP"
FT /evidence="ECO:0000250|UniProtKB:Q6ZQE4"
FT MOD_RES 368
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:18691976"
FT MOD_RES 424
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 425
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT CARBOHYD 125
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 110..182
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:17974005"
FT /id="VSP_011896"
FT VARIANT 217
FT /note="I -> V (in dbSNP:rs17546579)"
FT /id="VAR_057817"
FT CONFLICT 442
FT /note="F -> L (in Ref. 4; CAH18250)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 444 AA; 50640 MW; F45D4D3F9B86C77B CRC64;
MAGGMKVAVS PAVGPGPWGS GVGGGGTVRL LLILSGCLVY GTAETDVNVV MLQESQVCEK
RASQQFCYTN VLIPKWHDIW TRIQIRVNSS RLVRVTQVEN EEKLKELEQF SIWNFFSSFL
KEKLNDTYVN VGLYSTKTCL KVEIIEKDTK YSVIVIRRFD PKLFLVFLLG LMLFFCGDLL
SRSQIFYYST GMTVGIVASL LIIIFILSKF MPKKSPIYVI LVGGWSFSLY LIQLVFKNLQ
EIWRCYWQYL LSYVLTVGFM SFAVCYKYGP LENERSINLL TWTLQLMGLC FMYSGIQIPH
IALAIIIIAL CTKNLEHPIQ WLYITCRKVC KGAEKPVPPR LLTEEEYRIQ GEVETRKALE
ELREFCNSPD CSAWKTVSRI QSPKRFADFV EGSSHLTPNE VSVHEQEYGL GSIIAQDEIY
EEASSEEEDS YSRCPAITQN NFLT
