NUP42_HUMAN
ID NUP42_HUMAN Reviewed; 423 AA.
AC O15504; A4D143; B4DP42; Q49AE7; Q9BS49;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Nucleoporin NUP42 {ECO:0000305};
DE AltName: Full=NLP-1;
DE AltName: Full=NUP42 homolog;
DE AltName: Full=Nucleoporin hCG1;
DE AltName: Full=Nucleoporin-42 {ECO:0000312|HGNC:HGNC:17010};
DE AltName: Full=Nucleoporin-like protein 2;
GN Name=NUP42 {ECO:0000312|HGNC:HGNC:17010}; Synonyms=CG1, NUPL2;
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] (ISOFORM 1).
RX PubMed=9450185;
RA Van Laer L., Van Camp G., van Zuylen D., Green E.D., Verstreken M.,
RA Schatteman I., Van de Heyning P., Balemans W., Coucke P., Greinwald J.H.,
RA Smith R.J.H., Huizing E., Willems P.;
RT "Refined mapping of a gene for autosomal dominant progressive sensorineural
RT hearing loss (DFNA5) to a 2-cM region, and exclusion of a candidate gene
RT that is expressed in the cochlea.";
RL Eur. J. Hum. Genet. 5:397-405(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
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=12690205; DOI=10.1126/science.1083423;
RA Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K.,
RA Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R.,
RA Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A.,
RA Kanematsu E., Gentles S., Christopoulos C.C., Choufani S., Kwasnicka D.,
RA Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S.,
RA Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R.,
RA Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N.,
RA Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E.,
RA Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R.,
RA Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T.,
RA Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W.,
RA Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A.,
RA Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X.,
RA Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E.,
RA Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H.,
RA Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J.,
RA Adams M.D., Tsui L.-C.;
RT "Human chromosome 7: DNA sequence and biology.";
RL Science 300:767-772(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC TISSUE=Testis, and Urinary bladder;
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 INTERACTION WITH NXF1.
RX PubMed=10228171; DOI=10.1093/emboj/18.9.2593;
RA Katahira J., Straesser K., Podtelejnikov A., Mann M., Jung J.U., Hurt E.;
RT "The Mex67p-mediated nuclear mRNA export pathway is conserved from yeast to
RT human.";
RL EMBO J. 18:2593-2609(1999).
RN [7]
RP FUNCTION.
RX PubMed=10610322; DOI=10.1093/emboj/18.20.5761;
RA Strahm Y., Fahrenkrog B., Zenklusen D., Rychner E., Kantor J., Rosbach M.,
RA Stutz F.;
RT "The RNA export factor Gle1p is located on the cytoplasmic fibrils of the
RT NPC and physically interacts with the FG-nucleoporin Rip1p, the DEAD-box
RT protein Rat8p/Dbp5p and a new protein Ymr255p.";
RL EMBO J. 18:5761-5777(1999).
RN [8]
RP SUBCELLULAR LOCATION, GLYCOSYLATION, TISSUE SPECIFICITY, AND INTERACTION
RP WITH XPO1 AND HIV-1 VIRUS REV PROTEIN.
RX PubMed=10358091; DOI=10.1074/jbc.274.24.17309;
RA Farjot G., Sergeant A., Mikaelian I.;
RT "A new nucleoporin-like protein interacts with both HIV-1 Rev nuclear
RT export signal and CRM-1.";
RL J. Biol. Chem. 274:17309-17317(1999).
RN [9]
RP SUBCELLULAR LOCATION, INTERACTION WITH HIV-1 VIRUS VPR PROTEIN, AND
RP FUNCTION (MICROBIAL INFECTION).
RX PubMed=12228227; DOI=10.1074/jbc.m207439200;
RA Le Rouzic E., Mousnier A., Rustum C., Stutz F., Hallberg E., Dargemont C.,
RA Benichou S.;
RT "Docking of HIV-1 Vpr to the nuclear envelope is mediated by the
RT interaction with the nucleoporin hCG1.";
RL J. Biol. Chem. 277:45091-45098(2002).
RN [10]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH GLE1.
RX PubMed=16000379; DOI=10.1091/mbc.e04-11-0998;
RA Kendirgi F., Rexer D.J., Alcazar-Roman A.R., Onishko H.M., Wente S.R.;
RT "Interaction between the shuttling mRNA export factor Gle1 and the
RT nucleoporin hCG1: a conserved mechanism in the export of Hsp70 mRNA.";
RL Mol. Biol. Cell 16:4304-4315(2005).
RN [11]
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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-106, AND IDENTIFICATION BY
RP 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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-106, AND IDENTIFICATION BY
RP 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: Required for the export of mRNAs containing poly(A) tails
CC from the nucleus into the cytoplasm. {ECO:0000269|PubMed:10610322,
CC ECO:0000269|PubMed:16000379}.
CC -!- FUNCTION: (Microbial infection) In case of infection by HIV-1, it may
CC participate in the docking of viral Vpr at the nuclear envelope.
CC {ECO:0000269|PubMed:12228227}.
CC -!- SUBUNIT: Probable component of the nuclear pore complex (NPC).
CC Interacts with nuclear export protein NXF1 (PubMed:10228171). Interacts
CC with GLE1. Able to form a heterotrimer with NUP155 and GLE1 in vitro
CC (PubMed:16000379). Interacts with XPO1 (PubMed:10358091).
CC {ECO:0000269|PubMed:10228171, ECO:0000269|PubMed:10358091,
CC ECO:0000269|PubMed:16000379}.
CC -!- SUBUNIT: (Microbial infection) Interacts with the HIV-1 virus proteins
CC Rev and Vpr. The interaction with HIV-1 Rev, a protein that mediates
CC nuclear export of unspliced viral RNAs, suggests that its function may
CC be bypassed by the HIV-1 virus. {ECO:0000269|PubMed:10358091,
CC ECO:0000269|PubMed:12228227}.
CC -!- INTERACTION:
CC O15504-2; O76011: KRT34; NbExp=3; IntAct=EBI-14488689, EBI-1047093;
CC -!- SUBCELLULAR LOCATION: Nucleus, nuclear pore complex
CC {ECO:0000269|PubMed:12228227, ECO:0000269|PubMed:16000379}. Nucleus
CC membrane {ECO:0000269|PubMed:12228227, ECO:0000269|PubMed:16000379};
CC Peripheral membrane protein; Cytoplasmic side
CC {ECO:0000269|PubMed:12228227}. Note=Excluded from the nucleolus.
CC {ECO:0000269|PubMed:10358091}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=O15504-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O15504-2; Sequence=VSP_016481, VSP_016482;
CC Name=3;
CC IsoId=O15504-3; Sequence=VSP_016480;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC {ECO:0000269|PubMed:10358091}.
CC -!- DOMAIN: The FG repeats are interaction sites for karyopherins
CC (importins, exportins) and form probably an affinity gradient, guiding
CC the transport proteins unidirectionally with their cargo through the
CC NPC. {ECO:0000250}.
CC -!- PTM: O-glycosylated. {ECO:0000269|PubMed:10358091}.
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DR EMBL; U97198; AAC33794.1; -; mRNA.
DR EMBL; BT007409; AAP36077.1; -; mRNA.
DR EMBL; AK298183; BAG60454.1; -; mRNA.
DR EMBL; CH236948; EAL24260.1; -; Genomic_DNA.
DR EMBL; BC005327; AAH05327.1; -; mRNA.
DR EMBL; BC039333; AAH39333.1; -; mRNA.
DR CCDS; CCDS5379.1; -. [O15504-1]
DR RefSeq; NP_031368.1; NM_007342.2. [O15504-1]
DR PDB; 6B4F; X-ray; 2.81 A; C/D=381-423.
DR PDB; 6B4I; X-ray; 3.62 A; C/D=381-423.
DR PDB; 6B4J; X-ray; 3.40 A; C/D=376-422.
DR PDBsum; 6B4F; -.
DR PDBsum; 6B4I; -.
DR PDBsum; 6B4J; -.
DR AlphaFoldDB; O15504; -.
DR SMR; O15504; -.
DR BioGRID; 116278; 146.
DR ComplexPortal; CPX-873; Nuclear pore complex.
DR CORUM; O15504; -.
DR IntAct; O15504; 25.
DR MINT; O15504; -.
DR STRING; 9606.ENSP00000258742; -.
DR TCDB; 1.I.1.1.3; the nuclear pore complex (npc) family.
DR GlyGen; O15504; 3 sites, 1 O-linked glycan (3 sites).
DR iPTMnet; O15504; -.
DR PhosphoSitePlus; O15504; -.
DR SwissPalm; O15504; -.
DR BioMuta; NUPL2; -.
DR EPD; O15504; -.
DR jPOST; O15504; -.
DR MassIVE; O15504; -.
DR MaxQB; O15504; -.
DR PaxDb; O15504; -.
DR PeptideAtlas; O15504; -.
DR PRIDE; O15504; -.
DR ProteomicsDB; 48700; -. [O15504-1]
DR ProteomicsDB; 48701; -. [O15504-2]
DR ProteomicsDB; 48702; -. [O15504-3]
DR Antibodypedia; 44074; 129 antibodies from 21 providers.
DR DNASU; 11097; -.
DR Ensembl; ENST00000258742.10; ENSP00000258742.5; ENSG00000136243.18. [O15504-1]
DR Ensembl; ENST00000438012.5; ENSP00000415511.1; ENSG00000136243.18. [O15504-2]
DR GeneID; 11097; -.
DR KEGG; hsa:11097; -.
DR MANE-Select; ENST00000258742.10; ENSP00000258742.5; NM_007342.3; NP_031368.1.
DR UCSC; uc003svu.4; human. [O15504-1]
DR CTD; 11097; -.
DR DisGeNET; 11097; -.
DR GeneCards; NUP42; -.
DR HGNC; HGNC:17010; NUP42.
DR HPA; ENSG00000136243; Low tissue specificity.
DR neXtProt; NX_O15504; -.
DR OpenTargets; ENSG00000136243; -.
DR PharmGKB; PA134990469; -.
DR VEuPathDB; HostDB:ENSG00000136243; -.
DR eggNOG; ENOG502R2TD; Eukaryota.
DR GeneTree; ENSGT00390000000118; -.
DR HOGENOM; CLU_048441_0_0_1; -.
DR InParanoid; O15504; -.
DR OMA; FEAKKFT; -.
DR OrthoDB; 1562631at2759; -.
DR PhylomeDB; O15504; -.
DR TreeFam; TF106503; -.
DR PathwayCommons; O15504; -.
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; O15504; -.
DR SIGNOR; O15504; -.
DR BioGRID-ORCS; 11097; 59 hits in 1083 CRISPR screens.
DR ChiTaRS; NUPL2; human.
DR GeneWiki; NUPL2; -.
DR GenomeRNAi; 11097; -.
DR Pharos; O15504; Tbio.
DR PRO; PR:O15504; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; O15504; protein.
DR Bgee; ENSG00000136243; Expressed in cerebellar hemisphere and 186 other tissues.
DR ExpressionAtlas; O15504; baseline and differential.
DR Genevisible; O15504; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005635; C:nuclear envelope; IDA:ComplexPortal.
DR GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005643; C:nuclear pore; IC:ComplexPortal.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0005049; F:nuclear export signal receptor activity; IDA:GO_Central.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR GO; GO:0006913; P:nucleocytoplasmic transport; IC:ComplexPortal.
DR GO; GO:0006611; P:protein export from nucleus; IGI:GO_Central.
DR InterPro; IPR000571; Znf_CCCH.
DR SMART; SM00356; ZnF_C3H1; 1.
DR PROSITE; PS50103; ZF_C3H1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Glycoprotein; Membrane; Metal-binding;
KW mRNA transport; Nuclear pore complex; Nucleus; Phosphoprotein;
KW Protein transport; Reference proteome; Repeat; Translocation; Transport;
KW Zinc; Zinc-finger.
FT CHAIN 1..423
FT /note="Nucleoporin NUP42"
FT /id="PRO_0000204895"
FT REPEAT 14..15
FT /note="FG 1"
FT REPEAT 95..96
FT /note="FG 2"
FT REPEAT 218..219
FT /note="FG 3"
FT REPEAT 220..221
FT /note="FG 4"
FT REPEAT 265..266
FT /note="FG 5"
FT REPEAT 271..272
FT /note="FG 6"
FT REPEAT 288..289
FT /note="FG 7"
FT REPEAT 290..291
FT /note="FG 8"
FT REPEAT 311..312
FT /note="FG 9"
FT REPEAT 336..337
FT /note="FG 10"
FT REPEAT 345..346
FT /note="FG 11"
FT REPEAT 364..365
FT /note="FG 12"
FT ZN_FING 1..25
FT /note="C3H1-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT REGION 24..85
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 94..170
FT /note="Interaction with HIV-1 Vpr"
FT REGION 365..423
FT /note="Interaction with GLE1"
FT /evidence="ECO:0000269|PubMed:16000379"
FT COMPBIAS 31..71
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 106
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..228
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_016480"
FT VAR_SEQ 204..224
FT /note="LSDVKDGVNQAAPAFGFGSSQ -> KCLWKIYTHLSPKIYGPDCAL (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334, ECO:0000303|Ref.2"
FT /id="VSP_016481"
FT VAR_SEQ 225..423
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334, ECO:0000303|Ref.2"
FT /id="VSP_016482"
FT VARIANT 391
FT /note="D -> N (in dbSNP:rs13243961)"
FT /id="VAR_050572"
FT VARIANT 392
FT /note="K -> N (in dbSNP:rs34902971)"
FT /id="VAR_050573"
FT HELIX 395..402
FT /evidence="ECO:0007829|PDB:6B4F"
FT STRAND 403..405
FT /evidence="ECO:0007829|PDB:6B4F"
FT HELIX 418..420
FT /evidence="ECO:0007829|PDB:6B4F"
SQ SEQUENCE 423 AA; 44872 MW; 6F8B95073312E999 CRC64;
MAICQFFLQG RCRFGDRCWN EHPGARGAGG GRQQPQQQPS GNNRRGWNTT SQRYSNVIQP
SSFSKSTPWG GSRDQEKPYF SSFDSGASTN RKEGFGLSEN PFASLSPDEQ KDEKKLLEGI
VKDMEVWESS GQWMFSVYSP VKKKPNISGF TDISPEELRL EYHNFLTSNN LQSYLNSVQR
LINQWRNRVN ELKSLNISTK VALLSDVKDG VNQAAPAFGF GSSQAATFMS PGFPVNNSSS
DNAQNFSFKT NSGFAAASSG SPAGFGSSPA FGAAASTSSG ISTSAPAFGF GKPEVTSAAS
FSFKSPAASS FGSPGFSGLP ASLATGPVRA PVAPAFGGGS SVAGFGSPGS HSHTAFSKPS
SDTFGNSSIS TSLSASSSII ATDNVLFTPR DKLTVEELEQ FQSKKFTLGK IPLKPPPLEL
LNV
