UB2Q1_HUMAN
ID UB2Q1_HUMAN Reviewed; 422 AA.
AC Q7Z7E8; B4DF92; Q29SN7; Q3B841; Q5I0X2; Q6IS04; Q6P7P2; Q96MV4; Q9BVX5;
AC Q9UGL6;
DT 21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Ubiquitin-conjugating enzyme E2 Q1;
DE EC=2.3.2.23;
DE AltName: Full=E2 ubiquitin-conjugating enzyme Q1;
DE AltName: Full=Protein NICE-5;
DE AltName: Full=Ubiquitin carrier protein Q1;
DE AltName: Full=Ubiquitin-protein ligase Q1;
GN Name=UBE2Q1; Synonyms=NICE5, UBE2Q; ORFNames=PRO3094;
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).
RA Altmann M.E., Schulze E., Adham I.M., Koehler M., Engel W.;
RT "Isolation and characterization of the human UBE2Q gene and its murine
RT ortholog.";
RL Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Wassler M., Sagar B., Geng Y.-J.;
RT "Cloning and characterization of galactosyl transferase-associated protein
RT (GTAP), a human ubiquitin-conjugating enzyme that regulate stem cell
RT adhesion, growth and differentiation.";
RL Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 204-422.
RC TISSUE=Cerebellum;
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=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 163-422 (ISOFORM 1).
RC TISSUE=Cervix, and Uterus;
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 [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 282-422, AND TISSUE SPECIFICITY.
RC TISSUE=Keratinocyte;
RX PubMed=11230159; DOI=10.1101/gr.114801;
RA Marenholz I., Zirra M., Fischer D.F., Backendorf C., Ziegler A.,
RA Mischke D.;
RT "Identification of human epidermal differentiation complex (EDC)-encoded
RT genes by subtractive hybridization of entire YACs to a gridded keratinocyte
RT cDNA library.";
RL Genome Res. 11:341-355(2001).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 312-386.
RC TISSUE=Fetal liver;
RA Zhang C., Yu Y., Zhang S., Wei H., Zhou G., Ouyang S., Luo L., Bi J.,
RA Liu M., He F.;
RT "Functional prediction of the coding sequences of 121 new genes deduced by
RT analysis of cDNA clones from human fetal liver.";
RL Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 352-422.
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP 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 [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [13] {ECO:0007744|PDB:2QGX}
RP X-RAY CRYSTALLOGRAPHY (2.56 ANGSTROMS) OF 247-414, AND AUTOUBIQUITINATION.
RX PubMed=22496338; DOI=10.1074/mcp.o111.013706;
RA Sheng Y., Hong J.H., Doherty R., Srikumar T., Shloush J., Avvakumov G.V.,
RA Walker J.R., Xue S., Neculai D., Wan J.W., Kim S.K., Arrowsmith C.H.,
RA Raught B., Dhe-Paganon S.;
RT "A human ubiquitin conjugating enzyme (E2)-HECT E3 ligase structure-
RT function screen.";
RL Mol. Cell. Proteomics 11:329-341(2012).
CC -!- FUNCTION: Catalyzes the covalent attachment of ubiquitin to other
CC proteins (PubMed:22496338). May be involved in hormonal homeostasis in
CC females. Involved in regulation of B4GALT1 cell surface expression,
CC B4GALT1-mediated cell adhesion to laminin and embryoid body formation
CC (By similarity). {ECO:0000250|UniProtKB:Q7TSS2,
CC ECO:0000269|PubMed:22496338}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine +
CC [E2 ubiquitin-conjugating enzyme]-L-cysteine = [E1 ubiquitin-
CC activating enzyme]-L-cysteine + S-ubiquitinyl-[E2 ubiquitin-
CC conjugating enzyme]-L-cysteine.; EC=2.3.2.23;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00388};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000255|PROSITE-ProRule:PRU00388}.
CC -!- SUBUNIT: Monomer and homodimer. Only the homodimer is linked to
CC ubiquitin through thiolester activation. Interacts (via N-terminus)
CC with B4GALT1 (via N-terminal cytoplasmic domain). The interaction is
CC direct. {ECO:0000250|UniProtKB:Q7TSS2}.
CC -!- INTERACTION:
CC Q7Z7E8; Q9UNE7: STUB1; NbExp=3; IntAct=EBI-1783287, EBI-357085;
CC Q7Z7E8-2; Q13643: FHL3; NbExp=3; IntAct=EBI-10258181, EBI-741101;
CC Q7Z7E8-2; P62879: GNB2; NbExp=3; IntAct=EBI-10258181, EBI-356942;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q7TSS2}. Cell
CC projection, filopodium {ECO:0000250|UniProtKB:Q7TSS2}. Cytoplasm,
CC cytosol {ECO:0000250|UniProtKB:Q7TSS2}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q7Z7E8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q7Z7E8-2; Sequence=VSP_017296;
CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:11230159}.
CC -!- PTM: Autoubiquitinated in vitro in the presence of NEDD4L.
CC {ECO:0000269|PubMed:22496338}.
CC -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
CC {ECO:0000255|PROSITE-ProRule:PRU00388}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF71141.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAH61583.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAH87836.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAI07058.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAB71173.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAB65097.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AY112698; AAM60814.1; -; mRNA.
DR EMBL; AY948200; AAY23342.1; -; mRNA.
DR EMBL; AK056388; BAB71173.1; ALT_INIT; mRNA.
DR EMBL; AK293986; BAG57353.1; -; mRNA.
DR EMBL; AL592078; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471121; EAW53193.1; -; Genomic_DNA.
DR EMBL; BC000848; AAH00848.1; -; mRNA.
DR EMBL; BC015316; AAH15316.2; -; mRNA.
DR EMBL; BC061583; AAH61583.1; ALT_INIT; mRNA.
DR EMBL; BC070158; AAH70158.1; -; mRNA.
DR EMBL; BC087836; AAH87836.1; ALT_INIT; mRNA.
DR EMBL; BC107057; AAI07058.1; ALT_INIT; mRNA.
DR EMBL; AJ243666; CAB65097.1; ALT_INIT; mRNA.
DR EMBL; AF116721; AAF71141.1; ALT_INIT; mRNA.
DR EMBL; CR457219; CAG33500.1; -; mRNA.
DR CCDS; CCDS1069.1; -. [Q7Z7E8-1]
DR RefSeq; NP_060052.3; NM_017582.6. [Q7Z7E8-1]
DR PDB; 2QGX; X-ray; 2.56 A; A/B/C/D=247-414.
DR PDBsum; 2QGX; -.
DR AlphaFoldDB; Q7Z7E8; -.
DR SMR; Q7Z7E8; -.
DR BioGRID; 120732; 39.
DR IntAct; Q7Z7E8; 19.
DR MINT; Q7Z7E8; -.
DR STRING; 9606.ENSP00000292211; -.
DR GlyGen; Q7Z7E8; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q7Z7E8; -.
DR PhosphoSitePlus; Q7Z7E8; -.
DR BioMuta; UBE2Q1; -.
DR DMDM; 74750234; -.
DR EPD; Q7Z7E8; -.
DR jPOST; Q7Z7E8; -.
DR MassIVE; Q7Z7E8; -.
DR MaxQB; Q7Z7E8; -.
DR PaxDb; Q7Z7E8; -.
DR PeptideAtlas; Q7Z7E8; -.
DR PRIDE; Q7Z7E8; -.
DR ProteomicsDB; 69523; -. [Q7Z7E8-1]
DR ProteomicsDB; 69524; -. [Q7Z7E8-2]
DR Antibodypedia; 34155; 144 antibodies from 23 providers.
DR DNASU; 55585; -.
DR Ensembl; ENST00000292211.5; ENSP00000292211.4; ENSG00000160714.10. [Q7Z7E8-1]
DR GeneID; 55585; -.
DR KEGG; hsa:55585; -.
DR MANE-Select; ENST00000292211.5; ENSP00000292211.4; NM_017582.7; NP_060052.3.
DR UCSC; uc001fff.2; human. [Q7Z7E8-1]
DR CTD; 55585; -.
DR DisGeNET; 55585; -.
DR GeneCards; UBE2Q1; -.
DR HGNC; HGNC:15698; UBE2Q1.
DR HPA; ENSG00000160714; Low tissue specificity.
DR MIM; 617429; gene.
DR neXtProt; NX_Q7Z7E8; -.
DR OpenTargets; ENSG00000160714; -.
DR PharmGKB; PA38029; -.
DR VEuPathDB; HostDB:ENSG00000160714; -.
DR eggNOG; KOG0897; Eukaryota.
DR GeneTree; ENSGT00940000160166; -.
DR HOGENOM; CLU_053863_0_0_1; -.
DR InParanoid; Q7Z7E8; -.
DR OMA; NIQENYP; -.
DR OrthoDB; 1214134at2759; -.
DR PhylomeDB; Q7Z7E8; -.
DR TreeFam; TF313338; -.
DR BRENDA; 2.3.2.23; 2681.
DR PathwayCommons; Q7Z7E8; -.
DR Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR SignaLink; Q7Z7E8; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 55585; 74 hits in 1081 CRISPR screens.
DR ChiTaRS; UBE2Q1; human.
DR EvolutionaryTrace; Q7Z7E8; -.
DR GenomeRNAi; 55585; -.
DR Pharos; Q7Z7E8; Tbio.
DR PRO; PR:Q7Z7E8; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q7Z7E8; protein.
DR Bgee; ENSG00000160714; Expressed in left testis and 201 other tissues.
DR Genevisible; Q7Z7E8; HS.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0030175; C:filopodium; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0061631; F:ubiquitin conjugating enzyme activity; IBA:GO_Central.
DR GO; GO:0007566; P:embryo implantation; IEA:Ensembl.
DR GO; GO:0009566; P:fertilization; IEA:Ensembl.
DR GO; GO:0007617; P:mating behavior; IEA:Ensembl.
DR GO; GO:0070459; P:prolactin secretion; IEA:Ensembl.
DR GO; GO:0000209; P:protein polyubiquitination; IBA:GO_Central.
DR GO; GO:0061458; P:reproductive system development; IEA:Ensembl.
DR GO; GO:0001967; P:suckling behavior; IEA:Ensembl.
DR Gene3D; 3.10.110.10; -; 1.
DR IDEAL; IID00639; -.
DR InterPro; IPR000608; UBQ-conjugat_E2.
DR InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
DR Pfam; PF00179; UQ_con; 1.
DR SUPFAM; SSF54495; SSF54495; 2.
DR PROSITE; PS50127; UBC_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; ATP-binding;
KW Cell projection; Cytoplasm; Nucleotide-binding; Nucleus;
KW Reference proteome; Transferase; Ubl conjugation; Ubl conjugation pathway.
FT CHAIN 1..422
FT /note="Ubiquitin-conjugating enzyme E2 Q1"
FT /id="PRO_0000223876"
FT DOMAIN 251..415
FT /note="UBC core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
FT REGION 1..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 174..221
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 183..204
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 205..221
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 351
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895"
FT VAR_SEQ 1..169
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_017296"
FT CONFLICT 287
FT /note="N -> Y (in Ref. 7; CAB65097)"
FT /evidence="ECO:0000305"
FT HELIX 250..264
FT /evidence="ECO:0007829|PDB:2QGX"
FT HELIX 267..270
FT /evidence="ECO:0007829|PDB:2QGX"
FT STRAND 273..278
FT /evidence="ECO:0007829|PDB:2QGX"
FT HELIX 279..281
FT /evidence="ECO:0007829|PDB:2QGX"
FT STRAND 285..291
FT /evidence="ECO:0007829|PDB:2QGX"
FT HELIX 298..309
FT /evidence="ECO:0007829|PDB:2QGX"
FT STRAND 315..320
FT /evidence="ECO:0007829|PDB:2QGX"
FT TURN 325..327
FT /evidence="ECO:0007829|PDB:2QGX"
FT STRAND 331..337
FT /evidence="ECO:0007829|PDB:2QGX"
FT STRAND 339..341
FT /evidence="ECO:0007829|PDB:2QGX"
FT STRAND 348..350
FT /evidence="ECO:0007829|PDB:2QGX"
FT TURN 357..359
FT /evidence="ECO:0007829|PDB:2QGX"
FT HELIX 366..379
FT /evidence="ECO:0007829|PDB:2QGX"
FT STRAND 386..388
FT /evidence="ECO:0007829|PDB:2QGX"
FT HELIX 390..392
FT /evidence="ECO:0007829|PDB:2QGX"
FT HELIX 395..405
FT /evidence="ECO:0007829|PDB:2QGX"
SQ SEQUENCE 422 AA; 46127 MW; 106FF7E59DF65555 CRC64;
MQQPQPQGQQ QPGPGQQLGG QGAAPGAGGG PGGGPGPGPC LRRELKLLES IFHRGHERFR
IASACLDELS CEFLLAGAGG AGAGAAPGPH LPPRGSVPGD PVRIHCNITE SYPAVPPIWS
VESDDPNLAA VLERLVDIKK GNTLLLQHLK RIISDLCKLY NLPQHPDVEM LDQPLPAEQC
TQEDVSSEDE DEEMPEDTED LDHYEMKEEE PAEGKKSEDD GIGKENLAIL EKIKKNQRQD
YLNGAVSGSV QATDRLMKEL RDIYRSQSFK GGNYAVELVN DSLYDWNVKL LKVDQDSALH
NDLQILKEKE GADFILLNFS FKDNFPFDPP FVRVVSPVLS GGYVLGGGAI CMELLTKQGW
SSAYSIESVI MQISATLVKG KARVQFGANK SQYSLTRAQQ SYKSLVQIHE KNGWYTPPKE
DG
