BASP1_HUMAN
ID BASP1_HUMAN Reviewed; 227 AA.
AC P80723; B4DJA8; D3DTD5; O43596; Q5U0S0; Q9BWA5;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 184.
DE RecName: Full=Brain acid soluble protein 1;
DE AltName: Full=22 kDa neuronal tissue-enriched acidic protein;
DE AltName: Full=Neuronal axonal membrane protein NAP-22;
GN Name=BASP1; Synonyms=NAP22;
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=9749536;
RA Park S., Kim Y.-I., Kim B., Seong C., Oh Y., Baek K., Yoon J.;
RT "Characterization of bovine and human cDNAs encoding NAP-22 (22 kDa
RT neuronal tissue-enriched acidic protein) homologs.";
RL Mol. Cells 8:471-477(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 2).
RC TISSUE=Subthalamic nucleus;
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].
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Lung;
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 PROTEIN SEQUENCE OF 2-227, MYRISTOYLATION AT GLY-2, AND MASS SPECTROMETRY.
RC TISSUE=Brain;
RX PubMed=9310187; DOI=10.1016/s0300-9084(97)80032-6;
RA Mosevitsky M.I., Capony J.-P., Skladchikova G.Y.U., Novitskaya V.A.,
RA Plekhanov A.Y.U., Zakharov V.V.;
RT "The BASP1 family of myristoylated proteins abundant in axonal termini.
RT Primary structure analysis and physico-chemical properties.";
RL Biochimie 79:373-384(1997).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-36, AND IDENTIFICATION BY
RP 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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-31; THR-36; SER-164; SER-170;
RP SER-172; SER-176; THR-196 AND SER-205, AND IDENTIFICATION BY MASS
RP 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-36 AND THR-196, AND
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 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 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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-36; SER-164; SER-205 AND
RP SER-219, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
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).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-36, AND IDENTIFICATION BY
RP 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).
RN [15]
RP MYRISTOYLATION AT GLY-2, CLEAVAGE OF INITIATOR METHIONINE, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=25255805; DOI=10.1038/ncomms5919;
RA Thinon E., Serwa R.A., Broncel M., Brannigan J.A., Brassat U., Wright M.H.,
RA Heal W.P., Wilkinson A.J., Mann D.J., Tate E.W.;
RT "Global profiling of co- and post-translationally N-myristoylated proteomes
RT in human cells.";
RL Nat. Commun. 5:4919-4919(2014).
RN [16]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-163, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25114211; DOI=10.1073/pnas.1413825111;
RA Impens F., Radoshevich L., Cossart P., Ribet D.;
RT "Mapping of SUMO sites and analysis of SUMOylation changes induced by
RT external stimuli.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014).
RN [17]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [18]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-25; LYS-84 AND LYS-97, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
CC -!- INTERACTION:
CC P80723; Q99732: LITAF; NbExp=3; IntAct=EBI-358583, EBI-725647;
CC -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor. Cell projection,
CC growth cone. Note=Associated with the membranes of growth cones that
CC form the tips of elongating axons.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P80723-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P80723-2; Sequence=VSP_037994;
CC -!- TISSUE SPECIFICITY: Brain.
CC -!- MASS SPECTROMETRY: Mass=22780; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:9310187};
CC -!- SIMILARITY: Belongs to the BASP1 family. {ECO:0000305}.
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DR EMBL; AF039656; AAC67374.1; -; mRNA.
DR EMBL; BT019340; AAV38147.1; -; mRNA.
DR EMBL; BT019341; AAV38148.1; -; mRNA.
DR EMBL; AK295995; BAG58770.1; -; mRNA.
DR EMBL; CH471102; EAX08012.1; -; Genomic_DNA.
DR EMBL; CH471102; EAX08013.1; -; Genomic_DNA.
DR EMBL; BC000518; AAH00518.1; -; mRNA.
DR CCDS; CCDS3888.1; -. [P80723-1]
DR RefSeq; NP_001258535.1; NM_001271606.1. [P80723-1]
DR RefSeq; NP_006308.3; NM_006317.4. [P80723-1]
DR AlphaFoldDB; P80723; -.
DR BMRB; P80723; -.
DR BioGRID; 115680; 223.
DR IntAct; P80723; 83.
DR MINT; P80723; -.
DR STRING; 9606.ENSP00000319281; -.
DR TCDB; 1.A.71.1.1; the brain acid-soluble protein channel (basp1 channel) family.
DR GlyGen; P80723; 2 sites, 1 O-linked glycan (2 sites).
DR iPTMnet; P80723; -.
DR PhosphoSitePlus; P80723; -.
DR SwissPalm; P80723; -.
DR BioMuta; BASP1; -.
DR DMDM; 6686256; -.
DR CPTAC; CPTAC-31; -.
DR CPTAC; CPTAC-32; -.
DR EPD; P80723; -.
DR jPOST; P80723; -.
DR MassIVE; P80723; -.
DR MaxQB; P80723; -.
DR PaxDb; P80723; -.
DR PeptideAtlas; P80723; -.
DR PRIDE; P80723; -.
DR ProteomicsDB; 57688; -. [P80723-1]
DR ProteomicsDB; 57689; -. [P80723-2]
DR TopDownProteomics; P80723-1; -. [P80723-1]
DR TopDownProteomics; P80723-2; -. [P80723-2]
DR Antibodypedia; 54132; 162 antibodies from 26 providers.
DR DNASU; 10409; -.
DR Ensembl; ENST00000322611.4; ENSP00000319281.3; ENSG00000176788.9. [P80723-1]
DR Ensembl; ENST00000616743.1; ENSP00000482066.1; ENSG00000176788.9. [P80723-1]
DR GeneID; 10409; -.
DR KEGG; hsa:10409; -.
DR MANE-Select; ENST00000322611.4; ENSP00000319281.3; NM_006317.5; NP_006308.3.
DR UCSC; uc003jfx.5; human. [P80723-1]
DR CTD; 10409; -.
DR DisGeNET; 10409; -.
DR GeneCards; BASP1; -.
DR HGNC; HGNC:957; BASP1.
DR HPA; ENSG00000176788; Group enriched (brain, epididymis).
DR MIM; 605940; gene.
DR neXtProt; NX_P80723; -.
DR OpenTargets; ENSG00000176788; -.
DR PharmGKB; PA25261; -.
DR VEuPathDB; HostDB:ENSG00000176788; -.
DR eggNOG; ENOG502RXJZ; Eukaryota.
DR GeneTree; ENSGT00730000111450; -.
DR HOGENOM; CLU_093511_0_0_1; -.
DR InParanoid; P80723; -.
DR OMA; QLKRGFK; -.
DR OrthoDB; 1639554at2759; -.
DR PathwayCommons; P80723; -.
DR Reactome; R-HSA-9035034; RHOF GTPase cycle.
DR SignaLink; P80723; -.
DR BioGRID-ORCS; 10409; 29 hits in 1081 CRISPR screens.
DR ChiTaRS; BASP1; human.
DR GeneWiki; BASP1; -.
DR GenomeRNAi; 10409; -.
DR Pharos; P80723; Tbio.
DR PRO; PR:P80723; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; P80723; protein.
DR Bgee; ENSG00000176788; Expressed in orbitofrontal cortex and 203 other tissues.
DR ExpressionAtlas; P80723; baseline and differential.
DR Genevisible; P80723; HS.
DR GO; GO:0030054; C:cell junction; IDA:HPA.
DR GO; GO:0000785; C:chromatin; IEA:Ensembl.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005856; C:cytoskeleton; TAS:ProtInc.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0030426; C:growth cone; IEA:UniProtKB-SubCell.
DR GO; GO:0016363; C:nuclear matrix; IDA:UniProtKB.
DR GO; GO:0016607; C:nuclear speck; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0016605; C:PML body; IDA:UniProtKB.
DR GO; GO:0031982; C:vesicle; HDA:UniProtKB.
DR GO; GO:0019904; F:protein domain specific binding; IPI:UniProtKB.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; ISS:UniProtKB.
DR GO; GO:0003714; F:transcription corepressor activity; IMP:UniProtKB.
DR GO; GO:0060539; P:diaphragm development; ISS:UniProtKB.
DR GO; GO:0008406; P:gonad development; ISS:UniProtKB.
DR GO; GO:0060231; P:mesenchymal to epithelial transition; ISS:UniProtKB.
DR GO; GO:0072075; P:metanephric mesenchyme development; ISS:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0072112; P:podocyte differentiation; ISS:UniProtKB.
DR GO; GO:0060421; P:positive regulation of heart growth; ISS:UniProtKB.
DR GO; GO:2001076; P:positive regulation of metanephric ureteric bud development; ISS:UniProtKB.
DR GO; GO:0021762; P:substantia nigra development; HEP:UniProtKB.
DR GO; GO:0007356; P:thorax and anterior abdomen determination; ISS:UniProtKB.
DR DisProt; DP00930; -.
DR InterPro; IPR008408; BASP1.
DR PANTHER; PTHR23212; PTHR23212; 1.
DR Pfam; PF05466; BASP1; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Cell projection;
KW Direct protein sequencing; Isopeptide bond; Lipoprotein; Membrane;
KW Myristate; Phosphoprotein; Reference proteome; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:25255805,
FT ECO:0000269|PubMed:9310187"
FT CHAIN 2..227
FT /note="Brain acid soluble protein 1"
FT /id="PRO_0000142895"
FT REGION 1..227
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..102
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 165..201
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 31
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 36
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 40
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q91XV3"
FT MOD_RES 164
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 170
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 172
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 176
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 195
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q91XV3"
FT MOD_RES 196
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 205
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 219
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000269|PubMed:25255805,
FT ECO:0000269|PubMed:9310187"
FT CROSSLNK 25
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 84
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 97
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 163
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25114211"
FT VAR_SEQ 88..141
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_037994"
FT VARIANT 76
FT /note="A -> V (in dbSNP:rs3733748)"
FT /id="VAR_048396"
FT CONFLICT 45
FT /note="A -> P (in Ref. 1; AAC67374)"
FT /evidence="ECO:0000305"
FT CONFLICT 114..115
FT /note="AA -> LR (in Ref. 1; AAC67374)"
FT /evidence="ECO:0000305"
FT CONFLICT 128..132
FT /note="APAES -> GPRPR (in Ref. 1; AAC67374)"
FT /evidence="ECO:0000305"
FT CONFLICT 152
FT /note="E -> G (in Ref. 5; AAH00518)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 227 AA; 22693 MW; 56FFFCEA441062AB CRC64;
MGGKLSKKKK GYNVNDEKAK EKDKKAEGAA TEEEGTPKES EPQAAAEPAE AKEGKEKPDQ
DAEGKAEEKE GEKDAAAAKE EAPKAEPEKT EGAAEAKAEP PKAPEQEQAA PGPAAGGEAP
KAAEAAAAPA ESAAPAAGEE PSKEEGEPKK TEAPAAPAAQ ETKSDGAPAS DSKPGSSEAA
PSSKETPAAT EAPSSTPKAQ GPAASAEEPK PVEAPAANSD QTVTVKE
