ID   S10AA_HUMAN             Reviewed;          97 AA.
AC   P60903; A8K4V8; P08206; Q5T1C5;
DT   01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   04-NOV-2026, entry version 196.
DE   RecName: Full=Protein S100-A10;
DE   AltName: Full=Calpactin I light chain;
DE   AltName: Full=Calpactin-1 light chain;
DE   AltName: Full=Cellular ligand of annexin II;
DE   AltName: Full=S100 calcium-binding protein A10;
DE   AltName: Full=p10 protein;
DE   AltName: Full=p11;
GN   Name=S100A10; Synonyms=ANX2LG, CAL1L, CLP11;
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].
RX   PubMed=1831433; DOI=10.1016/0378-1119(91)90086-q;
RA   Kube E., Weber K., Gerke V.;
RT   "Primary structure of human, chicken, and Xenopus laevis p11, a cellular
RT   ligand of the Src-kinase substrate, annexin II.";
RL   Gene 102:255-259(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1533380; DOI=10.1016/0378-1119(92)90406-f;
RA   Harder T., Kube E., Gerke V.;
RT   "Cloning and characterization of the human gene encoding p11: structural
RT   similarity to other members of the S-100 gene family.";
RL   Gene 113:269-274(1992).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Keratinocyte;
RX   PubMed=1386341; DOI=10.1016/0888-7543(92)90171-n;
RA   Dooley T.P., Weiland K.L., Simon M.;
RT   "cDNA sequence of human p11 calpactin I light chain.";
RL   Genomics 13:866-868(1992).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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   [5]
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   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
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   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-23; LYS-28; LYS-37; LYS-54 AND
RP   LYS-57, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19608861; DOI=10.1126/science.1175371;
RA   Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA   Olsen J.V., Mann M.;
RT   "Lysine acetylation targets protein complexes and co-regulates major
RT   cellular functions.";
RL   Science 325:834-840(2009).
RN   [8]
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   [9]
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).
RN   [10]
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   [11]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-37, AND IDENTIFICATION BY MASS
RP   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).
RN   [12]
RP   X-RAY CRYSTALLOGRAPHY, AND SUBUNIT.
RX   PubMed=9886297; DOI=10.1038/4965;
RA   Rety S., Sopkova J., Renouard M., Osterloh D., Gerke V., Tabaries S.,
RA   Russo-Marie F., Lewit-Bentley A.;
RT   "The crystal structure of a complex of p11 with the annexin II N-terminal
RT   peptide.";
RL   Nat. Struct. Biol. 6:89-95(1999).
CC   -!- FUNCTION: Because S100A10 induces the dimerization of ANXA2/p36, it may
CC       function as a regulator of protein phosphorylation in that the ANXA2
CC       monomer is the preferred target (in vitro) of tyrosine-specific kinase.
CC   -!- SUBUNIT: Heterotetramer containing 2 light chains of S100A10/p11 and 2
CC       heavy chains of ANXA2/p36 (PubMed:9886297). Interacts with SCN10A (By
CC       similarity). {ECO:0000250|UniProtKB:P05943,
CC       ECO:0000269|PubMed:9886297}.
CC   -!- INTERACTION:
CC       P60903; Q09666: AHNAK; NbExp=2; IntAct=EBI-717048, EBI-2555881;
CC       P60903; P07355: ANXA2; NbExp=6; IntAct=EBI-717048, EBI-352622;
CC       P60903; P46092: CCR10; NbExp=5; IntAct=EBI-717048, EBI-348022;
CC       P60903; Q14527: HLTF; NbExp=2; IntAct=EBI-717048, EBI-1045161;
CC       P60903; Q8NB16-2: MLKL; NbExp=3; IntAct=EBI-717048, EBI-19046912;
CC       P60903; P60321: NANOS2; NbExp=3; IntAct=EBI-717048, EBI-10216569;
CC       P60903; P33764: S100A3; NbExp=3; IntAct=EBI-717048, EBI-1044747;
CC       P60903; Q8WXG8: S100Z; NbExp=6; IntAct=EBI-717048, EBI-12198403;
CC       P60903; Q8TD43: TRPM4; NbExp=2; IntAct=EBI-717048, EBI-11723041;
CC       P60903; O75604: USP2; NbExp=3; IntAct=EBI-717048, EBI-743272;
CC       P60903; Q8N5A5-2: ZGPAT; NbExp=3; IntAct=EBI-717048, EBI-10183064;
CC   -!- MISCELLANEOUS: Does not appear to bind calcium. Contains 2 ancestral
CC       calcium site related to EF-hand domains that have lost their ability to
CC       bind calcium.
CC   -!- SIMILARITY: Belongs to the S-100 family. {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC       Haematology;
CC       URL="https://atlasgeneticsoncology.org/gene/44145/S100A10";
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DR   EMBL; M81457; AAA58404.1; -; mRNA.
DR   EMBL; M38591; AAA58426.1; -; mRNA.
DR   EMBL; M77483; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AK291073; BAF83762.1; -; mRNA.
DR   EMBL; AL450992; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC015973; AAH15973.1; -; mRNA.
DR   EMBL; BC105786; AAI05787.1; -; mRNA.
DR   CCDS; CCDS1008.1; -.
DR   PIR; JC1139; JC1139.
DR   RefSeq; NP_002957.1; NM_002966.3.
DR   PDB; 1A4P; X-ray; 2.25 A; A/B=2-97.
DR   PDB; 1BT6; X-ray; 2.40 A; A/B=2-97.
DR   PDB; 4DRW; X-ray; 3.50 A; A/B/C/D=1-93.
DR   PDB; 4FTG; X-ray; 2.51 A; A/B=2-97.
DR   PDB; 4HRE; X-ray; 2.79 A; E/F/I/J=2-97.
DR   PDB; 4HRG; X-ray; 2.00 A; A/B=1-93.
DR   PDB; 4HRH; X-ray; 3.00 A; A/B=1-93.
DR   AlphaFoldDB; P60903; -.
DR   SMR; P60903; -.
DR   BioGRID; 112189; 137.
DR   ComplexPortal; CPX-850; AHNAK - Annexin A2 - S100-A10 complex.
DR   ComplexPortal; CPX-853; Annexin A2 - S100-A10 complex.
DR   ComplexPortal; CPX-856; SMARCA3 - Annexin A2 - S100-A10 complex.
DR   FunCoup; P60903; 239.
DR   IntAct; P60903; 65.
DR   NDEx; IQUERY-CP-S100A10; 2 NDEx IQuery Curated Pathways.
DR   STRING; 9606.ENSP00000357801; -.
DR   BindingDB; P60903; -.
DR   ChEMBL; CHEMBL1764939; -.
DR   DrugBank; DB12695; Phenethyl Isothiocyanate.
DR   TCDB; 8.A.81.1.2; the s100 calcium-binding protein (s100) family.
DR   GlyGen; P60903; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; P60903; -.
DR   MetOSite; P60903; -.
DR   PhosphoSitePlus; P60903; -.
DR   SwissPalm; P60903; -.
DR   BioMuta; S100A10; -.
DR   DMDM; 46397706; -.
DR   jPOST; P60903; -.
DR   MassIVE; P60903; -.
DR   PaxDb; 9606-ENSP00000357801; -.
DR   PeptideAtlas; P60903; -.
DR   ProteomicsDB; 57237; -.
DR   Pumba; P60903; -.
DR   TopDownProteomics; P60903; -.
DR   Antibodypedia; 1093; 575 antibodies from 43 providers.
DR   DNASU; 6281; -.
DR   Ensembl; ENST00000368809.1; ENSP00000357799.1; ENSG00000197747.10.
DR   Ensembl; ENST00000368811.8; ENSP00000357801.3; ENSG00000197747.10.
DR   Ensembl; ENST00000872056.1; ENSP00000542115.1; ENSG00000197747.10.
DR   Ensembl; ENST00000872057.1; ENSP00000542116.1; ENSG00000197747.10.
DR   Ensembl; ENST00000919940.1; ENSP00000589999.1; ENSG00000197747.10.
DR   Ensembl; ENST00000919941.1; ENSP00000590000.1; ENSG00000197747.10.
DR   Ensembl; ENST00000919942.1; ENSP00000590001.1; ENSG00000197747.10.
DR   Ensembl; ENST00000919943.1; ENSP00000590002.1; ENSG00000197747.10.
DR   GeneID; 6281; -.
DR   KEGG; hsa:6281; -.
DR   MANE-Select; ENST00000368811.8; ENSP00000357801.3; NM_002966.3; NP_002957.1.
DR   UCSC; uc001ezl.4; human.
DR   AGR; HGNC:10487; -.
DR   ClinPGx; PA34899; -.
DR   CTD; 6281; -.
DR   DisGeNET; 6281; -.
DR   GeneCards; S100A10; -.
DR   HGNC; HGNC:10487; S100A10.
DR   HPA; ENSG00000197747; Tissue enhanced (esophagus).
DR   MalaCards; S100A10; -.
DR   MIM; 114085; gene.
DR   OpenTargets; ENSG00000197747; -.
DR   VEuPathDB; HostDB:ENSG00000197747; -.
DR   eggNOG; ENOG502S6TB; Eukaryota.
DR   GeneTree; ENSGT00940000154197; -.
DR   HOGENOM; CLU_138624_2_1_1; -.
DR   InParanoid; P60903; -.
DR   OMA; ACEQCYA; -.
DR   OrthoDB; 26525at2759; -.
DR   PAN-GO; P60903; 4 GO annotations based on evolutionary models.
DR   PhylomeDB; P60903; -.
DR   PathwayCommons; P60903; -.
DR   Reactome; R-HSA-75205; Dissolution of Fibrin Clot.
DR   SignaLink; P60903; -.
DR   SIGNOR; P60903; -.
DR   Agora; ENSG00000197747; -.
DR   BioGRID-ORCS; 6281; 20 hits in 1155 CRISPR screens.
DR   ChiTaRS; S100A10; human.
DR   EvolutionaryTrace; P60903; -.
DR   GeneWiki; S100A10; -.
DR   GenomeRNAi; 6281; -.
DR   Pharos; P60903; Tbio.
DR   PRO; PR:P60903; -.
DR   Proteomes; UP000005640; Chromosome 1.
DR   RNAct; P60903; protein.
DR   Bgee; ENSG00000197747; Expressed in mucosa of sigmoid colon and 214 other cell types or tissues.
DR   GO; GO:1990665; C:AnxA2-p11 complex; IDA:UniProtKB.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR   GO; GO:0031012; C:extracellular matrix; HDA:BHF-UCL.
DR   GO; GO:0005576; C:extracellular region; HDA:BHF-UCL.
DR   GO; GO:0016363; C:nuclear matrix; NAS:ComplexPortal.
DR   GO; GO:0005886; C:plasma membrane; IDA:ComplexPortal.
DR   GO; GO:0098797; C:plasma membrane protein complex; IPI:ComplexPortal.
DR   GO; GO:0090575; C:RNA polymerase II transcription regulator complex; EXP:ComplexPortal.
DR   GO; GO:0005509; F:calcium ion binding; IBA:GO_Central.
DR   GO; GO:0048306; F:calcium-dependent protein binding; IBA:GO_Central.
DR   GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR   GO; GO:0044325; F:transmembrane transporter binding; IPI:UniProtKB.
DR   GO; GO:0001765; P:membrane raft assembly; IDA:UniProtKB.
DR   GO; GO:0042789; P:mRNA transcription by RNA polymerase II; IEA:Ensembl.
DR   GO; GO:0045921; P:positive regulation of exocytosis; NAS:ComplexPortal.
DR   GO; GO:0051894; P:positive regulation of focal adhesion assembly; IMP:UniProtKB.
DR   GO; GO:0043547; P:positive regulation of GTPase activity; IMP:UniProtKB.
DR   GO; GO:1905686; P:positive regulation of plasma membrane repair; NAS:ComplexPortal.
DR   GO; GO:0010756; P:positive regulation of plasminogen activation; IDA:ComplexPortal.
DR   GO; GO:0051496; P:positive regulation of stress fiber assembly; IMP:UniProtKB.
DR   GO; GO:1900026; P:positive regulation of substrate adhesion-dependent cell spreading; IMP:UniProtKB.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR   GO; GO:0072659; P:protein localization to plasma membrane; IDA:UniProtKB.
DR   GO; GO:0050767; P:regulation of neurogenesis; IEA:Ensembl.
DR   GO; GO:0006900; P:vesicle budding from membrane; IDA:UniProtKB.
DR   CDD; cd05024; S-100A10; 1.
DR   FunFam; 1.10.238.10:FF:000167; Protein S100-A10; 1.
DR   Gene3D; 1.10.238.10; EF-hand; 1.
DR   IDEAL; IID00813; -.
DR   InterPro; IPR011992; EF-hand-dom_pair.
DR   InterPro; IPR028476; S100-A10.
DR   InterPro; IPR001751; S100/CaBP7/8-like_CS.
DR   InterPro; IPR013787; S100_Ca-bd_sub.
DR   PANTHER; PTHR11639:SF74; PROTEIN S100-A10; 1.
DR   PANTHER; PTHR11639; S100 CALCIUM-BINDING PROTEIN; 1.
DR   Pfam; PF01023; S_100; 1.
DR   SMART; SM01394; S_100; 1.
DR   SUPFAM; SSF47473; EF-hand; 1.
DR   PROSITE; PS00303; S100_CABP; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Isopeptide bond; Proteomics identification;
KW   Reference proteome; Ubl conjugation.
FT   CHAIN           1..97
FT                   /note="Protein S100-A10"
FT                   /id="PRO_0000144002"
FT   REGION          60..71
FT                   /note="Ancestral calcium site"
FT   MOD_RES         23
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:19608861"
FT   MOD_RES         28
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:19608861"
FT   MOD_RES         37
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0007744|PubMed:19608861"
FT   MOD_RES         54
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:19608861"
FT   MOD_RES         57
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:19608861"
FT   CROSSLNK        37
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2); alternate"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   HELIX           4..20
FT                   /evidence="ECO:0007829|PDB:4HRG"
FT   HELIX           21..23
FT                   /evidence="ECO:0007829|PDB:4HRG"
FT   STRAND          24..26
FT                   /evidence="ECO:0007829|PDB:4HRE"
FT   HELIX           28..38
FT                   /evidence="ECO:0007829|PDB:4HRG"
FT   HELIX           42..45
FT                   /evidence="ECO:0007829|PDB:4HRG"
FT   HELIX           51..57
FT                   /evidence="ECO:0007829|PDB:4HRG"
FT   STRAND          59..61
FT                   /evidence="ECO:0007829|PDB:4HRG"
FT   STRAND          63..65
FT                   /evidence="ECO:0007829|PDB:1A4P"
FT   HELIX           69..90
FT                   /evidence="ECO:0007829|PDB:4HRG"
SQ   SEQUENCE   97 AA;  11203 MW;  3E8E03A6E7DD7A8D CRC64;
     MPSQMEHAME TMMFTFHKFA GDKGYLTKED LRVLMEKEFP GFLENQKDPL AVDKIMKDLD
     QCRDGKVGFQ SFFSLIAGLT IACNDYFVVH MKQKGKK
//