HMCES_HUMAN
ID HMCES_HUMAN Reviewed; 354 AA.
AC Q96FZ2; A6NJR9; Q96G34; Q9NRP3;
DT 24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Abasic site processing protein HMCES {ECO:0000305};
DE AltName: Full=Embryonic stem cell-specific 5-hydroxymethylcytosine-binding protein {ECO:0000312|HGNC:HGNC:24446};
DE Short=ES cell-specific 5hmC-binding protein {ECO:0000312|HGNC:HGNC:24446};
DE AltName: Full=Peptidase HMCES {ECO:0000305};
DE EC=3.4.-.- {ECO:0000250|UniProtKB:Q8R1M0};
DE AltName: Full=SRAP domain-containing protein 1 {ECO:0000250|UniProtKB:Q8R1M0};
GN Name=HMCES {ECO:0000303|PubMed:30554877, ECO:0000312|HGNC:HGNC:24446};
GN Synonyms=C3orf37 {ECO:0000312|HGNC:HGNC:24446}, DC12 {ECO:0000303|Ref.1},
GN SRAPD1 {ECO:0000312|HGNC:HGNC:24446};
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].
RC TISSUE=Dendritic cell;
RA Peng Y., Li Y., Tu Y., Gu Y., Han Z., Fu G., Chen Z.;
RT "Novel genes expressed in human dendritic cells.";
RL Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, Lung, 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 [5]
RP IDENTIFICATION.
RX PubMed=23945014; DOI=10.1186/1745-6150-8-20;
RA Aravind L., Anand S., Iyer L.M.;
RT "Novel autoproteolytic and DNA-damage sensing components in the bacterial
RT SOS response and oxidized methylcytosine-induced eukaryotic DNA
RT demethylation systems.";
RL Biol. Direct 8:20-20(2013).
RN [6]
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 [7]
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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-160; SER-295 AND SER-322, AND
RP IDENTIFICATION BY 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).
RN [9]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-339, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25755297; DOI=10.1074/mcp.o114.044792;
RA Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
RA Vertegaal A.C.;
RT "System-wide analysis of SUMOylation dynamics in response to replication
RT stress reveals novel small ubiquitin-like modified target proteins and
RT acceptor lysines relevant for genome stability.";
RL Mol. Cell. Proteomics 14:1419-1434(2015).
RN [10]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-148; LYS-151; LYS-275; LYS-276;
RP LYS-306; LYS-339 AND LYS-342, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [11]
RP FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, INTERACTION WITH PCNA,
RP AND MUTAGENESIS OF CYS-2; ARG-98 AND 337-TRP-LEU-338.
RX PubMed=30554877; DOI=10.1016/j.cell.2018.10.055;
RA Mohni K.N., Wessel S.R., Zhao R., Wojciechowski A.C., Luzwick J.W.,
RA Layden H., Eichman B.F., Thompson P.S., Mehta K.P.M., Cortez D.;
RT "HMCES maintains genome integrity by shielding abasic sites in single-
RT strand DNA.";
RL Cell 176:144-153(2019).
RN [12]
RP FUNCTION.
RX PubMed=31235915; DOI=10.1038/s41594-019-0255-5;
RA Thompson P.S., Amidon K.M., Mohni K.N., Cortez D., Eichman B.F.;
RT "Protection of abasic sites during DNA replication by a stable thiazolidine
RT protein-DNA cross-link.";
RL Nat. Struct. Mol. Biol. 26:613-618(2019).
RN [13] {ECO:0007744|PDB:5KO9, ECO:0007744|PDB:6OE7, ECO:0007744|PDB:6OEA, ECO:0007744|PDB:6OEB}
RP X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) OF 2-270 IN COMPLEX WITH A DNA
RP ABASIC SITE, THIAZOLIDINE LINKAGE TO A DNA ABASIC SITE, FUNCTION, CATALYTIC
RP ACTIVITY, ACTIVE SITE, AND MUTAGENESIS OF ARG-4 AND TRP-81.
RX PubMed=31235913; DOI=10.1038/s41594-019-0246-6;
RA Halabelian L., Ravichandran M., Li Y., Zeng H., Rao A., Aravind L.,
RA Arrowsmith C.H.;
RT "Structural basis of HMCES interactions with abasic DNA and multivalent
RT substrate recognition.";
RL Nat. Struct. Mol. Biol. 26:607-612(2019).
RN [14] {ECO:0007744|PDB:6OOV}
RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 2-270 IN COMPLEX WITH
RP DOUBLE-STRANDED DNA CONTAINING AN OVERHANG, FUNCTION, AND MUTAGENESIS OF
RP CYS-2 AND ARG-212.
RX PubMed=31806351; DOI=10.1016/j.molcel.2019.10.031;
RA Shukla V., Halabelian L., Balagere S., Samaniego-Castruita D.,
RA Feldman D.E., Arrowsmith C.H., Rao A., Aravind L.;
RT "HMCES functions in the alternative end-joining pathway of the DNA DSB
RT repair during class switch recombination in B cells.";
RL Mol. Cell 0:0-0(2019).
CC -!- FUNCTION: Sensor of abasic sites in single-stranded DNA (ssDNA)
CC required to preserve genome integrity by promoting error-free repair of
CC abasic sites (PubMed:30554877, PubMed:31235915, PubMed:31235913). Acts
CC as an enzyme that recognizes and binds abasic sites in ssDNA at
CC replication forks and chemically modifies the lesion by forming a
CC covalent cross-link with DNA: forms a stable thiazolidine linkage
CC between a ring-opened abasic site and the alpha-amino and sulfhydryl
CC substituents of its N-terminal catalytic cysteine residue
CC (PubMed:30554877, PubMed:31235913). The HMCES DNA-protein cross-link is
CC then degraded by the proteasome (PubMed:30554877). Promotes error-free
CC repair of abasic sites by acting as a 'suicide' enzyme that is
CC degraded, thereby protecting abasic sites from translesion synthesis
CC (TLS) polymerases and endonucleases that are error-prone and would
CC generate mutations and double-strand breaks (PubMed:30554877). Has
CC preference for ssDNA, but can also accommodate double-stranded DNA with
CC 3' or 5' overhang (dsDNA), and dsDNA-ssDNA 3' junction
CC (PubMed:31235915, PubMed:31806351). Also involved in class switch
CC recombination (CSR) in B-cells independently of the formation of a DNA-
CC protein cross-link: acts by binding and protecting ssDNA overhangs to
CC promote DNA double-strand break repair through the microhomology-
CC mediated alternative-end-joining (Alt-EJ) pathway (By similarity). Acts
CC as a protease: mediates autocatalytic processing of its N-terminal
CC methionine in order to expose the catalytic cysteine (By similarity).
CC {ECO:0000250|UniProtKB:Q8R1M0, ECO:0000269|PubMed:30554877,
CC ECO:0000269|PubMed:31235913, ECO:0000269|PubMed:31235915,
CC ECO:0000269|PubMed:31806351}.
CC -!- SUBUNIT: Interacts (via PIP-box motif) with PCNA.
CC {ECO:0000269|PubMed:30554877}.
CC -!- SUBCELLULAR LOCATION: Chromosome {ECO:0000269|PubMed:30554877}.
CC Note=Recruited to chromatin following DNA damage (PubMed:30554877).
CC Localizes to replication forks (PubMed:30554877).
CC {ECO:0000269|PubMed:30554877}.
CC -!- DEVELOPMENTAL STAGE: Expressed at higher level in S-phase than in
CC quiescent cells. {ECO:0000269|PubMed:30554877}.
CC -!- DOMAIN: Glu-127 is involved in sensing abasic sites in single-stranded
CC DNA (ssDNA). His-210 stabilizes the abasic sites by forming a hydrogen
CC bond with the O4' hydroxyl group. {ECO:0000250|UniProtKB:P76318}.
CC -!- PTM: Ubiquitinated; the covalent HMCES DNA-protein cross-link is
CC ubiquitinated, leading to its degradation by the proteasome.
CC {ECO:0000269|PubMed:30554877}.
CC -!- SIMILARITY: Belongs to the SOS response-associated peptidase family.
CC {ECO:0000305}.
CC -!- CAUTION: Was initially reported to specifically bind 5-
CC hydroxymethylcytosine (5hmC)-containing DNA in stem cells (By
CC similarity). It was later suggested to act as an endonuclease that
CC specifically cleaves 5hmC-containing DNA (By similarity). However, the
CC endonuclease activity on 5hmC-containing DNA could not be confirmed by
CC another report (PubMed:30554877). {ECO:0000250|UniProtKB:Q8R1M0,
CC ECO:0000269|PubMed:30554877}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF86870.1; Type=Frameshift; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Protein Spotlight; Note=Integrity - Issue 226 of
CC June 2020;
CC URL="https://web.expasy.org/spotlight/back_issues/226/";
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DR EMBL; AF201934; AAF86870.1; ALT_FRAME; mRNA.
DR EMBL; AC137695; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471052; EAW79266.1; -; Genomic_DNA.
DR EMBL; BC009993; AAH09993.1; -; mRNA.
DR EMBL; BC010125; AAH10125.1; -; mRNA.
DR EMBL; BC050686; AAH50686.1; -; mRNA.
DR EMBL; BC088363; AAH88363.1; -; mRNA.
DR CCDS; CCDS33852.1; -.
DR RefSeq; NP_001006109.1; NM_001006109.1.
DR RefSeq; NP_064572.2; NM_020187.2.
DR RefSeq; XP_005247693.1; XM_005247636.3.
DR RefSeq; XP_016862366.1; XM_017006877.1.
DR PDB; 5KO9; X-ray; 1.50 A; A=1-270.
DR PDB; 6OE7; X-ray; 2.20 A; A=2-270.
DR PDB; 6OEA; X-ray; 2.10 A; A=2-270.
DR PDB; 6OEB; X-ray; 2.10 A; A=2-270.
DR PDB; 6OOV; X-ray; 2.20 A; A/B=2-270.
DR PDBsum; 5KO9; -.
DR PDBsum; 6OE7; -.
DR PDBsum; 6OEA; -.
DR PDBsum; 6OEB; -.
DR PDBsum; 6OOV; -.
DR AlphaFoldDB; Q96FZ2; -.
DR SMR; Q96FZ2; -.
DR BioGRID; 121265; 45.
DR IntAct; Q96FZ2; 19.
DR MINT; Q96FZ2; -.
DR STRING; 9606.ENSP00000372955; -.
DR GlyGen; Q96FZ2; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q96FZ2; -.
DR PhosphoSitePlus; Q96FZ2; -.
DR SwissPalm; Q96FZ2; -.
DR BioMuta; HMCES; -.
DR DMDM; 74731769; -.
DR EPD; Q96FZ2; -.
DR jPOST; Q96FZ2; -.
DR MassIVE; Q96FZ2; -.
DR MaxQB; Q96FZ2; -.
DR PaxDb; Q96FZ2; -.
DR PeptideAtlas; Q96FZ2; -.
DR PRIDE; Q96FZ2; -.
DR ProteomicsDB; 76573; -.
DR Antibodypedia; 55718; 141 antibodies from 19 providers.
DR DNASU; 56941; -.
DR Ensembl; ENST00000383463.9; ENSP00000372955.3; ENSG00000183624.14.
DR Ensembl; ENST00000389735.7; ENSP00000374385.3; ENSG00000183624.14.
DR Ensembl; ENST00000502878.6; ENSP00000426215.1; ENSG00000183624.14.
DR GeneID; 56941; -.
DR KEGG; hsa:56941; -.
DR MANE-Select; ENST00000383463.9; ENSP00000372955.3; NM_020187.3; NP_064572.2.
DR UCSC; uc003elt.4; human.
DR CTD; 56941; -.
DR DisGeNET; 56941; -.
DR GeneCards; HMCES; -.
DR HGNC; HGNC:24446; HMCES.
DR HPA; ENSG00000183624; Low tissue specificity.
DR MIM; 618288; gene.
DR neXtProt; NX_Q96FZ2; -.
DR OpenTargets; ENSG00000183624; -.
DR PharmGKB; PA142672398; -.
DR VEuPathDB; HostDB:ENSG00000183624; -.
DR eggNOG; KOG2618; Eukaryota.
DR GeneTree; ENSGT00390000018439; -.
DR InParanoid; Q96FZ2; -.
DR OMA; WVTCSVI; -.
DR OrthoDB; 1487237at2759; -.
DR PhylomeDB; Q96FZ2; -.
DR TreeFam; TF324343; -.
DR PathwayCommons; Q96FZ2; -.
DR SignaLink; Q96FZ2; -.
DR BioGRID-ORCS; 56941; 26 hits in 1067 CRISPR screens.
DR ChiTaRS; HMCES; human.
DR GenomeRNAi; 56941; -.
DR Pharos; Q96FZ2; Tbio.
DR PRO; PR:Q96FZ2; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q96FZ2; protein.
DR Bgee; ENSG00000183624; Expressed in islet of Langerhans and 197 other tissues.
DR ExpressionAtlas; Q96FZ2; baseline and differential.
DR Genevisible; Q96FZ2; HS.
DR GO; GO:0005657; C:replication fork; IDA:UniProtKB.
DR GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0003697; F:single-stranded DNA binding; IDA:UniProtKB.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IDA:UniProtKB.
DR GO; GO:0097681; P:double-strand break repair via alternative nonhomologous end joining; IEA:Ensembl.
DR GO; GO:0045830; P:positive regulation of isotype switching; ISS:UniProtKB.
DR GO; GO:0018142; P:protein-DNA covalent cross-linking; IDA:UniProtKB.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.90.1680.10; -; 1.
DR InterPro; IPR003738; SRAP.
DR InterPro; IPR036590; SRAP-like.
DR PANTHER; PTHR13604; PTHR13604; 1.
DR Pfam; PF02586; SRAP; 1.
DR SUPFAM; SSF143081; SSF143081; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Autocatalytic cleavage; Chromosome;
KW Covalent protein-DNA linkage; DNA damage; DNA-binding; Hydrolase;
KW Isopeptide bond; Phosphoprotein; Protease; Reference proteome;
KW Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q8R1M0"
FT CHAIN 2..354
FT /note="Abasic site processing protein HMCES"
FT /id="PRO_0000164394"
FT REGION 292..354
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 332..338
FT /note="PIP-box"
FT /evidence="ECO:0000269|PubMed:30554877"
FT COMPBIAS 293..307
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 308..324
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 334..354
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 2
FT /note="Nucleophile"
FT /evidence="ECO:0000269|PubMed:31235913,
FT ECO:0000305|PubMed:30554877"
FT SITE 127
FT /note="Required for sensing abasic sites"
FT /evidence="ECO:0000250|UniProtKB:P76318"
FT SITE 210
FT /note="Required to stabilize abasic sites"
FT /evidence="ECO:0000250|UniProtKB:P76318"
FT MOD_RES 2
FT /note="Thiazolidine linkage to a ring-opened DNA abasic
FT site"
FT /evidence="ECO:0000269|PubMed:31235913"
FT MOD_RES 160
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 295
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 322
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT CROSSLNK 148
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 151
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 275
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 276
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 306
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 339
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25755297,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 342
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT MUTAGEN 2
FT /note="C->A: Cells are hypersensitive to ionizing
FT radiations. Abolished ability to form a covalent cross-link
FT with DNA. Does not affect single-stranded DNA (ssDNA)-
FT binding. Does not affect ability to promote class switch
FT recombination (CSR) in B-cells."
FT /evidence="ECO:0000269|PubMed:30554877,
FT ECO:0000269|PubMed:31806351"
FT MUTAGEN 4
FT /note="R->A: Strongly reduced binding to single-stranded
FT DNA."
FT /evidence="ECO:0000269|PubMed:31235913"
FT MUTAGEN 81
FT /note="W->E: Strongly reduced binding to single-stranded
FT DNA."
FT /evidence="ECO:0000269|PubMed:31235913"
FT MUTAGEN 98
FT /note="R->A: Cells are hypersensitive to ionizing
FT radiations. Abolished ability to form a covalent cross-link
FT with DNA. Abolished binding to single-stranded DNA
FT (ssDNA)."
FT /evidence="ECO:0000269|PubMed:30554877"
FT MUTAGEN 212
FT /note="R->A: Abolished ability to bind DNA and abolished
FT ability to promote class switch recombination (CSR) in B-
FT cells."
FT /evidence="ECO:0000269|PubMed:31806351"
FT MUTAGEN 337..338
FT /note="WL->AA: Abolished interaction with PCNA. Cells are
FT hypersensitive to ionizing radiations."
FT /evidence="ECO:0000269|PubMed:30554877"
FT CONFLICT 60
FT /note="E -> D (in Ref. 4; AAH09993)"
FT /evidence="ECO:0000305"
FT STRAND 5..7
FT /evidence="ECO:0007829|PDB:5KO9"
FT HELIX 11..16
FT /evidence="ECO:0007829|PDB:5KO9"
FT STRAND 31..34
FT /evidence="ECO:0007829|PDB:5KO9"
FT HELIX 35..37
FT /evidence="ECO:0007829|PDB:5KO9"
FT STRAND 41..44
FT /evidence="ECO:0007829|PDB:5KO9"
FT STRAND 48..55
FT /evidence="ECO:0007829|PDB:5KO9"
FT HELIX 56..58
FT /evidence="ECO:0007829|PDB:5KO9"
FT STRAND 67..76
FT /evidence="ECO:0007829|PDB:5KO9"
FT STRAND 84..86
FT /evidence="ECO:0007829|PDB:6OEA"
FT HELIX 87..89
FT /evidence="ECO:0007829|PDB:5KO9"
FT STRAND 96..98
FT /evidence="ECO:0007829|PDB:5KO9"
FT HELIX 99..101
FT /evidence="ECO:0007829|PDB:5KO9"
FT TURN 102..104
FT /evidence="ECO:0007829|PDB:5KO9"
FT HELIX 106..113
FT /evidence="ECO:0007829|PDB:5KO9"
FT STRAND 117..130
FT /evidence="ECO:0007829|PDB:5KO9"
FT STRAND 137..143
FT /evidence="ECO:0007829|PDB:5KO9"
FT HELIX 166..168
FT /evidence="ECO:0007829|PDB:5KO9"
FT STRAND 174..183
FT /evidence="ECO:0007829|PDB:5KO9"
FT STRAND 192..201
FT /evidence="ECO:0007829|PDB:5KO9"
FT HELIX 204..206
FT /evidence="ECO:0007829|PDB:5KO9"
FT TURN 207..209
FT /evidence="ECO:0007829|PDB:5KO9"
FT STRAND 211..214
FT /evidence="ECO:0007829|PDB:5KO9"
FT HELIX 220..227
FT /evidence="ECO:0007829|PDB:5KO9"
FT TURN 229..231
FT /evidence="ECO:0007829|PDB:5KO9"
FT HELIX 234..238
FT /evidence="ECO:0007829|PDB:5KO9"
FT STRAND 248..252
FT /evidence="ECO:0007829|PDB:5KO9"
FT HELIX 254..257
FT /evidence="ECO:0007829|PDB:5KO9"
FT HELIX 264..267
FT /evidence="ECO:0007829|PDB:5KO9"
SQ SEQUENCE 354 AA; 40575 MW; 209496BB7E331785 CRC64;
MCGRTSCHLP RDVLTRACAY QDRRGQQRLP EWRDPDKYCP SYNKSPQSNS PVLLSRLHFE
KDADSSERII APMRWGLVPS WFKESDPSKL QFNTTNCRSD TVMEKRSFKV PLGKGRRCVV
LADGFYEWQR CQGTNQRQPY FIYFPQIKTE KSGSIGAADS PENWEKVWDN WRLLTMAGIF
DCWEPPEGGD VLYSYTIITV DSCKGLSDIH HRMPAILDGE EAVSKWLDFG EVSTQEALKL
IHPTENITFH AVSSVVNNSR NNTPECLAPV DLVVKKELRA SGSSQRMLQW LATKSPKKED
SKTPQKEESD VPQWSSQFLQ KSPLPTKRGT AGLLEQWLKR EKEEEPVAKR PYSQ
