SUMO5_HUMAN
ID SUMO5_HUMAN Reviewed; 101 AA.
AC G2XKQ0;
DT 10-OCT-2018, integrated into UniProtKB/Swiss-Prot.
DT 10-OCT-2018, sequence version 2.
DT 03-AUG-2022, entry version 57.
DE RecName: Full=Small ubiquitin-related modifier 5 {ECO:0000303|PubMed:27211601};
DE Short=SUMO-5;
DE AltName: Full=SUMO1 pseudogene 1 {ECO:0000312|HGNC:HGNC:33148};
DE AltName: Full=Ubiquitin-like 2 {ECO:0000312|HGNC:HGNC:33148};
DE AltName: Full=Ubiquitin-like 6 {ECO:0000312|HGNC:HGNC:33148};
DE Flags: Precursor;
GN Name=SUMO1P1 {ECO:0000312|HGNC:HGNC:33148};
GN Synonyms=SUMO5 {ECO:0000303|PubMed:27211601},
GN UBL2 {ECO:0000312|HGNC:HGNC:33148}, UBL6 {ECO:0000312|HGNC:HGNC:33148};
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], SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP SUMOYLATION AT LYS-18, MUTAGENESIS OF HIS-12; 17-ILE--ASP-21; LYS-18;
RP ILE-95 AND 96-GLY-GLY-97, SUBUNIT, FUNCTION IN SUMOYLATION OF PML,
RP INTERACTION WITH HIPK2; SP100; PML; DAXX; CBX4; PIAS1; UBE2I AND
RP PML-RARALPHA ONCOPROTEIN, AND IDENTIFICATION IN COMPLEX WITH SAE2.
RX PubMed=27211601; DOI=10.1038/srep26509;
RA Liang Y.C., Lee C.C., Yao Y.L., Lai C.C., Schmitz M.L., Yang W.M.;
RT "SUMO5, a novel poly-sumo isoform, regulates pml nuclear bodies.";
RL Sci. Rep. 6:26509-26509(2016).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11780052; DOI=10.1038/414865a;
RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P.,
RA Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D.,
RA Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G.,
RA Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E.,
RA Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D.,
RA Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M.,
RA Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D.,
RA Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M.,
RA Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A.,
RA Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L.,
RA Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L.,
RA Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 20.";
RL Nature 414:865-871(2001).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.51 ANGSTROMS) OF 5-8.
RX PubMed=30675988; DOI=10.1002/cbic.201800737;
RA Albert L., Penalver A., Djokovic N., Werel L., Hoffarth M., Ruzic D.,
RA Xu J., Essen L.O., Nikolic K., Dou Y., Vazquez O.;
RT "Modulating protein-protein interactions with visible-light responsive
RT peptide backbone photoswitches.";
RL ChemBioChem 20:1417-1429(2019).
CC -!- FUNCTION: Ubiquitin-like protein that can be covalently attached to
CC proteins as a monomer or as a lysine-linked polymer. Regulates the life
CC cycle of promyelocytic leukemia nuclear bodies (PML-NBs).
CC PolySUMO1P1/SUMO5 conjugation on 'Lys-160' of PML facilitates
CC recruitment of PML-NB components, which enlarges PML-NB. SUMO1P1/SUMO5
CC also increases polySUMO2/3 conjugation of PML, resulting in RNF4-
CC mediated disruption of PML-NBs. {ECO:0000269|PubMed:27211601}.
CC -!- SUBUNIT: Interacts with CBX4 (PubMed:27211601). Interacts with PIAS1
CC (PubMed:27211601). Found in a complex with SAE2 (PubMed:27211601).
CC Interacts with UBE2I (PubMed:27211601). Interacts with SP100
CC (PubMed:27211601). Interacts with HIPK2 (PubMed:27211601). Interacts
CC with DAXX (PubMed:27211601). Interacts with PML-RARA oncoprotein; PML-
CC RARalpha outcompetes PML for SUMO1P1/SUMO5 conjugation
CC (PubMed:27211601). {ECO:0000269|PubMed:27211601}.
CC -!- INTERACTION:
CC G2XKQ0; A0A0S2Z4M1: AXIN1; NbExp=3; IntAct=EBI-10175576, EBI-16429430;
CC G2XKQ0; O15169: AXIN1; NbExp=3; IntAct=EBI-10175576, EBI-710484;
CC G2XKQ0; Q96B23: C18orf25; NbExp=3; IntAct=EBI-10175576, EBI-742108;
CC G2XKQ0; P61024: CKS1B; NbExp=3; IntAct=EBI-10175576, EBI-456371;
CC G2XKQ0; Q8WWZ3: EDARADD; NbExp=5; IntAct=EBI-10175576, EBI-2949647;
CC G2XKQ0; P62508: ESRRG; NbExp=3; IntAct=EBI-10175576, EBI-2834260;
CC G2XKQ0; Q9BPY3: FAM118B; NbExp=3; IntAct=EBI-10175576, EBI-726822;
CC G2XKQ0; Q8TCP9: FAM200A; NbExp=3; IntAct=EBI-10175576, EBI-2799179;
CC G2XKQ0; O75344: FKBP6; NbExp=6; IntAct=EBI-10175576, EBI-744771;
CC G2XKQ0; Q53SE7: FLJ13057; NbExp=3; IntAct=EBI-10175576, EBI-10172181;
CC G2XKQ0; P07910: HNRNPC; NbExp=3; IntAct=EBI-10175576, EBI-357966;
CC G2XKQ0; Q9BYQ4: KRTAP9-2; NbExp=3; IntAct=EBI-10175576, EBI-1044640;
CC G2XKQ0; Q96JM7: L3MBTL3; NbExp=3; IntAct=EBI-10175576, EBI-2686809;
CC G2XKQ0; Q5TA79: LCE2A; NbExp=3; IntAct=EBI-10175576, EBI-10246607;
CC G2XKQ0; Q5TA82: LCE2D; NbExp=3; IntAct=EBI-10175576, EBI-10246750;
CC G2XKQ0; Q8NDC0: MAPK1IP1L; NbExp=3; IntAct=EBI-10175576, EBI-741424;
CC G2XKQ0; Q15742: NAB2; NbExp=3; IntAct=EBI-10175576, EBI-8641936;
CC G2XKQ0; O75928: PIAS2; NbExp=3; IntAct=EBI-10175576, EBI-348555;
CC G2XKQ0; Q01826: SATB1; NbExp=3; IntAct=EBI-10175576, EBI-743747;
CC G2XKQ0; Q9Y6X0: SETBP1; NbExp=3; IntAct=EBI-10175576, EBI-2548259;
CC G2XKQ0; P35711: SOX5; NbExp=3; IntAct=EBI-10175576, EBI-3505701;
CC G2XKQ0; P63165: SUMO1; NbExp=3; IntAct=EBI-10175576, EBI-80140;
CC G2XKQ0; Q12933: TRAF2; NbExp=3; IntAct=EBI-10175576, EBI-355744;
CC G2XKQ0; P36406: TRIM23; NbExp=3; IntAct=EBI-10175576, EBI-740098;
CC G2XKQ0; Q9UBT2: UBA2; NbExp=3; IntAct=EBI-10175576, EBI-718569;
CC G2XKQ0; P63279: UBE2I; NbExp=3; IntAct=EBI-10175576, EBI-80168;
CC G2XKQ0; Q7KZS0: UBE2I; NbExp=3; IntAct=EBI-10175576, EBI-10180829;
CC G2XKQ0; Q9HCK0: ZBTB26; NbExp=3; IntAct=EBI-10175576, EBI-3918996;
CC G2XKQ0; Q15916: ZBTB6; NbExp=3; IntAct=EBI-10175576, EBI-7227791;
CC G2XKQ0; O60232: ZNRD2; NbExp=3; IntAct=EBI-10175576, EBI-741415;
CC G2XKQ0; B2R8Y4; NbExp=3; IntAct=EBI-10175576, EBI-10175581;
CC G2XKQ0; Q59GP6; NbExp=3; IntAct=EBI-10175576, EBI-10243413;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:27211601}. Note=Forms
CC prominent non-membrane-bound structures in the nucleus.
CC {ECO:0000269|PubMed:27211601}.
CC -!- TISSUE SPECIFICITY: High expression levels in testes and peripheral
CC blood leukocyte (PubMed:27211601). Expressed also in lung, placenta,
CC liver, spleen and thymus (PubMed:27211601).
CC {ECO:0000269|PubMed:27211601}.
CC -!- PTM: Cleavage of precursor form is necessary for function.
CC {ECO:0000250|UniProtKB:P63165}.
CC -!- PTM: Autosumoylated at Lys-18. {ECO:0000269|PubMed:27211601}.
CC -!- MISCELLANEOUS: Highly conserved among primate species, however is not
CC detected in mice. {ECO:0000269|PubMed:27211601}.
CC -!- SIMILARITY: Belongs to the ubiquitin family. SUMO subfamily.
CC {ECO:0000305}.
CC -!- CAUTION: Defined as a pseudogene by HGNC. However the existence of the
CC functional protein is supported by the inhibition of its expression and
CC its function using siRNAs specifically targeting SUMO1P1/SUMO5.
CC {ECO:0000269|PubMed:27211601}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FJ042790; ACM86836.1; -; mRNA.
DR EMBL; AC005220; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PDB; 6IAM; X-ray; 1.51 A; C=5-8.
DR PDBsum; 6IAM; -.
DR AlphaFoldDB; G2XKQ0; -.
DR SMR; G2XKQ0; -.
DR IntAct; G2XKQ0; 36.
DR iPTMnet; G2XKQ0; -.
DR PhosphoSitePlus; G2XKQ0; -.
DR jPOST; G2XKQ0; -.
DR MassIVE; G2XKQ0; -.
DR PeptideAtlas; G2XKQ0; -.
DR PRIDE; G2XKQ0; -.
DR GeneCards; SUMO1P1; -.
DR HGNC; HGNC:33148; SUMO1P1.
DR neXtProt; NX_G2XKQ0; -.
DR PathwayCommons; G2XKQ0; -.
DR SignaLink; G2XKQ0; -.
DR Pharos; G2XKQ0; Tbio.
DR Proteomes; UP000005640; Unplaced.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:UniProtKB.
DR GO; GO:0031386; F:protein tag; IBA:GO_Central.
DR GO; GO:0008134; F:transcription factor binding; ISS:AgBase.
DR GO; GO:0044389; F:ubiquitin-like protein ligase binding; IBA:GO_Central.
DR GO; GO:0030578; P:PML body organization; IMP:UniProtKB.
DR GO; GO:0016925; P:protein sumoylation; IDA:UniProtKB.
DR CDD; cd16114; Ubl_SUMO1; 1.
DR InterPro; IPR022617; Rad60/SUMO-like_dom.
DR InterPro; IPR046332; SUMO1_Ubl.
DR InterPro; IPR000626; Ubiquitin-like_dom.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR Pfam; PF11976; Rad60-SLD; 1.
DR SMART; SM00213; UBQ; 1.
DR SUPFAM; SSF54236; SSF54236; 1.
DR PROSITE; PS50053; UBIQUITIN_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Isopeptide bond; Nucleus; Reference proteome;
KW Ubl conjugation; Ubl conjugation pathway.
FT CHAIN 1..101
FT /note="Small ubiquitin-related modifier 5"
FT /id="PRO_0000445393"
FT PROPEP 98..101
FT /evidence="ECO:0000250|UniProtKB:P63165"
FT /id="PRO_0000445394"
FT DOMAIN 20..97
FT /note="Ubiquitin-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT MOTIF 17..21
FT /note="Required for PML-NB formation"
FT /evidence="ECO:0000269|PubMed:27211601"
FT CROSSLNK 18
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1P1/SUMO5)"
FT /evidence="ECO:0000269|PubMed:27211601"
FT CROSSLNK 97
FT /note="Glycyl lysine isopeptide (Gly-Lys) (interchain with
FT K-? in acceptor proteins)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT MUTAGEN 12
FT /note="H->D: Does not affect nuclear bodies formation."
FT /evidence="ECO:0000269|PubMed:27211601"
FT MUTAGEN 17..21
FT /note="IKDED->KEGEY: Unable to form nuclear bodies."
FT /evidence="ECO:0000269|PubMed:27211601"
FT MUTAGEN 18
FT /note="K->R: Unable to form nuclear bodies."
FT /evidence="ECO:0000269|PubMed:27211601"
FT MUTAGEN 95
FT /note="I->T: Does not affect nuclear bodies formatiom."
FT /evidence="ECO:0000269|PubMed:27211601"
FT MUTAGEN 96..97
FT /note="GG->AA: Lost the ability to conjugate UBE2I. Unable
FT to form nuclear bodies."
FT /evidence="ECO:0000269|PubMed:27211601"
FT CONFLICT 8
FT /note="P -> L (in Ref. 1; ACM86836)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 101 AA; 11526 MW; 01289B0B66A680FA CRC64;
MSDLEAKPST EHLGDKIKDE DIKLRVIGQD SSEIHFKVKM TTPLKKLKKS YCQRQGVPVN
SLRFLFEGQR IADNHTPEEL GMEEEDVIEV YQEQIGGHST V
