ID SLX4I_HUMAN Reviewed; 408 AA. AC Q5VYV7; Q05CG2; Q05CT9; DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot. DT 07-DEC-2004, sequence version 1. DT 29-SEP-2021, entry version 113. DE RecName: Full=Protein SLX4IP; DE AltName: Full=SLX4-interacting protein; GN Name=SLX4IP; Synonyms=C20orf94; 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 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 [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Prostate; 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 [3] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007; RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., RA Greff Z., Keri G., Stemmann O., Mann M.; RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the RT kinome across the cell cycle."; RL Mol. Cell 31:438-448(2008). RN [4] RP INTERACTION WITH SLX4. RX PubMed=19596235; DOI=10.1016/j.cell.2009.06.030; RA Svendsen J.M., Smogorzewska A., Sowa M.E., O'Connell B.C., Gygi S.P., RA Elledge S.J., Harper J.W.; RT "Mammalian BTBD12/SLX4 assembles a Holliday junction resolvase and is RT required for DNA repair."; RL Cell 138:63-77(2009). RN [5] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-130; SER-213 AND THR-392, 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 [6] RP CHROMOSOMAL REARRANGEMENT. RX PubMed=24045615; DOI=10.1093/hmg/ddt447; RA Meissner B., Bartram T., Eckert C., Trka J., Panzer-Gruemayer R., RA Hermanova I., Ellinghaus E., Franke A., Moericke A., Schrauder A., RA Teigler-Schlegel A., Doerge P., von Stackelberg A., Basso G., Bartram C.R., RA Kirschner-Schwabe R., Bornhaeuser B., Bourquin J.P., Cazzaniga G., RA Hauer J., Attarbaschi A., Izraeli S., Zaliova M., Cario G., Zimmermann M., RA Avigad S., Sokalska-Duhme M., Metzler M., Schrappe M., Koehler R., RA Te Kronnie G., Stanulla M.; RT "Frequent and sex-biased deletion of SLX4IP by illegitimate V(D)J-mediated RT recombination in childhood acute lymphoblastic leukemia."; RL Hum. Mol. Genet. 23:590-601(2014). RN [7] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-79; LYS-239; LYS-347 AND LYS-356, RP AND IDENTIFICATION BY MASS 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 [8] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-61; LYS-79; LYS-167; LYS-176; RP LYS-239; LYS-242; LYS-256; LYS-291; LYS-347; LYS-356; LYS-372 AND LYS-399, RP AND 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 -!- SUBUNIT: Interacts with SLX4/BTBD12; subunit of different structure- CC specific endonucleases. {ECO:0000269|PubMed:19596235}. CC -!- INTERACTION: CC Q5VYV7; Q8IY92: SLX4; NbExp=4; IntAct=EBI-2370881, EBI-2370740; CC -!- DISEASE: Note=Chromosomal aberrations involving SLX4IP are found in CC acute lymphoblastic leukemia. A site-specific deletion within the 5' CC region of SLX4IP is found in 30% of childhood acute lymphoblastic CC leukemia in general and more than 60% of ETV6/RUNX1-rearranged acute CC lymphoblastic leukemia. Breakpoints within SLX4IP reveal junctions with CC typical characteristics of illegitimate V(D)J mediated recombination. CC SLX4IP deletions are significantly associated with male gender and CC ETV6/RUNX1-rearranged acute lymphoblastic leukemia. CC {ECO:0000269|PubMed:24045615}. CC -!- SIMILARITY: Belongs to the SLX4IP family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAH20787.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305}; CC Sequence=AAH26094.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305}; 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; AL133340; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL353599; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL035456; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC020787; AAH20787.1; ALT_SEQ; mRNA. DR EMBL; BC026094; AAH26094.1; ALT_SEQ; mRNA. DR CCDS; CCDS33439.1; -. DR RefSeq; NP_001009608.1; NM_001009608.2. DR SMR; Q5VYV7; -. DR BioGRID; 126147; 46. DR IntAct; Q5VYV7; 28. DR STRING; 9606.ENSP00000335557; -. DR iPTMnet; Q5VYV7; -. DR PhosphoSitePlus; Q5VYV7; -. DR BioMuta; SLX4IP; -. DR DMDM; 74747720; -. DR EPD; Q5VYV7; -. DR jPOST; Q5VYV7; -. DR MassIVE; Q5VYV7; -. DR MaxQB; Q5VYV7; -. DR PaxDb; Q5VYV7; -. DR PeptideAtlas; Q5VYV7; -. DR PRIDE; Q5VYV7; -. DR ProteomicsDB; 65652; -. DR Antibodypedia; 62780; 21 antibodies. DR DNASU; 128710; -. DR Ensembl; ENST00000334534; ENSP00000335557; ENSG00000149346. DR GeneID; 128710; -. DR KEGG; hsa:128710; -. DR UCSC; uc010zre.3; human. DR CTD; 128710; -. DR DisGeNET; 128710; -. DR GeneCards; SLX4IP; -. DR HGNC; HGNC:16225; SLX4IP. DR HPA; ENSG00000149346; Low tissue specificity. DR MIM; 615958; gene. DR neXtProt; NX_Q5VYV7; -. DR OpenTargets; ENSG00000149346; -. DR PharmGKB; PA25801; -. DR VEuPathDB; HostDB:ENSG00000149346; -. DR eggNOG; ENOG502QQHZ; Eukaryota. DR GeneTree; ENSGT00390000016400; -. DR HOGENOM; CLU_039900_0_0_1; -. DR InParanoid; Q5VYV7; -. DR OMA; GIHLRCI; -. DR OrthoDB; 575561at2759; -. DR PhylomeDB; Q5VYV7; -. DR TreeFam; TF330769; -. DR PathwayCommons; Q5VYV7; -. DR BioGRID-ORCS; 128710; 6 hits in 1016 CRISPR screens. DR ChiTaRS; SLX4IP; human. DR GenomeRNAi; 128710; -. DR Pharos; Q5VYV7; Tdark. DR PRO; PR:Q5VYV7; -. DR Proteomes; UP000005640; Chromosome 20. DR RNAct; Q5VYV7; protein. DR Bgee; ENSG00000149346; Expressed in metanephros and 209 other tissues. DR ExpressionAtlas; Q5VYV7; baseline and differential. DR Genevisible; Q5VYV7; HS. DR InterPro; IPR031479; SLX4IP. DR PANTHER; PTHR28557; PTHR28557; 1. DR Pfam; PF15744; UPF0492; 1. PE 1: Evidence at protein level; KW Isopeptide bond; Phosphoprotein; Reference proteome; Ubl conjugation. FT CHAIN 1..408 FT /note="Protein SLX4IP" FT /id="PRO_0000306119" FT REGION 173..226 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 243..313 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 365..408 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 176..196 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 206..220 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 271..296 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 297..313 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 367..394 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 130 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 213 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 392 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:23186163" FT CROSSLNK 61 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 79 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 167 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 176 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 239 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 242 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 256 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 291 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 347 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 356 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 372 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 399 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT VARIANT 317 FT /note="R -> Q (in dbSNP:rs6077853)" FT /id="VAR_035277" SQ SEQUENCE 408 AA; 45552 MW; 4CBC9DF90E3B14E9 CRC64; MASKKFAVKC GNFAVLVDLH ILPQGSNKDT SWFSEQKKEE VCLLLKETID SRVQEYLEVR KQHRPSNAEF TRSNPLSLKG YGFQITAYFL KRGIRLRCIR STQNAELCVF PDRFVVCVSQ LAFSRDLLAS QNEDLTERVL HGVSDYFAEC AESSLPPSAK LRRNALKEIV KRTETKSSVT SKSQTRRDTV ETSSDSVIAE IARRRNDGQA SSSPPSESMG QAKDSIKAAE SHWGLPVQKL EKVNQTQPED TSGQQKPHPG ERLKTGLLSR SPVCSCESAS PCPKQSPRVA KTQQKRRNCS SAEDFDHHGR VSLGSDRLVP REIIVEKSKA VRVLPASELS DPGLLLKQDL AKTTSKEELH VLESLSSRHL MKNNPGQAQQ TGLATNTERL STIQNSPTKK RKKYERGH //