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 13-FEB-2019, entry version 99. 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; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; 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., RA Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., RA Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., RA Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., RA Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., RA Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., RA 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., RA Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., RA Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., RA Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., RA Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., RA Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., RA Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., RA 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 RT project: 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 RT the 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 RP THR-392, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP 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., RA Bartram C.R., Kirschner-Schwabe R., Bornhaeuser B., Bourquin J.P., RA Cazzaniga G., Hauer J., Attarbaschi A., Izraeli S., Zaliova M., RA Cario G., Zimmermann M., Avigad S., Sokalska-Duhme M., Metzler M., RA Schrappe M., Koehler R., Te Kronnie G., Stanulla M.; RT "Frequent and sex-biased deletion of SLX4IP by illegitimate V(D)J- RT mediated 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 RP LYS-356, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP 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 RT replication stress reveals novel small ubiquitin-like modified target RT proteins and 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; RP LYS-176; LYS-239; LYS-242; LYS-256; LYS-291; LYS-347; LYS-356; LYS-372 RP AND LYS-399, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP 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- RT modification with phosphorylation."; RL Nat. Struct. Mol. Biol. 24:325-336(2017). CC -!- SUBUNIT: Interacts with SLX4/BTBD12; subunit of different CC structure-specific endonucleases. {ECO:0000269|PubMed:19596235}. CC -!- INTERACTION: CC Q8IY92:SLX4; NbExp=4; IntAct=EBI-2370881, EBI-2370740; CC -!- DISEASE: Note=Chromosomal aberrations involving SLX4IP are found CC in acute lymphoblastic leukemia. A site-specific deletion within CC the 5' region of SLX4IP is found in 30% of childhood acute CC lymphoblastic leukemia in general and more than 60% of ETV6/RUNX1- CC rearranged acute lymphoblastic leukemia. Breakpoints within SLX4IP CC reveal junctions with typical characteristics of illegitimate CC V(D)J mediated recombination. SLX4IP deletions are significantly CC associated with male gender and ETV6/RUNX1-rearranged acute CC lymphoblastic leukemia. {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 UniGene; Hs.668782; -. DR UniGene; Hs.744930; -. DR ProteinModelPortal; Q5VYV7; -. DR BioGrid; 126147; 22. DR IntAct; Q5VYV7; 22. DR STRING; 9606.ENSP00000335557; -. DR iPTMnet; Q5VYV7; -. DR PhosphoSitePlus; Q5VYV7; -. DR BioMuta; SLX4IP; -. DR DMDM; 74747720; -. DR EPD; Q5VYV7; -. DR jPOST; Q5VYV7; -. DR MaxQB; Q5VYV7; -. DR PaxDb; Q5VYV7; -. DR PeptideAtlas; Q5VYV7; -. DR PRIDE; Q5VYV7; -. DR ProteomicsDB; 65652; -. DR Ensembl; ENST00000334534; ENSP00000335557; ENSG00000149346. DR GeneID; 128710; -. DR KEGG; hsa:128710; -. DR UCSC; uc010zre.3; human. DR CTD; 128710; -. DR DisGeNET; 128710; -. DR EuPathDB; HostDB:ENSG00000149346.14; -. DR GeneCards; SLX4IP; -. DR H-InvDB; HIX0027687; -. DR HGNC; HGNC:16225; SLX4IP. DR HPA; HPA046372; -. DR MIM; 615958; gene. DR neXtProt; NX_Q5VYV7; -. DR OpenTargets; ENSG00000149346; -. DR PharmGKB; PA25801; -. DR eggNOG; ENOG410IK12; Eukaryota. DR eggNOG; ENOG4111ZEV; LUCA. DR GeneTree; ENSGT00390000016400; -. DR HOGENOM; HOG000112024; -. DR HOVERGEN; HBG094893; -. DR InParanoid; Q5VYV7; -. DR OMA; QKRRNCS; -. DR OrthoDB; 575561at2759; -. DR PhylomeDB; Q5VYV7; -. DR TreeFam; TF330769; -. DR ChiTaRS; SLX4IP; human. DR GenomeRNAi; 128710; -. DR PRO; PR:Q5VYV7; -. DR Proteomes; UP000005640; Chromosome 20. DR Bgee; ENSG00000149346; Expressed in 194 organ(s), highest expression level in caput epididymis. 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 Complete proteome; Isopeptide bond; Phosphoprotein; Polymorphism; KW Reference proteome; Ubl conjugation. FT CHAIN 1 408 Protein SLX4IP. FT /FTId=PRO_0000306119. FT MOD_RES 130 130 Phosphoserine. FT {ECO:0000244|PubMed:23186163}. FT MOD_RES 213 213 Phosphoserine. FT {ECO:0000244|PubMed:23186163}. FT MOD_RES 392 392 Phosphothreonine. FT {ECO:0000244|PubMed:23186163}. FT CROSSLNK 61 61 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in SUMO2). FT {ECO:0000244|PubMed:28112733}. FT CROSSLNK 79 79 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in SUMO2). FT {ECO:0000244|PubMed:25755297, FT ECO:0000244|PubMed:28112733}. FT CROSSLNK 167 167 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in SUMO2). FT {ECO:0000244|PubMed:28112733}. FT CROSSLNK 176 176 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in SUMO2). FT {ECO:0000244|PubMed:28112733}. FT CROSSLNK 239 239 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in SUMO2). FT {ECO:0000244|PubMed:25755297, FT ECO:0000244|PubMed:28112733}. FT CROSSLNK 242 242 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in SUMO2). FT {ECO:0000244|PubMed:28112733}. FT CROSSLNK 256 256 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in SUMO2). FT {ECO:0000244|PubMed:28112733}. FT CROSSLNK 291 291 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in SUMO2). FT {ECO:0000244|PubMed:28112733}. FT CROSSLNK 347 347 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in SUMO2). FT {ECO:0000244|PubMed:25755297, FT ECO:0000244|PubMed:28112733}. FT CROSSLNK 356 356 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in SUMO2). FT {ECO:0000244|PubMed:25755297, FT ECO:0000244|PubMed:28112733}. FT CROSSLNK 372 372 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in SUMO2). FT {ECO:0000244|PubMed:28112733}. FT CROSSLNK 399 399 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in SUMO2). FT {ECO:0000244|PubMed:28112733}. FT VARIANT 317 317 R -> Q (in dbSNP:rs6077853). FT /FTId=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 //