SLF2_HUMAN
ID SLF2_HUMAN Reviewed; 1173 AA.
AC Q8IX21; A8K950; B1AL17; Q5W0L8; Q6GMU6; Q9NPE8;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2005, sequence version 2.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=SMC5-SMC6 complex localization factor protein 2 {ECO:0000312|HGNC:HGNC:17814};
DE AltName: Full=Smc5/6 localization factor 1 {ECO:0000303|PubMed:25931565};
GN Name=SLF2 {ECO:0000303|PubMed:25931565, ECO:0000312|HGNC:HGNC:17814};
GN Synonyms=C10orf6, FAM178A;
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] (ISOFORM 1), VARIANT TYR-541, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Lymphoblast;
RX PubMed=12459258; DOI=10.1016/s0378-1119(02)01019-3;
RA Nikali K., Saharinen J., Peltonen L.;
RT "cDNA cloning, expression profile and genomic structure of a novel human
RT transcript on chromosome 10q24, and its analyses as a candidate gene for
RT infantile onset spinocerebellar ataxia.";
RL Gene 299:111-115(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Testis;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC TISSUE=Kidney;
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 BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-603; SER-607 AND SER-614, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-481, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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 [8]
RP SUBCELLULAR LOCATION, AND MUTAGENESIS OF TYR-142.
RX PubMed=24561620; DOI=10.1038/ncb2918;
RA Alabert C., Bukowski-Wills J.C., Lee S.B., Kustatscher G., Nakamura K.,
RA de Lima Alves F., Menard P., Mejlvang J., Rappsilber J., Groth A.;
RT "Nascent chromatin capture proteomics determines chromatin dynamics during
RT DNA replication and identifies unknown fork components.";
RL Nat. Cell Biol. 16:281-293(2014).
RN [9]
RP FUNCTION, INTERACTION WITH RAD18; SLF1; SMC5 AND SMC6, SUBCELLULAR
RP LOCATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=25931565; DOI=10.1126/science.1253671;
RA Raeschle M., Smeenk G., Hansen R.K., Temu T., Oka Y., Hein M.Y.,
RA Nagaraj N., Long D.T., Walter J.C., Hofmann K., Storchova Z., Cox J.,
RA Bekker-Jensen S., Mailand N., Mann M.;
RT "DNA repair. Proteomics reveals dynamic assembly of repair complexes during
RT bypass of DNA cross-links.";
RL Science 348:1253671-1253671(2015).
CC -!- FUNCTION: Plays a role in the DNA damage response (DDR) pathway by
CC regulating postreplication repair of UV-damaged DNA and genomic
CC stability maintenance (PubMed:25931565). The SLF1-SLF2 complex acts to
CC link RAD18 with the SMC5-SMC6 complex at replication-coupled
CC interstrand cross-links (ICL) and DNA double-strand breaks (DSBs) sites
CC on chromatin during DNA repair in response to stalled replication forks
CC (PubMed:25931565). Promotes the recruitment of the SMC5-SMC6 complex to
CC DNA lesions (PubMed:25931565). {ECO:0000269|PubMed:25931565}.
CC -!- SUBUNIT: Interacts with SLF1 (via N-terminus); this interaction links
CC RAD18 to the SMC5-SMC6 complex (PubMed:25931565). Interacts with RAD18;
CC this interaction is increased in a SLF1-dependent manner
CC (PubMed:25931565). Interacts with SMC5 and SMC6 (PubMed:25931565).
CC {ECO:0000269|PubMed:25931565}.
CC -!- INTERACTION:
CC Q8IX21; P25786: PSMA1; NbExp=3; IntAct=EBI-2682240, EBI-359352;
CC Q8IX21; Q5VUG0: SFMBT2; NbExp=3; IntAct=EBI-2682240, EBI-12025260;
CC Q8IX21; Q8IY18: SMC5; NbExp=2; IntAct=EBI-2682240, EBI-605405;
CC Q8IX21; Q96SB8: SMC6; NbExp=5; IntAct=EBI-2682240, EBI-605415;
CC Q8IX21; Q14142: TRIM14; NbExp=3; IntAct=EBI-2682240, EBI-2820256;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:24561620,
CC ECO:0000269|PubMed:25931565}. Note=Mainly localizes in the nucleus
CC (PubMed:24561620). Colocalizes with PCNA on replication sites
CC (PubMed:24561620). Associates with chromatin (PubMed:25931565).
CC Accumulates with RAD18 and the SMC5-SMC6 complex at replication-coupled
CC DNA interstrand repair and DNA double-strand breaks (DSBs) sites on
CC chromatin in a ubiquitin-dependent manner (PubMed:25931565).
CC {ECO:0000269|PubMed:24561620, ECO:0000269|PubMed:25931565}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8IX21-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8IX21-2; Sequence=VSP_045621;
CC Name=3;
CC IsoId=Q8IX21-3; Sequence=VSP_054914, VSP_054915;
CC -!- TISSUE SPECIFICITY: Widely expressed (PubMed:12459258). Expressed at
CC higher level in skeletal muscle and at slightly lower level in brain,
CC liver and heart, than in lung, kidney, spleen and thymus
CC (PubMed:12459258). {ECO:0000269|PubMed:12459258}.
CC -!- MISCELLANEOUS: Localized in the locus associated with inherited
CC infantile onset spinocerebellar ataxia (IOSCA). No mutation were found
CC associated with IOSCA compared to control subjects. The expression
CC level in the brain was not different between the 2 populations.
CC -!- SIMILARITY: Belongs to the FAM178 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA91657.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF460991; AAN84475.1; -; mRNA.
DR EMBL; AK001374; BAA91657.1; ALT_INIT; mRNA.
DR EMBL; AK292565; BAF85254.1; -; mRNA.
DR EMBL; AL138762; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL133215; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC030565; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BC073832; AAH73832.1; -; mRNA.
DR CCDS; CCDS44470.1; -. [Q8IX21-2]
DR CCDS; CCDS65918.1; -. [Q8IX21-3]
DR CCDS; CCDS7500.1; -. [Q8IX21-1]
DR RefSeq; NP_001129595.1; NM_001136123.1. [Q8IX21-2]
DR RefSeq; NP_001230699.1; NM_001243770.1. [Q8IX21-3]
DR RefSeq; NP_060591.3; NM_018121.3. [Q8IX21-1]
DR AlphaFoldDB; Q8IX21; -.
DR BioGRID; 120841; 23.
DR ComplexPortal; CPX-5992; SMC5-SMC6 SUMO ligase complex, EID3 variant.
DR ComplexPortal; CPX-6086; SMC5-SMC6 SUMO ligase complex, NSE4EA variant.
DR IntAct; Q8IX21; 19.
DR MINT; Q8IX21; -.
DR STRING; 9606.ENSP00000359292; -.
DR iPTMnet; Q8IX21; -.
DR PhosphoSitePlus; Q8IX21; -.
DR BioMuta; SLF2; -.
DR DMDM; 73620064; -.
DR EPD; Q8IX21; -.
DR jPOST; Q8IX21; -.
DR MassIVE; Q8IX21; -.
DR MaxQB; Q8IX21; -.
DR PaxDb; Q8IX21; -.
DR PeptideAtlas; Q8IX21; -.
DR PRIDE; Q8IX21; -.
DR ProteomicsDB; 3129; -.
DR ProteomicsDB; 70968; -. [Q8IX21-1]
DR Antibodypedia; 49598; 19 antibodies from 8 providers.
DR DNASU; 55719; -.
DR Ensembl; ENST00000238961.9; ENSP00000238961.3; ENSG00000119906.13. [Q8IX21-1]
DR Ensembl; ENST00000370269.3; ENSP00000359292.3; ENSG00000119906.13. [Q8IX21-2]
DR Ensembl; ENST00000609386.1; ENSP00000476379.1; ENSG00000119906.13. [Q8IX21-3]
DR GeneID; 55719; -.
DR KEGG; hsa:55719; -.
DR MANE-Select; ENST00000238961.9; ENSP00000238961.3; NM_018121.4; NP_060591.3.
DR UCSC; uc001krq.5; human. [Q8IX21-1]
DR CTD; 55719; -.
DR DisGeNET; 55719; -.
DR GeneCards; SLF2; -.
DR HGNC; HGNC:17814; SLF2.
DR HPA; ENSG00000119906; Low tissue specificity.
DR MIM; 610348; gene.
DR neXtProt; NX_Q8IX21; -.
DR OpenTargets; ENSG00000119906; -.
DR PharmGKB; PA162387411; -.
DR VEuPathDB; HostDB:ENSG00000119906; -.
DR eggNOG; ENOG502QW1I; Eukaryota.
DR GeneTree; ENSGT00530000064017; -.
DR HOGENOM; CLU_008361_0_0_1; -.
DR InParanoid; Q8IX21; -.
DR OMA; HYLVQMK; -.
DR OrthoDB; 713086at2759; -.
DR PhylomeDB; Q8IX21; -.
DR TreeFam; TF332216; -.
DR PathwayCommons; Q8IX21; -.
DR SignaLink; Q8IX21; -.
DR BioGRID-ORCS; 55719; 49 hits in 1075 CRISPR screens.
DR ChiTaRS; SLF2; human.
DR GenomeRNAi; 55719; -.
DR Pharos; Q8IX21; Tbio.
DR PRO; PR:Q8IX21; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; Q8IX21; protein.
DR Bgee; ENSG00000119906; Expressed in adrenal tissue and 196 other tissues.
DR ExpressionAtlas; Q8IX21; baseline and differential.
DR Genevisible; Q8IX21; HS.
DR GO; GO:0000785; C:chromatin; IDA:UniProtKB.
DR GO; GO:0000781; C:chromosome, telomeric region; IC:ComplexPortal.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0035861; C:site of double-strand break; IDA:UniProtKB.
DR GO; GO:0030915; C:Smc5-Smc6 complex; IC:ComplexPortal.
DR GO; GO:0044877; F:protein-containing complex binding; IPI:UniProtKB.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:UniProtKB.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IDA:UniProtKB.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IC:ComplexPortal.
DR GO; GO:2000781; P:positive regulation of double-strand break repair; IDA:UniProtKB.
DR GO; GO:0034184; P:positive regulation of maintenance of mitotic sister chromatid cohesion; IMP:UniProtKB.
DR GO; GO:0031334; P:positive regulation of protein-containing complex assembly; IMP:UniProtKB.
DR GO; GO:1990166; P:protein localization to site of double-strand break; IDA:UniProtKB.
DR GO; GO:0016925; P:protein sumoylation; IC:ComplexPortal.
DR GO; GO:0032204; P:regulation of telomere maintenance; IC:ComplexPortal.
DR InterPro; IPR044276; CANIN_dom.
DR InterPro; IPR026161; FAM178.
DR PANTHER; PTHR16046; PTHR16046; 1.
DR Pfam; PF14816; CANIN; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; DNA damage; DNA repair; Nucleus; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..1173
FT /note="SMC5-SMC6 complex localization factor protein 2"
FT /id="PRO_0000089778"
FT REGION 1..109
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 161..230
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 256..275
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 280..373
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 394..620
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 635..663
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 137..149
FT /note="APIM motif"
FT COMPBIAS 72..90
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 91..107
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 174..196
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 197..220
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 261..275
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 294..310
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 330..373
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 399..432
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 448..462
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 497..530
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 578..592
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 606..620
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 481
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 603
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 607
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 614
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT VAR_SEQ 48..63
FT /note="KQSIIDFFKPASKQDR -> YRAEGLRRGRVAGARV (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_054914"
FT VAR_SEQ 64..1173
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_054915"
FT VAR_SEQ 1163..1173
FT /note="GQLHDFWVPDS -> VSFCYTISCILNSFAEWHSSYCLK (in isoform
FT 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_045621"
FT VARIANT 541
FT /note="S -> Y (in dbSNP:rs10883563)"
FT /evidence="ECO:0000269|PubMed:12459258"
FT /id="VAR_023112"
FT MUTAGEN 142
FT /note="Y->A: In APIMmut; does not affect subcellular
FT location."
FT /evidence="ECO:0000269|PubMed:24561620"
SQ SEQUENCE 1173 AA; 131873 MW; 0A9FB5662185A633 CRC64;
MTRRCMPARP GFPSSPAPGS SPPRCHLRPG STAHAAAGKR TESPGDRKQS IIDFFKPASK
QDRHMLDSPQ KSNIKYGGSR LSITGTEQFE RKLSSPKESK PKRVPPEKSP IIEAFMKGVK
EHHEDHGIHE SRRPCLSLAS KYLAKGTNIY VPSSYHLPKE MKSLKKKHRS PERRKSLFIH
ENNEKNDRDR GKTNADSKKQ TTVAEADIFN NSSRSLSSRS SLSRHHPEES PLGAKFQLSL
ASYCRERELK RLRKEQMEQR INSENSFSEA SSLSLKSSIE RKYKPRQEQR KQNDIIPGKN
NLSNVENGHL SRKRSSSDSW EPTSAGSKQN KFPEKRKRNS VDSDLKSTRE SMIPKARESF
LEKRPDGPHQ KEKFIKHIAL KTPGDVLRLE DISKEPSDET DGSSAGLAPS NSGNSGHHST
RNSDQIQVAG TKETKMQKPH LPLSQEKSAI KKASNLQKNK TASSTTKEKE TKLPLLSRVP
SAGSSLVPLN AKNCALPVSK KDKERSSSKE CSGHSTESTK HKEHKAKTNK ADSNVSSGKI
SGGPLRSEYG TPTKSPPAAL EVVPCIPSPA APSDKAPSEG ESSGNSNAGS SALKRKLRGD
FDSDEESLGY NLDSDEEEET LKSLEEIMAL NFNQTPAATG KPPALSKGLR SQSSDYTGHV
HPGTYTNTLE RLVKEMEDTQ RLDELQKQLQ EDIRQGRGIK SPIRIGEEDS TDDEDGLLEE
HKEFLKKFSV TIDAIPDHHP GEEIFNFLNS GKIFNQYTLD LRDSGFIGQS AVEKLILKSG
KTDQIFLTTQ GFLTSAYHYV QCPVPVLKWL FRMMSVHTDC IVSVQILSTL MEITIRNDTF
SDSPVWPWIP SLSDVAAVFF NMGIDFRSLF PLENLQPDFN EDYLVSETQT TSRGKESEDS
SYKPIFSTLP ETNILNVVKF LGLCTSIHPE GYQDREIMLL ILMLFKMSLE KQLKQIPLVD
FQSLLINLMK NIRDWNTKVP ELCLGINELS SHPHNLLWLV QLVPNWTSRG RQLRQCLSLV
IISKLLDEKH EDVPNASNLQ VSVLHRYLVQ MKPSDLLKKM VLKKKAEQPD GIIDDSLHLE
LEKQAYYLTY ILLHLVGEVS CSHSFSSGQR KHFVLLCGAL EKHVKCDIRE DARLFYRTKV
KDLVARIHGK WQEIIQNCRP TQGQLHDFWV PDS
