SPAT5_HUMAN
ID SPAT5_HUMAN Reviewed; 893 AA.
AC Q8NB90; C9JT97; Q86XW1; Q8NI20; Q8TDL7;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-OCT-2010, sequence version 3.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Ribosome biogenesis protein SPATA5 {ECO:0000305};
DE EC=3.6.4.10 {ECO:0000250|UniProtKB:P32794};
DE AltName: Full=Spermatogenesis-associated factor protein {ECO:0000303|Ref.1};
DE AltName: Full=Spermatogenesis-associated protein 5 {ECO:0000305};
GN Name=SPATA5 {ECO:0000303|PubMed:26299366, ECO:0000312|HGNC:HGNC:18119};
GN Synonyms=AFG2, SPAF {ECO:0000303|Ref.1};
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).
RA Wang Z., Liu Y., Kulesz-Martin M.F.;
RT "Cloning and characterization of human SPAF, a new member of AAA-protein
RT family associated with spermatogenesis and malignant conversion.";
RL Submitted (MAR-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RA Xu J., Wang L., Ye X., Zeng L., Xie Y., Mao Y.;
RT "Cloning and characterization of a novel hSPAF gene.";
RL Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Testis;
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 [6]
RP SUBCELLULAR LOCATION.
RX PubMed=18445686; DOI=10.1242/jcs.019174;
RA Tegha-Dunghu J., Neumann B., Reber S., Krause R., Erfle H., Walter T.,
RA Held M., Rogers P., Hupfeld K., Ruppert T., Ellenberg J., Gruss O.J.;
RT "EML3 is a nuclear microtubule-binding protein required for the correct
RT alignment of chromosomes in metaphase.";
RL J. Cell Sci. 121:1718-1726(2008).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-272; SER-274 AND SER-279, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [8]
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 [9]
RP IDENTIFICATION BY 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 [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [11]
RP INVOLVEMENT IN NEDHSB, AND VARIANTS NEDHSB GLN-84; ILE-90; THR-100; THR-330
RP DEL; LEU-448; LEU-488; GLN-529; CYS-626; GLY-628; GLN-784 AND VAL-844.
RX PubMed=26299366; DOI=10.1016/j.ajhg.2015.07.014;
RA Tanaka A.J., Cho M.T., Millan F., Juusola J., Retterer K., Joshi C.,
RA Niyazov D., Garnica A., Gratz E., Deardorff M., Wilkins A.,
RA Ortiz-Gonzalez X., Mathews K., Panzer K., Brilstra E., van Gassen K.L.,
RA Volker-Touw C.M., van Binsbergen E., Sobreira N., Hamosh A., McKnight D.,
RA Monaghan K.G., Chung W.K.;
RT "Mutations in SPATA5 are associated with microcephaly, intellectual
RT disability, seizures, and hearing loss.";
RL Am. J. Hum. Genet. 97:457-464(2015).
RN [12]
RP INVOLVEMENT IN NEDHSB.
RX PubMed=27246907; DOI=10.1111/cge.12813;
RA Kurata H., Terashima H., Nakashima M., Okazaki T., Matsumura W., Ohno K.,
RA Saito Y., Maegaki Y., Kubota M., Nanba E., Saitsu H., Matsumoto N.,
RA Kato M.;
RT "Characterization of SPATA5-related encephalopathy in early childhood.";
RL Clin. Genet. 90:437-444(2016).
RN [13]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-859, AND IDENTIFICATION BY MASS
RP 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).
RN [14]
RP FUNCTION, INTERACTION WITH C1ORF109, INTERACTION WITH PRE-60S RIBOSOMAL
RP PARTICLES, VARIANTS NEDHSB THR-330 DEL AND GLY-628, AND CHARACTERIZATION OF
RP VARIANTS NEDHSB THR-330 DEL AND GLY-628.
RX PubMed=35354024; DOI=10.1016/j.celrep.2022.110597;
RA Ni C., Schmitz D.A., Lee J., Pawlowski K., Wu J., Buszczak M.;
RT "Labeling of heterochronic ribosomes reveals C1ORF109 and SPATA5 control a
RT late step in human ribosome assembly.";
RL Cell Rep. 38:110597-110597(2022).
RN [15]
RP VARIANT NEDHSB THR-330 DEL.
RX PubMed=28293831; DOI=10.1007/5584_2016_206;
RA Szczaluba K., Szymanska K., Kosinska J., Pollak A., Murcia V., Kedra A.,
RA Stawinski P., Rydzanicz M., Demkow U., Ploski R.;
RT "Isolated hearing impairment caused by SPATA5 mutations in a family with
RT variable phenotypic expression.";
RL Adv. Exp. Med. Biol. 980:59-66(2017).
RN [16]
RP VARIANTS NEDHSB 132-GLN--LEU-893 DEL AND THR-330 DEL.
RX PubMed=34360601; DOI=10.3390/ijms22157835;
RA Braun F., Hentschel A., Sickmann A., Marteau T., Hertel S., Foerster F.,
RA Prokisch H., Wagner M., Wortmann S., Della Marina A., Koelbel H., Roos A.,
RA Schara-Schmidt U.;
RT "Muscular and Molecular Pathology Associated with SPATA5 Deficiency in a
RT Child with EHLMRS.";
RL Int. J. Mol. Sci. 22:0-0(2021).
CC -!- FUNCTION: ATP-dependent chaperone, which plays an essential role in the
CC cytoplasmic maturation steps of pre-60S ribosomal particles by
CC promoting the release of shuttling protein RSL24D1/RLP24 from the pre-
CC ribosomal particles (PubMed:35354024). Acts together with SPATA5L1,
CC C1orf109 and CINP (PubMed:35354024). May be involved in morphological
CC and functional mitochondrial transformations during spermatogenesis (By
CC similarity). {ECO:0000250|UniProtKB:Q3UMC0,
CC ECO:0000269|PubMed:35354024}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.10;
CC Evidence={ECO:0000250|UniProtKB:P32794};
CC -!- SUBUNIT: Associates with pre-60S ribosomal particles (PubMed:35354024).
CC Interacts with C1orf109 (PubMed:35354024).
CC {ECO:0000269|PubMed:35354024}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18445686}.
CC Mitochondrion {ECO:0000250|UniProtKB:Q3UMC0}. Cytoplasm, cytoskeleton,
CC spindle {ECO:0000269|PubMed:18445686}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8NB90-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8NB90-2; Sequence=VSP_033048, VSP_033049;
CC Name=3;
CC IsoId=Q8NB90-3; Sequence=VSP_033046, VSP_033047;
CC -!- DOMAIN: The first ATP-binding region binds ATP with low affinity
CC whereas the second ATP-binding region binds ATP with high affinity.
CC {ECO:0000250|UniProtKB:P32794}.
CC -!- DISEASE: Neurodevelopmental disorder with hearing loss, seizures, and
CC brain abnormalities (NEDHSB) [MIM:616577]: An autosomal recessive
CC disorder characterized by intellectual disability, intractable
CC epilepsy, microcephaly, abnormal muscle tone, and sensorineural hearing
CC loss. {ECO:0000269|PubMed:26299366, ECO:0000269|PubMed:27246907,
CC ECO:0000269|PubMed:28293831, ECO:0000269|PubMed:34360601,
CC ECO:0000269|PubMed:35354024}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the AAA ATPase family. AFG2 subfamily.
CC {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; AF361489; AAM00262.1; -; mRNA.
DR EMBL; AF479656; AAM43608.1; -; mRNA.
DR EMBL; AK091384; BAC03651.1; -; mRNA.
DR EMBL; AC021205; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC026402; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC097492; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC109357; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC048217; AAH48217.1; -; mRNA.
DR CCDS; CCDS3730.1; -. [Q8NB90-1]
DR RefSeq; NP_001304728.1; NM_001317799.1.
DR RefSeq; NP_660208.2; NM_145207.2. [Q8NB90-1]
DR RefSeq; XP_011529981.1; XM_011531679.2. [Q8NB90-2]
DR AlphaFoldDB; Q8NB90; -.
DR SMR; Q8NB90; -.
DR BioGRID; 127927; 91.
DR IntAct; Q8NB90; 21.
DR MINT; Q8NB90; -.
DR STRING; 9606.ENSP00000274008; -.
DR ChEMBL; CHEMBL2311230; -.
DR GlyGen; Q8NB90; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q8NB90; -.
DR MetOSite; Q8NB90; -.
DR PhosphoSitePlus; Q8NB90; -.
DR BioMuta; SPATA5; -.
DR DMDM; 308153554; -.
DR EPD; Q8NB90; -.
DR jPOST; Q8NB90; -.
DR MassIVE; Q8NB90; -.
DR MaxQB; Q8NB90; -.
DR PaxDb; Q8NB90; -.
DR PeptideAtlas; Q8NB90; -.
DR PRIDE; Q8NB90; -.
DR ProteomicsDB; 72749; -. [Q8NB90-1]
DR ProteomicsDB; 72750; -. [Q8NB90-2]
DR ProteomicsDB; 72751; -. [Q8NB90-3]
DR Antibodypedia; 26869; 53 antibodies from 18 providers.
DR DNASU; 166378; -.
DR Ensembl; ENST00000274008.5; ENSP00000274008.3; ENSG00000145375.9. [Q8NB90-1]
DR GeneID; 166378; -.
DR KEGG; hsa:166378; -.
DR MANE-Select; ENST00000274008.5; ENSP00000274008.3; NM_145207.3; NP_660208.2.
DR UCSC; uc003iez.5; human. [Q8NB90-1]
DR CTD; 166378; -.
DR DisGeNET; 166378; -.
DR GeneCards; SPATA5; -.
DR HGNC; HGNC:18119; SPATA5.
DR HPA; ENSG00000145375; Low tissue specificity.
DR MalaCards; SPATA5; -.
DR MIM; 613940; gene.
DR MIM; 616577; phenotype.
DR neXtProt; NX_Q8NB90; -.
DR OpenTargets; ENSG00000145375; -.
DR Orphanet; 457351; Microcephaly-intellectual disability-sensorineural hearing loss-epilepsy-abnormal muscle tone syndrome.
DR PharmGKB; PA38294; -.
DR VEuPathDB; HostDB:ENSG00000145375; -.
DR eggNOG; KOG0730; Eukaryota.
DR GeneTree; ENSGT00940000157323; -.
DR HOGENOM; CLU_000688_10_0_1; -.
DR InParanoid; Q8NB90; -.
DR OrthoDB; 194195at2759; -.
DR PhylomeDB; Q8NB90; -.
DR TreeFam; TF314525; -.
DR PathwayCommons; Q8NB90; -.
DR SignaLink; Q8NB90; -.
DR BioGRID-ORCS; 166378; 663 hits in 1083 CRISPR screens.
DR ChiTaRS; SPATA5; human.
DR GeneWiki; SPATA5; -.
DR GenomeRNAi; 166378; -.
DR Pharos; Q8NB90; Tbio.
DR PRO; PR:Q8NB90; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; Q8NB90; protein.
DR Bgee; ENSG00000145375; Expressed in tendon of biceps brachii and 148 other tissues.
DR ExpressionAtlas; Q8NB90; baseline and differential.
DR Genevisible; Q8NB90; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0005819; C:spindle; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
DR GO; GO:1990275; F:preribosome binding; IDA:UniProtKB.
DR GO; GO:0007420; P:brain development; IMP:UniProtKB.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0042273; P:ribosomal large subunit biogenesis; IDA:UniProtKB.
DR GO; GO:0007283; P:spermatogenesis; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR041569; AAA_lid_3.
DR InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR003960; ATPase_AAA_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00004; AAA; 2.
DR Pfam; PF17862; AAA_lid_3; 2.
DR SMART; SM00382; AAA; 2.
DR SUPFAM; SSF50692; SSF50692; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR PROSITE; PS00674; AAA; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Chaperone; Cytoplasm; Cytoskeleton;
KW Deafness; Developmental protein; Differentiation; Disease variant;
KW Epilepsy; Hydrolase; Intellectual disability; Isopeptide bond;
KW Mitochondrion; Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Repeat; Ribosome biogenesis; Spermatogenesis; Ubl conjugation.
FT CHAIN 1..893
FT /note="Ribosome biogenesis protein SPATA5"
FT /id="PRO_0000330583"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 394..401
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P32794"
FT BINDING 668..675
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P32794"
FT MOD_RES 272
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 274
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 279
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT CROSSLNK 859
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 694..696
FT /note="GPE -> VGC (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_033046"
FT VAR_SEQ 697..893
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_033047"
FT VAR_SEQ 781..790
FT /note="ALMRPGRIDR -> VPPSQTFLLL (in isoform 2)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_033048"
FT VAR_SEQ 791..893
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_033049"
FT VARIANT 27
FT /note="C -> S (in dbSNP:rs35430470)"
FT /id="VAR_042703"
FT VARIANT 84
FT /note="R -> Q (in NEDHSB; dbSNP:rs745858366)"
FT /evidence="ECO:0000269|PubMed:26299366"
FT /id="VAR_075775"
FT VARIANT 90
FT /note="S -> I (in NEDHSB; dbSNP:rs796051893)"
FT /evidence="ECO:0000269|PubMed:26299366"
FT /id="VAR_075776"
FT VARIANT 100
FT /note="A -> T (in NEDHSB; dbSNP:rs796051895)"
FT /evidence="ECO:0000269|PubMed:26299366"
FT /id="VAR_075777"
FT VARIANT 132..893
FT /note="Missing (in NEDHSB)"
FT /evidence="ECO:0000269|PubMed:34360601"
FT /id="VAR_086543"
FT VARIANT 330
FT /note="Missing (in NEDHSB; impaired maturation of pre-60S
FT ribosome)"
FT /evidence="ECO:0000269|PubMed:26299366,
FT ECO:0000269|PubMed:28293831, ECO:0000269|PubMed:34360601,
FT ECO:0000269|PubMed:35354024"
FT /id="VAR_075778"
FT VARIANT 448
FT /note="S -> L (in NEDHSB; dbSNP:rs766034355)"
FT /evidence="ECO:0000269|PubMed:26299366"
FT /id="VAR_075779"
FT VARIANT 488
FT /note="V -> L (in NEDHSB)"
FT /evidence="ECO:0000269|PubMed:26299366"
FT /id="VAR_075780"
FT VARIANT 529
FT /note="R -> Q (in NEDHSB; dbSNP:rs567175477)"
FT /evidence="ECO:0000269|PubMed:26299366"
FT /id="VAR_075781"
FT VARIANT 626
FT /note="W -> C (in NEDHSB; dbSNP:rs1553969639)"
FT /evidence="ECO:0000269|PubMed:26299366"
FT /id="VAR_075782"
FT VARIANT 628
FT /note="D -> G (in NEDHSB; impaired maturation of pre-60S
FT ribosome; dbSNP:rs768528444)"
FT /evidence="ECO:0000269|PubMed:26299366,
FT ECO:0000269|PubMed:35354024"
FT /id="VAR_075783"
FT VARIANT 673
FT /note="S -> Y (in dbSNP:rs35133326)"
FT /id="VAR_042704"
FT VARIANT 784
FT /note="R -> Q (in NEDHSB; dbSNP:rs796051894)"
FT /evidence="ECO:0000269|PubMed:26299366"
FT /id="VAR_075784"
FT VARIANT 844
FT /note="A -> V (in NEDHSB; dbSNP:rs796051892)"
FT /evidence="ECO:0000269|PubMed:26299366"
FT /id="VAR_075785"
FT CONFLICT 55
FT /note="Missing (in Ref. 5; AAH48217)"
FT /evidence="ECO:0000305"
FT CONFLICT 66
FT /note="S -> P (in Ref. 1; AAM00262)"
FT /evidence="ECO:0000305"
FT CONFLICT 210
FT /note="S -> P (in Ref. 1; AAM00262)"
FT /evidence="ECO:0000305"
FT CONFLICT 568
FT /note="C -> Y (in Ref. 3; BAC03651)"
FT /evidence="ECO:0000305"
FT CONFLICT 603
FT /note="L -> F (in Ref. 1; AAM00262)"
FT /evidence="ECO:0000305"
FT CONFLICT 614
FT /note="M -> T (in Ref. 3; BAC03651)"
FT /evidence="ECO:0000305"
FT CONFLICT 695
FT /note="P -> S (in Ref. 2; AAM43608)"
FT /evidence="ECO:0000305"
FT CONFLICT 851
FT /note="D -> G (in Ref. 1; AAM00262)"
FT /evidence="ECO:0000305"
FT CONFLICT 891
FT /note="H -> R (in Ref. 1; AAM00262)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 893 AA; 97904 MW; 60214147CBB31F4A CRC64;
MSSKKNRKRL NQSAENGSSL PSAASSCAEA RAPSAGSDFA ATSGTLTVTN LLEKVDDKIP
KTFQNSLIHL GLNTMKSANI CIGRPVLLTS LNGKQEVYTA WPMAGFPGGK VGLSEMAQKN
VGVRPGDAIQ VQPLVGAVLQ AEEMDVALSD KDMEINEEEL TGCILRKLDG KIVLPGNFLY
CTFYGRPYKL QVLRVKGADG MILGGPQSDS DTDAQRMAFE QSSMETSSLE LSLQLSQLDL
EDTQIPTSRS TPYKPIDDRI TNKASDVLLD VTQSPGDGSG LMLEEVTGLK CNFESAREGN
EQLTEEERLL KFSIGAKCNT DTFYFISSTT RVNFTEIDKN SKEQDNQFKV TYDMIGGLSS
QLKAIREIIE LPLKQPELFK SYGIPAPRGV LLYGPPGTGK TMIARAVANE VGAYVSVING
PEIISKFYGE TEAKLRQIFA EATLRHPSII FIDELDALCP KREGAQNEVE KRVVASLLTL
MDGIGSEVSE GQVLVLGATN RPHALDAALR RPGRFDKEIE IGVPNAQDRL DILQKLLRRV
PHLLTEAELL QLANSAHGYV GADLKVLCNE AGLCALRRIL KKQPNLPDVK VAGLVKITLK
DFLQAMNDIR PSAMREIAID VPNVSWSDIG GLESIKLKLE QAVEWPLKHP ESFIRMGIQP
PKGVLLYGPP GCSKTMIAKA LANESGLNFL AIKGPELMNK YVGESERAVR ETFRKARAVA
PSIIFFDELD ALAVERGSSL GAGNVADRVL AQLLTEMDGI EQLKDVTILA ATNRPDRIDK
ALMRPGRIDR IIYVPLPDAA TRREIFKLQF HSMPVSNEVD LDELILQTDA YSGAEIVAVC
REAALLALEE DIQANLIMKR HFTQALSTVT PRIPESLRRF YEDYQEKSGL HTL
