SPART_MOUSE
ID SPART_MOUSE Reviewed; 671 AA.
AC Q8R1X6; Q6ZQ87; Q8BJD3; Q8BM37; Q8BZ63;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Spartin {ECO:0000305};
GN Name=Spart {ECO:0000250|UniProtKB:Q8N0X7};
GN Synonyms=Kiaa0610, Spg20 {ECO:0000312|MGI:MGI:2139806};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Embryonic tail;
RX PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: III.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:167-180(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 11-671 (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Bone, Embryo, and Eye;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-126, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-126, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, Liver, Lung, Pancreas, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: May be implicated in endosomal trafficking, or microtubule
CC dynamics, or both. Participates in cytokinesis.
CC {ECO:0000250|UniProtKB:Q8N0X7}.
CC -!- SUBUNIT: Interacts with ITCH and WWP1. Interacts (via MIT domain) with
CC IST1; leading to the recruitment of SPART to midbodies.
CC {ECO:0000250|UniProtKB:Q8N0X7}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q8N0X7}. Midbody
CC {ECO:0000250|UniProtKB:Q8N0X7}. Note=Transiently associated with
CC endosomes. Colocalized with IST1 to the ends of Flemming bodies during
CC cytokinesis. {ECO:0000250|UniProtKB:Q8N0X7}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8R1X6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8R1X6-2; Sequence=VSP_010934;
CC -!- PTM: Ubiquitinated; ubiquitination does not require ITCH and WWP1.
CC {ECO:0000250}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC39856.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAC97981.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK129171; BAC97981.1; ALT_INIT; mRNA.
DR EMBL; BC022921; AAH22921.1; -; mRNA.
DR EMBL; AK035081; BAC28937.1; -; mRNA.
DR EMBL; AK036569; BAC29482.1; -; mRNA.
DR EMBL; AK087388; BAC39856.1; ALT_INIT; mRNA.
DR CCDS; CCDS38432.1; -. [Q8R1X6-1]
DR CCDS; CCDS50908.1; -. [Q8R1X6-2]
DR RefSeq; NP_001138459.1; NM_001144987.1. [Q8R1X6-1]
DR RefSeq; NP_001138460.1; NM_001144988.1. [Q8R1X6-2]
DR RefSeq; NP_659144.1; NM_144895.2. [Q8R1X6-1]
DR RefSeq; XP_006501383.1; XM_006501320.2. [Q8R1X6-1]
DR AlphaFoldDB; Q8R1X6; -.
DR SMR; Q8R1X6; -.
DR BioGRID; 230829; 16.
DR STRING; 10090.ENSMUSP00000113621; -.
DR iPTMnet; Q8R1X6; -.
DR PhosphoSitePlus; Q8R1X6; -.
DR EPD; Q8R1X6; -.
DR MaxQB; Q8R1X6; -.
DR PaxDb; Q8R1X6; -.
DR PeptideAtlas; Q8R1X6; -.
DR PRIDE; Q8R1X6; -.
DR ProteomicsDB; 263310; -. [Q8R1X6-1]
DR ProteomicsDB; 263311; -. [Q8R1X6-2]
DR Antibodypedia; 42112; 207 antibodies from 31 providers.
DR Ensembl; ENSMUST00000044116; ENSMUSP00000042367; ENSMUSG00000036580. [Q8R1X6-1]
DR Ensembl; ENSMUST00000107971; ENSMUSP00000103605; ENSMUSG00000036580. [Q8R1X6-2]
DR Ensembl; ENSMUST00000118118; ENSMUSP00000113621; ENSMUSG00000036580. [Q8R1X6-1]
DR GeneID; 229285; -.
DR KEGG; mmu:229285; -.
DR UCSC; uc008pga.2; mouse. [Q8R1X6-1]
DR UCSC; uc008pgc.2; mouse. [Q8R1X6-2]
DR CTD; 229285; -.
DR MGI; MGI:2139806; Spg20.
DR VEuPathDB; HostDB:ENSMUSG00000036580; -.
DR eggNOG; KOG2709; Eukaryota.
DR GeneTree; ENSGT00390000012235; -.
DR InParanoid; Q8R1X6; -.
DR OMA; VCSIANC; -.
DR PhylomeDB; Q8R1X6; -.
DR TreeFam; TF105252; -.
DR BioGRID-ORCS; 229285; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Spg20; mouse.
DR PRO; PR:Q8R1X6; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q8R1X6; protein.
DR Bgee; ENSMUSG00000036580; Expressed in animal zygote and 265 other tissues.
DR ExpressionAtlas; Q8R1X6; baseline and differential.
DR Genevisible; Q8R1X6; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005811; C:lipid droplet; IDA:MGI.
DR GO; GO:0030496; C:midbody; ISO:MGI.
DR GO; GO:0005741; C:mitochondrial outer membrane; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0045202; C:synapse; IDA:MGI.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:MGI.
DR GO; GO:0009838; P:abscission; ISO:MGI.
DR GO; GO:0060612; P:adipose tissue development; IMP:MGI.
DR GO; GO:0030509; P:BMP signaling pathway; IMP:MGI.
DR GO; GO:0051301; P:cell division; ISO:MGI.
DR GO; GO:0048669; P:collateral sprouting in absence of injury; IMP:MGI.
DR GO; GO:0034389; P:lipid droplet organization; IMP:MGI.
DR GO; GO:0030514; P:negative regulation of BMP signaling pathway; IMP:MGI.
DR GO; GO:0048698; P:negative regulation of collateral sprouting in absence of injury; IMP:MGI.
DR GO; GO:0050905; P:neuromuscular process; IMP:MGI.
DR GO; GO:0051881; P:regulation of mitochondrial membrane potential; ISO:MGI.
DR InterPro; IPR007330; MIT_dom.
DR InterPro; IPR036181; MIT_dom_sf.
DR InterPro; IPR009686; Senescence/spartin_C.
DR InterPro; IPR045036; Spartin-like.
DR PANTHER; PTHR21068; PTHR21068; 1.
DR Pfam; PF06911; Senescence; 1.
DR SMART; SM00745; MIT; 1.
DR SUPFAM; SSF116846; SSF116846; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Cytoplasm; Isopeptide bond;
KW Phosphoprotein; Reference proteome; Ubl conjugation.
FT CHAIN 1..671
FT /note="Spartin"
FT /id="PRO_0000072120"
FT DOMAIN 16..94
FT /note="MIT"
FT DOMAIN 431..615
FT /note="Senescence"
FT /evidence="ECO:0000255"
FT REGION 110..175
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 346..421
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 635..671
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 157..171
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 363..379
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 653..671
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q8N0X7"
FT MOD_RES 126
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 474
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N0X7"
FT CROSSLNK 360
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q8N0X7"
FT VAR_SEQ 337..393
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14621295,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_010934"
FT CONFLICT 157
FT /note="S -> F (in Ref. 3; BAC28937)"
FT /evidence="ECO:0000305"
FT CONFLICT 264
FT /note="R -> P (in Ref. 3; BAC39856)"
FT /evidence="ECO:0000305"
FT CONFLICT 297
FT /note="D -> N (in Ref. 3; BAC39856)"
FT /evidence="ECO:0000305"
FT CONFLICT 344..353
FT /note="DEFQIPGRSS -> MNSKSLGDQA (in Ref. 3; BAC39856)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 671 AA; 72655 MW; 5C17F0268E420B26 CRC64;
MEREPENGEP AEIKIIKEAY EKAFMFVNKG LNTDELGQKE EAKNYYKQGI GHLLRGISIA
AAEPGHTGPA WEAARQMQQK MKETLQNVRT RLEILEKGLA TSLRNDLQDV PKLYPEFPPK
DACKKSPEQE SVSTAPQRAE VDGSASAACA GPSGAPSALP VPSPSCPAEA PPAYSPQAAE
GHYTVSYGTD SGEFSSVGED FYRNRSQPPP LETLGLDADE LILIPNGVQI FFVNPAGEVS
APSYPGYLRI VRFLDNSLDT VLNRPPGFLQ VCDWLYPLVP DRSPVLKCTV GAYMFPDTML
QAAGCFVGVV LSSELPEDDR ELFEDLLRQM SDLRLQANWN REEDEFQIPG RSSHPSEPPK
EASGTDVRQS SSSGSSIDQG SKDARHKGKR GKKTKDSSEE VNLSQIVPCE PSSEEKSKEL
PEWSEKVAHN ILSGASWVSW GLVKGAEFTG KAIQKGASKL RERIQPEEKP VEVSPAVTRG
LYIAKQATGG AAKVSQLLVD GVCTVANCVG KELAPHVKKH GSKLVPESLK RDKDGKSALD
GAMVVAASSV QGFSTVWQGL ECAAKCIVNN VSAETVQTVR YKYGHNAGEA THNAVDSAIN
VGLTAYNIDN IGIKAMVKKT AKQTGHTLLE DYQIVERPQR ESQGGATSTE GRRDIGKQVE
EEKPGAGKKD K
