FSD1_HUMAN
ID FSD1_HUMAN Reviewed; 496 AA.
AC Q9BTV5; B2RDT0; Q9BXN0; Q9HAG4;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Fibronectin type III and SPRY domain-containing protein 1;
DE AltName: Full=MID1-related protein 1;
DE AltName: Full=Microtubule-associated protein GLFND;
GN Name=FSD1; Synonyms=GLFND, MIR1; ORFNames=VLP27;
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], TISSUE SPECIFICITY, AND VARIANT VAL-232.
RX PubMed=11267680; DOI=10.1016/s0167-4781(01)00178-6;
RA Carim-Todd L., Escarceller M., Estivill X., Sumoy L.;
RT "Characterization of human FSD1, a novel brain specific gene on chromosome
RT 19 with paralogy to 9q31.";
RL Biochim. Biophys. Acta 1518:200-203(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND SUBCELLULAR LOCATION.
RC TISSUE=Fibrosarcoma;
RX PubMed=12445389; DOI=10.1016/s0960-9822(02)01299-x;
RA Manabe R., Whitmore L., Weiss J.M., Horwitz A.R.;
RT "Identification of a novel microtubule-associated protein that regulates
RT microtubule organization and cytokinesis by using a GFP-screening
RT strategy.";
RL Curr. Biol. 12:1946-1951(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo, and 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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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 FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND MUTAGENESIS OF
RP SER-313; SER-317; THR-322 AND SER-324.
RX PubMed=12154070; DOI=10.1242/jcs.115.17.3389;
RA Stein P.A., Toret C.P., Salic A.N., Rolls M.M., Rapoport T.A.;
RT "A novel centrosome-associated protein with affinity for microtubules.";
RL J. Cell Sci. 115:3389-3402(2002).
RN [6]
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 [7]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-320, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Colon carcinoma;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
CC -!- FUNCTION: May be involved in microtubule organization and
CC stabilization. {ECO:0000269|PubMed:12154070,
CC ECO:0000269|PubMed:12445389}.
CC -!- SUBUNIT: Oligomerization is required for binding to microtubules.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome. Nucleus. Cytoplasm. Cleavage furrow. Note=Cell-
CC cycle-dependent association with the centrosome. Colocalizes with a
CC subpopulation of microtubules. Does not associates with microtubules
CC during mitosis but reassociates with microtubules during cytokinesis.
CC Localizes to the central portions of a small subset of microtubules in
CC interphase cells and a subpopulation of microtubules in the cleavage
CC furrow, not present in the mitotic spindle.
CC -!- TISSUE SPECIFICITY: Highly expressed in brain tissues, including
CC cerebellum, cerebral cortex, medulla, occipital pole, frontal lobe,
CC temporal lobe and putamen. Lower expression in spinal chord.
CC {ECO:0000269|PubMed:11267680, ECO:0000269|PubMed:12154070}.
CC -!- DOMAIN: B30.2 box contains a microtubule-binding site.
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DR EMBL; AF316829; AAK26747.1; -; mRNA.
DR EMBL; AY032617; AAK51145.1; -; mRNA.
DR EMBL; AK021750; BAB13885.1; -; mRNA.
DR EMBL; AK315661; BAG38027.1; -; mRNA.
DR EMBL; BC003124; AAH03124.1; -; mRNA.
DR CCDS; CCDS12127.1; -.
DR RefSeq; NP_077309.1; NM_024333.2.
DR AlphaFoldDB; Q9BTV5; -.
DR BioGRID; 122600; 67.
DR IntAct; Q9BTV5; 43.
DR STRING; 9606.ENSP00000221856; -.
DR iPTMnet; Q9BTV5; -.
DR MetOSite; Q9BTV5; -.
DR PhosphoSitePlus; Q9BTV5; -.
DR BioMuta; FSD1; -.
DR DMDM; 74733152; -.
DR EPD; Q9BTV5; -.
DR jPOST; Q9BTV5; -.
DR MassIVE; Q9BTV5; -.
DR MaxQB; Q9BTV5; -.
DR PaxDb; Q9BTV5; -.
DR PeptideAtlas; Q9BTV5; -.
DR PRIDE; Q9BTV5; -.
DR ProteomicsDB; 79013; -.
DR Antibodypedia; 23560; 201 antibodies from 25 providers.
DR DNASU; 79187; -.
DR Ensembl; ENST00000221856.11; ENSP00000221856.5; ENSG00000105255.11.
DR GeneID; 79187; -.
DR KEGG; hsa:79187; -.
DR MANE-Select; ENST00000221856.11; ENSP00000221856.5; NM_024333.3; NP_077309.1.
DR UCSC; uc002lzy.3; human.
DR CTD; 79187; -.
DR DisGeNET; 79187; -.
DR GeneCards; FSD1; -.
DR HGNC; HGNC:13745; FSD1.
DR HPA; ENSG00000105255; Group enriched (brain, testis).
DR MIM; 609828; gene.
DR neXtProt; NX_Q9BTV5; -.
DR OpenTargets; ENSG00000105255; -.
DR PharmGKB; PA134882882; -.
DR VEuPathDB; HostDB:ENSG00000105255; -.
DR eggNOG; KOG2177; Eukaryota.
DR GeneTree; ENSGT00940000159440; -.
DR HOGENOM; CLU_013137_19_1_1; -.
DR InParanoid; Q9BTV5; -.
DR OMA; TPASWCL; -.
DR OrthoDB; 527460at2759; -.
DR PhylomeDB; Q9BTV5; -.
DR TreeFam; TF333654; -.
DR PathwayCommons; Q9BTV5; -.
DR SignaLink; Q9BTV5; -.
DR BioGRID-ORCS; 79187; 21 hits in 1076 CRISPR screens.
DR ChiTaRS; FSD1; human.
DR GenomeRNAi; 79187; -.
DR Pharos; Q9BTV5; Tbio.
DR PRO; PR:Q9BTV5; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q9BTV5; protein.
DR Bgee; ENSG00000105255; Expressed in right frontal lobe and 127 other tissues.
DR ExpressionAtlas; Q9BTV5; baseline and differential.
DR Genevisible; Q9BTV5; HS.
DR GO; GO:0005813; C:centrosome; IMP:UniProtKB.
DR GO; GO:0032154; C:cleavage furrow; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005874; C:microtubule; IMP:UniProtKB.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0042802; F:identical protein binding; IPI:UniProtKB.
DR GO; GO:0008017; F:microtubule binding; IMP:UniProtKB.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0031122; P:cytoplasmic microtubule organization; IMP:UniProtKB.
DR GO; GO:0051302; P:regulation of cell division; IDA:UniProtKB.
DR GO; GO:0032465; P:regulation of cytokinesis; IDA:UniProtKB.
DR GO; GO:0060236; P:regulation of mitotic spindle organization; IDA:UniProtKB.
DR CDD; cd00063; FN3; 1.
DR CDD; cd12901; SPRY_PRY_FSD1; 1.
DR Gene3D; 2.60.120.920; -; 1.
DR Gene3D; 2.60.40.10; -; 1.
DR InterPro; IPR001870; B30.2/SPRY.
DR InterPro; IPR043136; B30.2/SPRY_sf.
DR InterPro; IPR003649; Bbox_C.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR017903; COS_domain.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR035742; SPRY/PRY_FSD1.
DR InterPro; IPR003877; SPRY_dom.
DR Pfam; PF00041; fn3; 1.
DR Pfam; PF00622; SPRY; 1.
DR SMART; SM00502; BBC; 1.
DR SMART; SM00060; FN3; 1.
DR SMART; SM00449; SPRY; 1.
DR SUPFAM; SSF49265; SSF49265; 1.
DR SUPFAM; SSF49899; SSF49899; 1.
DR PROSITE; PS50188; B302_SPRY; 1.
DR PROSITE; PS51262; COS; 1.
DR PROSITE; PS50853; FN3; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; Coiled coil; Cytoplasm; Cytoskeleton;
KW Methylation; Microtubule; Mitosis; Nucleus; Reference proteome.
FT CHAIN 1..496
FT /note="Fibronectin type III and SPRY domain-containing
FT protein 1"
FT /id="PRO_0000316537"
FT DOMAIN 105..162
FT /note="COS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00586"
FT DOMAIN 164..268
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 268..477
FT /note="B30.2/SPRY"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00548"
FT REGION 301..336
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 4..99
FT /evidence="ECO:0000255"
FT MOD_RES 310
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q7TPM6"
FT MOD_RES 320
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT VARIANT 232
FT /note="L -> V (in dbSNP:rs35139245)"
FT /evidence="ECO:0000269|PubMed:11267680"
FT /id="VAR_038385"
FT MUTAGEN 313
FT /note="S->A: In mitosis, remained associated with
FT microtubules; when associated with A-317; A-322 and A-324."
FT /evidence="ECO:0000269|PubMed:12154070"
FT MUTAGEN 313
FT /note="S->D: Reduced ability to associate with
FT microtubules; when associated with D-317; E-322 and D-324."
FT /evidence="ECO:0000269|PubMed:12154070"
FT MUTAGEN 317
FT /note="S->A: In mitosis, remained associated with
FT microtubules; when associated with A-313; A-322 and A-324."
FT /evidence="ECO:0000269|PubMed:12154070"
FT MUTAGEN 317
FT /note="S->D: Reduced ability to associate with
FT microtubules; when associated with D-313; E-322 and D-324."
FT /evidence="ECO:0000269|PubMed:12154070"
FT MUTAGEN 322
FT /note="T->A: In mitosis, remained associated with
FT microtubules; when associated with A-313; A-317 and A-324."
FT /evidence="ECO:0000269|PubMed:12154070"
FT MUTAGEN 322
FT /note="T->E: Reduced ability to associate with
FT microtubules; when associated with D-313; D-317 and D-324."
FT /evidence="ECO:0000269|PubMed:12154070"
FT MUTAGEN 324
FT /note="S->A: In mitosis, remained associated with
FT microtubules; when associated with A-313; A-317 and A-322."
FT /evidence="ECO:0000269|PubMed:12154070"
FT MUTAGEN 324
FT /note="S->D: Reduced ability to associate with
FT microtubules; when associated with D-313; D-317 and E-322."
FT /evidence="ECO:0000269|PubMed:12154070"
FT CONFLICT 295
FT /note="G -> R (in Ref. 3; BAB13885)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 496 AA; 55820 MW; 0FE7B18F14C80D46 CRC64;
MEEQREALRK IIKTLAVKNE EIQSFIYSLK QMLLNVEANS AKVQEDLEAE FQSLFSLLEE
LKEGMLMKIK QDRASRTYEL QNQLAACTRA LESSEELLET ANQTLQAMDS EDFPQAAKQI
KDGVTMAPAF RLSLKAKVSD NMSHLMVDFA QERQMLQALK FLPVPSAPVI DLAESLVADN
CVTLVWRMPD EDSKIDHYVL EYRRTNFEGP PRLKEDQPWM VIEGIRQTEY TLTGLKFDMK
YMNFRVKACN KAVAGEFSEP VTLETPAFMF RLDASTSHQN LRVDDLSVEW DAMGGKVQDI
KAREKDGKGR TASPINSPAR GTPSPKRMPS GRGGRDRFTA ESYTVLGDTL IDGGEHYWEV
RYEPDSKAFG VGVAYRSLGR FEQLGKTAAS WCLHVNNWLQ VSFTAKHANK VKVLDAPVPD
CLGVHCDFHQ GLLSFYNART KQVLHTFKTR FTQPLLPAFT VWCGSFQVTT GLQVPSAVRC
LQKRGSATSS SNTSLT
