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Fibronectin type III and SPRY domain-containing protein 1 (MID1-related protein 1) (Microtubule-associated protein GLFND)

 FSD1_HUMAN              Reviewed;         496 AA.
Q9BTV5; B2RDT0; Q9BXN0; Q9HAG4;
05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
01-JUN-2001, sequence version 1.
22-NOV-2017, entry version 143.
RecName: Full=Fibronectin type III and SPRY domain-containing protein 1;
AltName: Full=MID1-related protein 1;
AltName: Full=Microtubule-associated protein GLFND;
Name=FSD1; Synonyms=GLFND, MIR1; ORFNames=VLP27;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND VARIANT VAL-232.
PubMed=11267680; DOI=10.1016/S0167-4781(01)00178-6;
Carim-Todd L., Escarceller M., Estivill X., Sumoy L.;
"Characterization of human FSD1, a novel brain specific gene on
chromosome 19 with paralogy to 9q31.";
Biochim. Biophys. Acta 1518:200-203(2001).
[2]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND SUBCELLULAR LOCATION.
TISSUE=Fibrosarcoma;
PubMed=12445389; DOI=10.1016/S0960-9822(02)01299-X;
Manabe R., Whitmore L., Weiss J.M., Horwitz A.R.;
"Identification of a novel microtubule-associated protein that
regulates microtubule organization and cytokinesis by using a GFP-
screening strategy.";
Curr. Biol. 12:1946-1951(2002).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Embryo, and Testis;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND MUTAGENESIS OF
SER-313; SER-317; THR-322 AND SER-324.
PubMed=12154070;
Stein P.A., Toret C.P., Salic A.N., Rolls M.M., Rapoport T.A.;
"A novel centrosome-associated protein with affinity for
microtubules.";
J. Cell Sci. 115:3389-3402(2002).
[6]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[7]
METHYLATION [LARGE SCALE ANALYSIS] AT ARG-320, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Colon carcinoma;
PubMed=24129315; DOI=10.1074/mcp.O113.027870;
Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V.,
Aguiar M., Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C.,
Vemulapalli V., Bedford M.T., Comb M.J.;
"Immunoaffinity enrichment and mass spectrometry analysis of protein
methylation.";
Mol. Cell. Proteomics 13:372-387(2014).
-!- FUNCTION: May be involved in microtubule organization and
stabilization. {ECO:0000269|PubMed:12154070,
ECO:0000269|PubMed:12445389}.
-!- SUBUNIT: Oligomerization is required for binding to microtubules.
-!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule
organizing center, centrosome. Nucleus. Cytoplasm. Cleavage
furrow. Note=Cell-cycle-dependent association with the centrosome.
Colocalizes with a subpopulation of microtubules. Does not
associates with microtubules during mitosis but reassociates with
microtubules during cytokinesis. Localizes to the central portions
of a small subset of microtubules in interphase cells and a
subpopulation of microtubules in the cleavage furrow, not present
in the mitotic spindle.
-!- TISSUE SPECIFICITY: Highly expressed in brain tissues, including
cerebellum, cerebral cortex, medulla, occipital pole, frontal
lobe, temporal lobe and putamen. Lower expression in spinal chord.
{ECO:0000269|PubMed:11267680, ECO:0000269|PubMed:12154070}.
-!- DOMAIN: B30.2 box contains a microtubule-binding site.
-----------------------------------------------------------------------
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EMBL; AF316829; AAK26747.1; -; mRNA.
EMBL; AY032617; AAK51145.1; -; mRNA.
EMBL; AK021750; BAB13885.1; -; mRNA.
EMBL; AK315661; BAG38027.1; -; mRNA.
EMBL; BC003124; AAH03124.1; -; mRNA.
CCDS; CCDS12127.1; -.
RefSeq; NP_077309.1; NM_024333.2.
UniGene; Hs.28144; -.
ProteinModelPortal; Q9BTV5; -.
SMR; Q9BTV5; -.
BioGrid; 122600; 62.
IntAct; Q9BTV5; 4.
MINT; MINT-1368061; -.
STRING; 9606.ENSP00000221856; -.
iPTMnet; Q9BTV5; -.
PhosphoSitePlus; Q9BTV5; -.
BioMuta; FSD1; -.
DMDM; 74733152; -.
EPD; Q9BTV5; -.
MaxQB; Q9BTV5; -.
PaxDb; Q9BTV5; -.
PeptideAtlas; Q9BTV5; -.
PRIDE; Q9BTV5; -.
DNASU; 79187; -.
Ensembl; ENST00000221856; ENSP00000221856; ENSG00000105255.
GeneID; 79187; -.
KEGG; hsa:79187; -.
UCSC; uc002lzy.3; human.
CTD; 79187; -.
DisGeNET; 79187; -.
EuPathDB; HostDB:ENSG00000105255.10; -.
GeneCards; FSD1; -.
HGNC; HGNC:13745; FSD1.
HPA; HPA043141; -.
MIM; 609828; gene.
neXtProt; NX_Q9BTV5; -.
OpenTargets; ENSG00000105255; -.
PharmGKB; PA134882882; -.
eggNOG; ENOG410ITFY; Eukaryota.
eggNOG; ENOG410ZECU; LUCA.
GeneTree; ENSGT00760000118878; -.
HOGENOM; HOG000231656; -.
HOVERGEN; HBG107931; -.
InParanoid; Q9BTV5; -.
OMA; AFMVWNG; -.
OrthoDB; EOG091G072W; -.
PhylomeDB; Q9BTV5; -.
TreeFam; TF333654; -.
GenomeRNAi; 79187; -.
PRO; PR:Q9BTV5; -.
Proteomes; UP000005640; Chromosome 19.
Bgee; ENSG00000105255; -.
CleanEx; HS_FSD1; -.
ExpressionAtlas; Q9BTV5; baseline and differential.
Genevisible; Q9BTV5; HS.
GO; GO:0032154; C:cleavage furrow; IEA:UniProtKB-SubCell.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
CDD; cd00063; FN3; 1.
CDD; cd12901; SPRY_PRY_FSD1; 1.
Gene3D; 2.60.40.10; -; 1.
InterPro; IPR001870; B30.2/SPRY.
InterPro; IPR003649; Bbox_C.
InterPro; IPR013320; ConA-like_dom_sf.
InterPro; IPR017903; COS_domain.
InterPro; IPR003961; FN3_dom.
InterPro; IPR036116; FN3_sf.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR035742; SPRY/PRY_FSD1.
InterPro; IPR003877; SPRY_dom.
Pfam; PF00041; fn3; 1.
Pfam; PF00622; SPRY; 1.
SMART; SM00502; BBC; 1.
SMART; SM00060; FN3; 1.
SMART; SM00449; SPRY; 1.
SUPFAM; SSF49265; SSF49265; 1.
SUPFAM; SSF49899; SSF49899; 1.
PROSITE; PS50188; B302_SPRY; 1.
PROSITE; PS51262; COS; 1.
PROSITE; PS50853; FN3; 1.
1: Evidence at protein level;
Cell cycle; Cell division; Coiled coil; Complete proteome; Cytoplasm;
Cytoskeleton; Methylation; Microtubule; Mitosis; Nucleus;
Phosphoprotein; Polymorphism; Reference proteome.
CHAIN 1 496 Fibronectin type III and SPRY domain-
containing protein 1.
/FTId=PRO_0000316537.
DOMAIN 105 162 COS. {ECO:0000255|PROSITE-
ProRule:PRU00586}.
DOMAIN 164 268 Fibronectin type-III.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 268 477 B30.2/SPRY. {ECO:0000255|PROSITE-
ProRule:PRU00548}.
COILED 4 99 {ECO:0000255}.
MOD_RES 310 310 Omega-N-methylarginine.
{ECO:0000250|UniProtKB:Q7TPM6}.
MOD_RES 320 320 Omega-N-methylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 491 491 Phosphoserine.
{ECO:0000250|UniProtKB:Q9BXM9}.
MOD_RES 494 494 Phosphoserine.
{ECO:0000250|UniProtKB:Q9BXM9}.
VARIANT 232 232 L -> V (in dbSNP:rs35139245).
{ECO:0000269|PubMed:11267680}.
/FTId=VAR_038385.
MUTAGEN 313 313 S->A: In mitosis, remained associated
with microtubules; when associated with
A-317; A-322 and A-324.
{ECO:0000269|PubMed:12154070}.
MUTAGEN 313 313 S->D: Reduced ability to associate with
microtubules; when associated with D-317;
E-322 and D-324.
{ECO:0000269|PubMed:12154070}.
MUTAGEN 317 317 S->A: In mitosis, remained associated
with microtubules; when associated with
A-313; A-322 and A-324.
{ECO:0000269|PubMed:12154070}.
MUTAGEN 317 317 S->D: Reduced ability to associate with
microtubules; when associated with D-313;
E-322 and D-324.
{ECO:0000269|PubMed:12154070}.
MUTAGEN 322 322 T->A: In mitosis, remained associated
with microtubules; when associated with
A-313; A-317 and A-324.
{ECO:0000269|PubMed:12154070}.
MUTAGEN 322 322 T->E: Reduced ability to associate with
microtubules; when associated with D-313;
D-317 and D-324.
{ECO:0000269|PubMed:12154070}.
MUTAGEN 324 324 S->A: In mitosis, remained associated
with microtubules; when associated with
A-313; A-317 and A-322.
{ECO:0000269|PubMed:12154070}.
MUTAGEN 324 324 S->D: Reduced ability to associate with
microtubules; when associated with D-313;
D-317 and E-322.
{ECO:0000269|PubMed:12154070}.
CONFLICT 295 295 G -> R (in Ref. 3; BAB13885).
{ECO:0000305}.
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


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