Full text data of FSD1
FSD1
(GLFND, MIR1)
[Confidence: low (only semi-automatic identification from reviews)]
Fibronectin type III and SPRY domain-containing protein 1 (MID1-related protein 1; Microtubule-associated protein GLFND)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Fibronectin type III and SPRY domain-containing protein 1 (MID1-related protein 1; Microtubule-associated protein GLFND)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q9BTV5
ID FSD1_HUMAN Reviewed; 496 AA.
AC Q9BTV5; B2RDT0; Q9BXN0; Q9HAG4;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-JUN-2001, sequence version 1.
DT 22-JAN-2014, entry version 107.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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
RT chromosome 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
RT regulates microtubule organization and cytokinesis by using a GFP-
RT screening 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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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
RT project: 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;
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
RT 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.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: May be involved in microtubule organization and
CC stabilization.
CC -!- SUBUNIT: Oligomerization is required for binding to microtubules.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome. Nucleus. Cytoplasm. Cleavage
CC furrow. Note=Cell-cycle-dependent association with the centrosome.
CC Colocalizes with a subpopulation of microtubules. Does not
CC associates with microtubules during mitosis but reassociates with
CC microtubules during cytokinesis. Localizes to the central portions
CC of a small subset of microtubules in interphase cells and a
CC subpopulation of microtubules in the cleavage furrow, not present
CC in the mitotic spindle.
CC -!- TISSUE SPECIFICITY: Highly expressed in brain tissues, including
CC cerebellum, cerebral cortex, medulla, occipital pole, frontal
CC lobe, temporal lobe and putamen. Lower expression in spinal chord.
CC -!- DOMAIN: B30.2 box contains a microtubule-binding site.
CC -!- SIMILARITY: Contains 1 B30.2/SPRY domain.
CC -!- SIMILARITY: Contains 1 COS domain.
CC -!- SIMILARITY: Contains 1 fibronectin type-III domain.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
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 RefSeq; NP_077309.1; NM_024333.2.
DR UniGene; Hs.28144; -.
DR ProteinModelPortal; Q9BTV5; -.
DR IntAct; Q9BTV5; 2.
DR MINT; MINT-1368061; -.
DR STRING; 9606.ENSP00000221856; -.
DR PhosphoSite; Q9BTV5; -.
DR DMDM; 74733152; -.
DR PaxDb; Q9BTV5; -.
DR PRIDE; Q9BTV5; -.
DR DNASU; 79187; -.
DR Ensembl; ENST00000221856; ENSP00000221856; ENSG00000105255.
DR GeneID; 79187; -.
DR KEGG; hsa:79187; -.
DR UCSC; uc002lzy.2; human.
DR CTD; 79187; -.
DR GeneCards; GC19P004304; -.
DR HGNC; HGNC:13745; FSD1.
DR HPA; HPA043141; -.
DR MIM; 609828; gene.
DR neXtProt; NX_Q9BTV5; -.
DR PharmGKB; PA134882882; -.
DR eggNOG; NOG302398; -.
DR HOGENOM; HOG000231656; -.
DR HOVERGEN; HBG107931; -.
DR InParanoid; Q9BTV5; -.
DR OMA; ASWCIHL; -.
DR OrthoDB; EOG7W6WKF; -.
DR PhylomeDB; Q9BTV5; -.
DR GenomeRNAi; 79187; -.
DR NextBio; 68182; -.
DR PRO; PR:Q9BTV5; -.
DR ArrayExpress; Q9BTV5; -.
DR Bgee; Q9BTV5; -.
DR CleanEx; HS_FSD1; -.
DR Genevestigator; Q9BTV5; -.
DR GO; GO:0032154; C:cleavage furrow; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IDA:HPA.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0007067; P:mitosis; IEA:UniProtKB-KW.
DR Gene3D; 2.60.40.10; -; 1.
DR InterPro; IPR001870; B30.2/SPRY.
DR InterPro; IPR003649; Bbox_C.
DR InterPro; IPR008985; ConA-like_lec_gl_sf.
DR InterPro; IPR017903; COS_domain.
DR InterPro; IPR003961; Fibronectin_type3.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003877; SPRY_rcpt.
DR Pfam; PF00041; fn3; 1.
DR Pfam; PF00622; SPRY; 1.
DR SMART; SM00502; BBC; 1.
DR SMART; SM00060; FN3; 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; Complete proteome; Cytoplasm;
KW Cytoskeleton; Microtubule; Mitosis; Nucleus; Polymorphism;
KW Reference proteome.
FT CHAIN 1 496 Fibronectin type III and SPRY domain-
FT containing protein 1.
FT /FTId=PRO_0000316537.
FT DOMAIN 105 162 COS.
FT DOMAIN 164 268 Fibronectin type-III.
FT DOMAIN 268 477 B30.2/SPRY.
FT COILED 4 99 Potential.
FT VARIANT 232 232 L -> V (in dbSNP:rs35139245).
FT /FTId=VAR_038385.
FT MUTAGEN 313 313 S->A: In mitosis, remained associated
FT with microtubules; when associated with
FT A-317; A-322 and A-324.
FT MUTAGEN 313 313 S->D: Reduced ability to associate with
FT microtubules; when associated with D-317;
FT E-322 and D-324.
FT MUTAGEN 317 317 S->A: In mitosis, remained associated
FT with microtubules; when associated with
FT A-313; A-322 and A-324.
FT MUTAGEN 317 317 S->D: Reduced ability to associate with
FT microtubules; when associated with D-313;
FT E-322 and D-324.
FT MUTAGEN 322 322 T->A: In mitosis, remained associated
FT with microtubules; when associated with
FT A-313; A-317 and A-324.
FT MUTAGEN 322 322 T->E: Reduced ability to associate with
FT microtubules; when associated with D-313;
FT D-317 and D-324.
FT MUTAGEN 324 324 S->A: In mitosis, remained associated
FT with microtubules; when associated with
FT A-313; A-317 and A-322.
FT MUTAGEN 324 324 S->D: Reduced ability to associate with
FT microtubules; when associated with D-313;
FT D-317 and E-322.
FT CONFLICT 295 295 G -> R (in Ref. 3; BAB13885).
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
//
ID FSD1_HUMAN Reviewed; 496 AA.
AC Q9BTV5; B2RDT0; Q9BXN0; Q9HAG4;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-JUN-2001, sequence version 1.
DT 22-JAN-2014, entry version 107.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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
RT chromosome 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
RT regulates microtubule organization and cytokinesis by using a GFP-
RT screening 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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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
RT project: 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;
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
RT 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.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: May be involved in microtubule organization and
CC stabilization.
CC -!- SUBUNIT: Oligomerization is required for binding to microtubules.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome. Nucleus. Cytoplasm. Cleavage
CC furrow. Note=Cell-cycle-dependent association with the centrosome.
CC Colocalizes with a subpopulation of microtubules. Does not
CC associates with microtubules during mitosis but reassociates with
CC microtubules during cytokinesis. Localizes to the central portions
CC of a small subset of microtubules in interphase cells and a
CC subpopulation of microtubules in the cleavage furrow, not present
CC in the mitotic spindle.
CC -!- TISSUE SPECIFICITY: Highly expressed in brain tissues, including
CC cerebellum, cerebral cortex, medulla, occipital pole, frontal
CC lobe, temporal lobe and putamen. Lower expression in spinal chord.
CC -!- DOMAIN: B30.2 box contains a microtubule-binding site.
CC -!- SIMILARITY: Contains 1 B30.2/SPRY domain.
CC -!- SIMILARITY: Contains 1 COS domain.
CC -!- SIMILARITY: Contains 1 fibronectin type-III domain.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
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 RefSeq; NP_077309.1; NM_024333.2.
DR UniGene; Hs.28144; -.
DR ProteinModelPortal; Q9BTV5; -.
DR IntAct; Q9BTV5; 2.
DR MINT; MINT-1368061; -.
DR STRING; 9606.ENSP00000221856; -.
DR PhosphoSite; Q9BTV5; -.
DR DMDM; 74733152; -.
DR PaxDb; Q9BTV5; -.
DR PRIDE; Q9BTV5; -.
DR DNASU; 79187; -.
DR Ensembl; ENST00000221856; ENSP00000221856; ENSG00000105255.
DR GeneID; 79187; -.
DR KEGG; hsa:79187; -.
DR UCSC; uc002lzy.2; human.
DR CTD; 79187; -.
DR GeneCards; GC19P004304; -.
DR HGNC; HGNC:13745; FSD1.
DR HPA; HPA043141; -.
DR MIM; 609828; gene.
DR neXtProt; NX_Q9BTV5; -.
DR PharmGKB; PA134882882; -.
DR eggNOG; NOG302398; -.
DR HOGENOM; HOG000231656; -.
DR HOVERGEN; HBG107931; -.
DR InParanoid; Q9BTV5; -.
DR OMA; ASWCIHL; -.
DR OrthoDB; EOG7W6WKF; -.
DR PhylomeDB; Q9BTV5; -.
DR GenomeRNAi; 79187; -.
DR NextBio; 68182; -.
DR PRO; PR:Q9BTV5; -.
DR ArrayExpress; Q9BTV5; -.
DR Bgee; Q9BTV5; -.
DR CleanEx; HS_FSD1; -.
DR Genevestigator; Q9BTV5; -.
DR GO; GO:0032154; C:cleavage furrow; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IDA:HPA.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0007067; P:mitosis; IEA:UniProtKB-KW.
DR Gene3D; 2.60.40.10; -; 1.
DR InterPro; IPR001870; B30.2/SPRY.
DR InterPro; IPR003649; Bbox_C.
DR InterPro; IPR008985; ConA-like_lec_gl_sf.
DR InterPro; IPR017903; COS_domain.
DR InterPro; IPR003961; Fibronectin_type3.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003877; SPRY_rcpt.
DR Pfam; PF00041; fn3; 1.
DR Pfam; PF00622; SPRY; 1.
DR SMART; SM00502; BBC; 1.
DR SMART; SM00060; FN3; 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; Complete proteome; Cytoplasm;
KW Cytoskeleton; Microtubule; Mitosis; Nucleus; Polymorphism;
KW Reference proteome.
FT CHAIN 1 496 Fibronectin type III and SPRY domain-
FT containing protein 1.
FT /FTId=PRO_0000316537.
FT DOMAIN 105 162 COS.
FT DOMAIN 164 268 Fibronectin type-III.
FT DOMAIN 268 477 B30.2/SPRY.
FT COILED 4 99 Potential.
FT VARIANT 232 232 L -> V (in dbSNP:rs35139245).
FT /FTId=VAR_038385.
FT MUTAGEN 313 313 S->A: In mitosis, remained associated
FT with microtubules; when associated with
FT A-317; A-322 and A-324.
FT MUTAGEN 313 313 S->D: Reduced ability to associate with
FT microtubules; when associated with D-317;
FT E-322 and D-324.
FT MUTAGEN 317 317 S->A: In mitosis, remained associated
FT with microtubules; when associated with
FT A-313; A-322 and A-324.
FT MUTAGEN 317 317 S->D: Reduced ability to associate with
FT microtubules; when associated with D-313;
FT E-322 and D-324.
FT MUTAGEN 322 322 T->A: In mitosis, remained associated
FT with microtubules; when associated with
FT A-313; A-317 and A-324.
FT MUTAGEN 322 322 T->E: Reduced ability to associate with
FT microtubules; when associated with D-313;
FT D-317 and D-324.
FT MUTAGEN 324 324 S->A: In mitosis, remained associated
FT with microtubules; when associated with
FT A-313; A-317 and A-322.
FT MUTAGEN 324 324 S->D: Reduced ability to associate with
FT microtubules; when associated with D-313;
FT D-317 and E-322.
FT CONFLICT 295 295 G -> R (in Ref. 3; BAB13885).
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
//
MIM
609828
*RECORD*
*FIELD* NO
609828
*FIELD* TI
*609828 FIBRONECTIN TYPE III AND SPRY DOMAINS-CONTAINING PROTEIN 1; FSD1
;;GLFND
*FIELD* TX
read more
CLONING
By EST database analysis and RACE of a fetal brain cDNA library,
Carim-Todd et al. (2001) cloned FSD1. The deduced 496-amino acid protein
has a calculated molecular mass of 55.8 kD. It contains an N-terminal
BBC domain (coiled-coil region downstream of B-box domains), a central
fibronectin (see 135600) type III domain, and a C-terminal SPRY domain.
FSD1 shares 92% amino acid identity with mouse Fsd1 and significant
similarity with its bovine and porcine paralogs. It also shares
significant similarity with FSD1NL (609829). Northern blot analysis of
several human tissues detected abundant expression of a major 1.8- to
2.0-kb transcript and minor 3.0- and 3.5-kb transcripts in brain only.
By screening a human fibrosarcoma cell line expression library to
identify microtubule-associated proteins, Manabe et al. (2002) cloned
FSD1, which they called GLFND. They identified several potential
phosphorylation sites in the protein.
GENE FUNCTION
Manabe et al. (2002) found that endogenous mammalian Fsd1 associated
with microtubules in several cell lines. Human FSD1 associated with a
subpopulation of microtubules that were acetylated, and expression of
FSD1 protected microtubules from depolymerizing agents. FSD1 with an
N-terminal deletion bound microtubules but altered their organization.
FSD1 dissociated from microtubules at the beginning of mitosis and
reassociated with them at cytokinesis. Ectopic expression of FSD1
inhibited cell division and cytokinesis in Chinese hamster ovary cells.
GENE STRUCTURE
Carim-Todd et al. (2001) determined that the FSD1 gene contains 13 exons
and spans about 19 kb.
MAPPING
By genomic sequence analysis, Carim-Todd et al. (2001) mapped the FSD1
gene to chromosome 19. Manabe et al. (2002) mapped the FSD1 gene to
chromosome 19p13.3.
*FIELD* RF
1. 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. 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.
*FIELD* CD
Patricia A. Hartz: 1/18/2006
*FIELD* ED
mgross: 03/22/2006
mgross: 1/18/2006
*RECORD*
*FIELD* NO
609828
*FIELD* TI
*609828 FIBRONECTIN TYPE III AND SPRY DOMAINS-CONTAINING PROTEIN 1; FSD1
;;GLFND
*FIELD* TX
read more
CLONING
By EST database analysis and RACE of a fetal brain cDNA library,
Carim-Todd et al. (2001) cloned FSD1. The deduced 496-amino acid protein
has a calculated molecular mass of 55.8 kD. It contains an N-terminal
BBC domain (coiled-coil region downstream of B-box domains), a central
fibronectin (see 135600) type III domain, and a C-terminal SPRY domain.
FSD1 shares 92% amino acid identity with mouse Fsd1 and significant
similarity with its bovine and porcine paralogs. It also shares
significant similarity with FSD1NL (609829). Northern blot analysis of
several human tissues detected abundant expression of a major 1.8- to
2.0-kb transcript and minor 3.0- and 3.5-kb transcripts in brain only.
By screening a human fibrosarcoma cell line expression library to
identify microtubule-associated proteins, Manabe et al. (2002) cloned
FSD1, which they called GLFND. They identified several potential
phosphorylation sites in the protein.
GENE FUNCTION
Manabe et al. (2002) found that endogenous mammalian Fsd1 associated
with microtubules in several cell lines. Human FSD1 associated with a
subpopulation of microtubules that were acetylated, and expression of
FSD1 protected microtubules from depolymerizing agents. FSD1 with an
N-terminal deletion bound microtubules but altered their organization.
FSD1 dissociated from microtubules at the beginning of mitosis and
reassociated with them at cytokinesis. Ectopic expression of FSD1
inhibited cell division and cytokinesis in Chinese hamster ovary cells.
GENE STRUCTURE
Carim-Todd et al. (2001) determined that the FSD1 gene contains 13 exons
and spans about 19 kb.
MAPPING
By genomic sequence analysis, Carim-Todd et al. (2001) mapped the FSD1
gene to chromosome 19. Manabe et al. (2002) mapped the FSD1 gene to
chromosome 19p13.3.
*FIELD* RF
1. 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. 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.
*FIELD* CD
Patricia A. Hartz: 1/18/2006
*FIELD* ED
mgross: 03/22/2006
mgross: 1/18/2006