Full text data of FSD1L
FSD1L
(CCDC10, CSDUFD1, FSD1CL, FSD1NL)
[Confidence: low (only semi-automatic identification from reviews)]
FSD1-like protein (Coiled-coil domain-containing protein 10; FSD1 N-terminal-like protein)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
FSD1-like protein (Coiled-coil domain-containing protein 10; FSD1 N-terminal-like protein)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q9BXM9
ID FSD1L_HUMAN Reviewed; 530 AA.
AC Q9BXM9; A2A338; A6NKH7; B7Z5S6; B7Z5W3; Q5T879; Q5T880;
DT 23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
read moreDT 10-AUG-2010, sequence version 2.
DT 22-JAN-2014, entry version 91.
DE RecName: Full=FSD1-like protein;
DE AltName: Full=Coiled-coil domain-containing protein 10;
DE AltName: Full=FSD1 N-terminal-like protein;
GN Name=FSD1L; Synonyms=CCDC10, CSDUFD1, FSD1CL, FSD1NL;
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] (ISOFORM 3).
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 [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E.,
RA Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S.,
RA Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R.,
RA Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P.,
RA Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W.,
RA Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G.,
RA Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M.,
RA Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W.,
RA Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A.,
RA Frankland J.A., French L., Fricker D.G., Garner P., Garnett J.,
RA Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C.,
RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M.,
RA Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S.,
RA McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J.,
RA Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R.,
RA Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M.,
RA Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M.,
RA Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A.,
RA Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P.,
RA Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W.,
RA Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S.,
RA Rogers J., Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-523, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-520, AND MASS
RP SPECTROMETRY.
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1 (ISOFORMS 2 AND 3), AND
RP MASS SPECTROMETRY.
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9BXM9-1; Sequence=Displayed;
CC Note=No experimental confirmation available;
CC Name=2;
CC IsoId=Q9BXM9-2; Sequence=VSP_039645;
CC Note=No experimental confirmation available. Contains a
CC N-acetylmethionine at position 1;
CC Name=3;
CC IsoId=Q9BXM9-3; Sequence=VSP_039645, VSP_039646, VSP_039647;
CC Note=Due to intron retention. Contains a N-acetylmethionine at
CC position 1;
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; AF316830; AAK26748.1; -; mRNA.
DR EMBL; AK299350; BAH13012.1; -; mRNA.
DR EMBL; AK299491; BAH13049.1; -; mRNA.
DR EMBL; AL161627; CAI13072.1; -; Genomic_DNA.
DR EMBL; AL161627; CAI13073.2; -; Genomic_DNA.
DR EMBL; AL158070; CAI13073.2; JOINED; Genomic_DNA.
DR EMBL; AL158070; CAM14451.1; -; Genomic_DNA.
DR EMBL; AL161627; CAM14451.1; JOINED; Genomic_DNA.
DR RefSeq; NP_001138785.1; NM_001145313.1.
DR RefSeq; NP_114125.1; NM_031919.3.
DR RefSeq; XP_005252316.1; XM_005252259.1.
DR UniGene; Hs.136901; -.
DR ProteinModelPortal; Q9BXM9; -.
DR SMR; Q9BXM9; 191-308, 374-488.
DR IntAct; Q9BXM9; 1.
DR STRING; 9606.ENSP00000417492; -.
DR PhosphoSite; Q9BXM9; -.
DR DMDM; 302393701; -.
DR PaxDb; Q9BXM9; -.
DR PRIDE; Q9BXM9; -.
DR DNASU; 83856; -.
DR Ensembl; ENST00000374710; ENSP00000363842; ENSG00000106701.
DR Ensembl; ENST00000374716; ENSP00000363848; ENSG00000106701.
DR Ensembl; ENST00000481272; ENSP00000417492; ENSG00000106701.
DR Ensembl; ENST00000484973; ENSP00000419691; ENSG00000106701.
DR GeneID; 83856; -.
DR KEGG; hsa:83856; -.
DR UCSC; uc011lvv.1; human.
DR CTD; 83856; -.
DR GeneCards; GC09P108210; -.
DR HGNC; HGNC:13753; FSD1L.
DR HPA; HPA035138; -.
DR MIM; 609829; gene.
DR neXtProt; NX_Q9BXM9; -.
DR PharmGKB; PA26931; -.
DR eggNOG; NOG302398; -.
DR HOGENOM; HOG000231656; -.
DR HOVERGEN; HBG107931; -.
DR OMA; QSQLSQC; -.
DR GenomeRNAi; 83856; -.
DR NextBio; 35460755; -.
DR PRO; PR:Q9BXM9; -.
DR ArrayExpress; Q9BXM9; -.
DR Bgee; Q9BXM9; -.
DR CleanEx; HS_FSD1L; -.
DR Genevestigator; Q9BXM9; -.
DR Gene3D; 2.60.40.10; -; 1.
DR InterPro; IPR001870; B30.2/SPRY.
DR InterPro; IPR003879; Butyrophylin.
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 PRINTS; PR01407; BUTYPHLNCDUF.
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 Acetylation; Alternative splicing; Coiled coil; Complete proteome;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1 530 FSD1-like protein.
FT /FTId=PRO_0000089405.
FT DOMAIN 137 194 COS.
FT DOMAIN 196 300 Fibronectin type-III.
FT DOMAIN 300 506 B30.2/SPRY.
FT COILED 102 141 Potential.
FT MOD_RES 520 520 Phosphoserine.
FT MOD_RES 523 523 Phosphoserine.
FT VAR_SEQ 6 37 Missing (in isoform 2 and isoform 3).
FT /FTId=VSP_039645.
FT VAR_SEQ 148 177 AARQIKDRVTMASAFRLSLKPKVSDNMTHL -> VHKNCIN
FT TLNKGSCIFKKAFLFFFSFGFLY (in isoform 3).
FT /FTId=VSP_039646.
FT VAR_SEQ 178 530 Missing (in isoform 3).
FT /FTId=VSP_039647.
FT CONFLICT 39 39 A -> S (in Ref. 2; BAH13012).
FT CONFLICT 342 342 Missing (in Ref. 2; BAH13049).
SQ SEQUENCE 530 AA; 59578 MW; B2AC94D87F6B6DA1 CRC64;
MDSQKYCFKE NENVTVDKAC FLISNITIGP ESINLQQEAL QRIISTLANK NDEIQNFIDT
LHHTLKGVQE NSSNILSELD EEFDSLYSIL DEVKESMINC IKQEQARKSQ ELQSQISQCN
NALENSEELL EFATRSLDIK EPEEFSKAAR QIKDRVTMAS AFRLSLKPKV SDNMTHLMVD
FSQERQMLQT LKFLPVPKAP EIDPVECLVA DNSVTVAWRM PEEDNKIDHF ILEHRKTNFD
GLPRVKDERC WEIIDNIKGT EYTLSGLKFD SKYMNFRVRA CNKAVAGEYS DPVTLETKAL
NFNLDNSSSH LNLKVEDTCV EWDPTGGKGQ ESKIKGKENK GRSGTPSPKR TSVGSRPPAV
RGSRDRFTGE SYTVLGDTAI ESGQHYWEVK AQKDCKSYSV GVAYKTLGKF DQLGKTNTSW
CIHVNNWLQN TFAAKHNNKV KALDVTVPEK IGVFCDFDGG QLSFYDANSK QLLYSFKTKF
TQPVLPGFMV WCGGLSLSTG MQVPSAVRTL QKSENGMTGS ASSLNNVVTQ
//
ID FSD1L_HUMAN Reviewed; 530 AA.
AC Q9BXM9; A2A338; A6NKH7; B7Z5S6; B7Z5W3; Q5T879; Q5T880;
DT 23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
read moreDT 10-AUG-2010, sequence version 2.
DT 22-JAN-2014, entry version 91.
DE RecName: Full=FSD1-like protein;
DE AltName: Full=Coiled-coil domain-containing protein 10;
DE AltName: Full=FSD1 N-terminal-like protein;
GN Name=FSD1L; Synonyms=CCDC10, CSDUFD1, FSD1CL, FSD1NL;
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] (ISOFORM 3).
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 [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E.,
RA Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S.,
RA Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R.,
RA Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P.,
RA Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W.,
RA Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G.,
RA Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M.,
RA Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W.,
RA Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A.,
RA Frankland J.A., French L., Fricker D.G., Garner P., Garnett J.,
RA Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C.,
RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M.,
RA Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S.,
RA McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J.,
RA Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R.,
RA Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M.,
RA Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M.,
RA Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A.,
RA Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P.,
RA Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W.,
RA Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S.,
RA Rogers J., Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-523, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-520, AND MASS
RP SPECTROMETRY.
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1 (ISOFORMS 2 AND 3), AND
RP MASS SPECTROMETRY.
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9BXM9-1; Sequence=Displayed;
CC Note=No experimental confirmation available;
CC Name=2;
CC IsoId=Q9BXM9-2; Sequence=VSP_039645;
CC Note=No experimental confirmation available. Contains a
CC N-acetylmethionine at position 1;
CC Name=3;
CC IsoId=Q9BXM9-3; Sequence=VSP_039645, VSP_039646, VSP_039647;
CC Note=Due to intron retention. Contains a N-acetylmethionine at
CC position 1;
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; AF316830; AAK26748.1; -; mRNA.
DR EMBL; AK299350; BAH13012.1; -; mRNA.
DR EMBL; AK299491; BAH13049.1; -; mRNA.
DR EMBL; AL161627; CAI13072.1; -; Genomic_DNA.
DR EMBL; AL161627; CAI13073.2; -; Genomic_DNA.
DR EMBL; AL158070; CAI13073.2; JOINED; Genomic_DNA.
DR EMBL; AL158070; CAM14451.1; -; Genomic_DNA.
DR EMBL; AL161627; CAM14451.1; JOINED; Genomic_DNA.
DR RefSeq; NP_001138785.1; NM_001145313.1.
DR RefSeq; NP_114125.1; NM_031919.3.
DR RefSeq; XP_005252316.1; XM_005252259.1.
DR UniGene; Hs.136901; -.
DR ProteinModelPortal; Q9BXM9; -.
DR SMR; Q9BXM9; 191-308, 374-488.
DR IntAct; Q9BXM9; 1.
DR STRING; 9606.ENSP00000417492; -.
DR PhosphoSite; Q9BXM9; -.
DR DMDM; 302393701; -.
DR PaxDb; Q9BXM9; -.
DR PRIDE; Q9BXM9; -.
DR DNASU; 83856; -.
DR Ensembl; ENST00000374710; ENSP00000363842; ENSG00000106701.
DR Ensembl; ENST00000374716; ENSP00000363848; ENSG00000106701.
DR Ensembl; ENST00000481272; ENSP00000417492; ENSG00000106701.
DR Ensembl; ENST00000484973; ENSP00000419691; ENSG00000106701.
DR GeneID; 83856; -.
DR KEGG; hsa:83856; -.
DR UCSC; uc011lvv.1; human.
DR CTD; 83856; -.
DR GeneCards; GC09P108210; -.
DR HGNC; HGNC:13753; FSD1L.
DR HPA; HPA035138; -.
DR MIM; 609829; gene.
DR neXtProt; NX_Q9BXM9; -.
DR PharmGKB; PA26931; -.
DR eggNOG; NOG302398; -.
DR HOGENOM; HOG000231656; -.
DR HOVERGEN; HBG107931; -.
DR OMA; QSQLSQC; -.
DR GenomeRNAi; 83856; -.
DR NextBio; 35460755; -.
DR PRO; PR:Q9BXM9; -.
DR ArrayExpress; Q9BXM9; -.
DR Bgee; Q9BXM9; -.
DR CleanEx; HS_FSD1L; -.
DR Genevestigator; Q9BXM9; -.
DR Gene3D; 2.60.40.10; -; 1.
DR InterPro; IPR001870; B30.2/SPRY.
DR InterPro; IPR003879; Butyrophylin.
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 PRINTS; PR01407; BUTYPHLNCDUF.
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 Acetylation; Alternative splicing; Coiled coil; Complete proteome;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1 530 FSD1-like protein.
FT /FTId=PRO_0000089405.
FT DOMAIN 137 194 COS.
FT DOMAIN 196 300 Fibronectin type-III.
FT DOMAIN 300 506 B30.2/SPRY.
FT COILED 102 141 Potential.
FT MOD_RES 520 520 Phosphoserine.
FT MOD_RES 523 523 Phosphoserine.
FT VAR_SEQ 6 37 Missing (in isoform 2 and isoform 3).
FT /FTId=VSP_039645.
FT VAR_SEQ 148 177 AARQIKDRVTMASAFRLSLKPKVSDNMTHL -> VHKNCIN
FT TLNKGSCIFKKAFLFFFSFGFLY (in isoform 3).
FT /FTId=VSP_039646.
FT VAR_SEQ 178 530 Missing (in isoform 3).
FT /FTId=VSP_039647.
FT CONFLICT 39 39 A -> S (in Ref. 2; BAH13012).
FT CONFLICT 342 342 Missing (in Ref. 2; BAH13049).
SQ SEQUENCE 530 AA; 59578 MW; B2AC94D87F6B6DA1 CRC64;
MDSQKYCFKE NENVTVDKAC FLISNITIGP ESINLQQEAL QRIISTLANK NDEIQNFIDT
LHHTLKGVQE NSSNILSELD EEFDSLYSIL DEVKESMINC IKQEQARKSQ ELQSQISQCN
NALENSEELL EFATRSLDIK EPEEFSKAAR QIKDRVTMAS AFRLSLKPKV SDNMTHLMVD
FSQERQMLQT LKFLPVPKAP EIDPVECLVA DNSVTVAWRM PEEDNKIDHF ILEHRKTNFD
GLPRVKDERC WEIIDNIKGT EYTLSGLKFD SKYMNFRVRA CNKAVAGEYS DPVTLETKAL
NFNLDNSSSH LNLKVEDTCV EWDPTGGKGQ ESKIKGKENK GRSGTPSPKR TSVGSRPPAV
RGSRDRFTGE SYTVLGDTAI ESGQHYWEVK AQKDCKSYSV GVAYKTLGKF DQLGKTNTSW
CIHVNNWLQN TFAAKHNNKV KALDVTVPEK IGVFCDFDGG QLSFYDANSK QLLYSFKTKF
TQPVLPGFMV WCGGLSLSTG MQVPSAVRTL QKSENGMTGS ASSLNNVVTQ
//
MIM
609829
*RECORD*
*FIELD* NO
609829
*FIELD* TI
*609829 FSD1 N-TERMINUS-LIKE PROTEIN; FSD1NL
;;FSD1-LIKE PROTEIN; FSD1L;;
MID1-RELATED PROTEIN 1; MIR1;;
read moreCOILED-COIL DOMAIN-CONTAINING PROTEIN 10; CCDC10
*FIELD* TX
CLONING
By screening an osteosarcoma cDNA expression library to identify
microtubule-associated proteins, Stein et al. (2002) cloned FSD1NL,
which they called MIR1. The deduced 496-amino acid protein contains a
coiled-coil region, followed by a fibronectin type-3 (FN3; see 135600)
domain and a C-terminal B30.2 box, all of which are believed to be
protein-protein interaction domains. MIR1 also has a 20-amino acid
region between the FN3 and B30.2 domains that has multiple consensus
sequences for proline-directed cyclin-dependent serine/threonine kinases
(see CDK5; 123831). Northern blot analysis of several human tissues
detected MIR1 expression only in brain. RNA dot blot analysis detected
MIR1 in all areas of adult brain tested, but little expression was found
in fetal brain. MIR1 was also expressed at lower levels in fetal and
adult thymus, pituitary, and testis, and weakly in several other
tissues. No expression was detected in cardiac or skeletal muscle.
Western blot analysis detected endogenous MIR1 at an apparent molecular
mass of 65 kD in a human osteosarcoma cell line and in rat and cow brain
cytosol.
GENE FUNCTION
Stein et al. (2002) found that association of endogenous Mir1 with
centrosomes was dependent on the stage of the cell cycle in baby hamster
kidney cells. Mir1 dissociated from centrosomes at the G2/M transition
and was recruited back to spindle poles during anaphase. When
overexpressed during interphase, human MIR1 bound along microtubule
filaments, which became stabilized, bundled, and detached from the
centrosome. When overexpressed during mitosis, MIR1 dissociated from
microtubules, but it still affected the normally focused localization of
gamma-tubulin (TUBG1; 191135) in spindle poles. Tight binding to
microtubules in interphase appeared to require an oligomeric state of
MIR1, and phosphorylation in mitosis at cyclin-dependent kinase sites
weakened the interaction.
MAPPING
By genomic sequence analysis, Carim-Todd et al. (2001) mapped the FSD1NL
gene to chromosome 9q31.
*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. 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.
*FIELD* CD
Patricia A. Hartz: 1/18/2006
*FIELD* ED
mgross: 01/18/2006
mgross: 1/18/2006
*RECORD*
*FIELD* NO
609829
*FIELD* TI
*609829 FSD1 N-TERMINUS-LIKE PROTEIN; FSD1NL
;;FSD1-LIKE PROTEIN; FSD1L;;
MID1-RELATED PROTEIN 1; MIR1;;
read moreCOILED-COIL DOMAIN-CONTAINING PROTEIN 10; CCDC10
*FIELD* TX
CLONING
By screening an osteosarcoma cDNA expression library to identify
microtubule-associated proteins, Stein et al. (2002) cloned FSD1NL,
which they called MIR1. The deduced 496-amino acid protein contains a
coiled-coil region, followed by a fibronectin type-3 (FN3; see 135600)
domain and a C-terminal B30.2 box, all of which are believed to be
protein-protein interaction domains. MIR1 also has a 20-amino acid
region between the FN3 and B30.2 domains that has multiple consensus
sequences for proline-directed cyclin-dependent serine/threonine kinases
(see CDK5; 123831). Northern blot analysis of several human tissues
detected MIR1 expression only in brain. RNA dot blot analysis detected
MIR1 in all areas of adult brain tested, but little expression was found
in fetal brain. MIR1 was also expressed at lower levels in fetal and
adult thymus, pituitary, and testis, and weakly in several other
tissues. No expression was detected in cardiac or skeletal muscle.
Western blot analysis detected endogenous MIR1 at an apparent molecular
mass of 65 kD in a human osteosarcoma cell line and in rat and cow brain
cytosol.
GENE FUNCTION
Stein et al. (2002) found that association of endogenous Mir1 with
centrosomes was dependent on the stage of the cell cycle in baby hamster
kidney cells. Mir1 dissociated from centrosomes at the G2/M transition
and was recruited back to spindle poles during anaphase. When
overexpressed during interphase, human MIR1 bound along microtubule
filaments, which became stabilized, bundled, and detached from the
centrosome. When overexpressed during mitosis, MIR1 dissociated from
microtubules, but it still affected the normally focused localization of
gamma-tubulin (TUBG1; 191135) in spindle poles. Tight binding to
microtubules in interphase appeared to require an oligomeric state of
MIR1, and phosphorylation in mitosis at cyclin-dependent kinase sites
weakened the interaction.
MAPPING
By genomic sequence analysis, Carim-Todd et al. (2001) mapped the FSD1NL
gene to chromosome 9q31.
*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. 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.
*FIELD* CD
Patricia A. Hartz: 1/18/2006
*FIELD* ED
mgross: 01/18/2006
mgross: 1/18/2006