ID FND3B_HUMAN Reviewed; 1204 AA. AC Q53EP0; B2RB36; B3KXR8; D3DNQ7; Q5U5T8; Q6PIJ3; Q6UXG1; Q6UXZ5; Q8IXB2; AC Q8NBU7; Q96D78; Q9H5I7; Q9NSQ8; DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-2007, sequence version 2. DT 27-MAR-2024, entry version 149. DE RecName: Full=Fibronectin type III domain-containing protein 3B; DE AltName: Full=Factor for adipocyte differentiation 104; DE AltName: Full=HCV NS5A-binding protein 37; GN Name=FNDC3B; Synonyms=FAD104, NS5ABP37; GN ORFNames=UNQ2421/PRO4979/PRO34274; 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] (ISOFORM 1), TISSUE SPECIFICITY, FUNCTION, AND RP VARIANT SER-179. RC TISSUE=Carcinoma; RX PubMed=15564382; DOI=10.1242/jcs.01546; RA Tominaga K., Johmura Y., Nishizuka M., Imagawa M.; RT "Fad24, a mammalian homolog of Noc3p, is a positive regulator in adipocyte RT differentiation."; RL J. Cell Sci. 117:6217-6226(2004). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), NUCLEOTIDE SEQUENCE RP [LARGE SCALE MRNA] OF 320-1204 (ISOFORM 1), AND VARIANT SER-179. RX PubMed=12975309; DOI=10.1101/gr.1293003; RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J., RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P., RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A., RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D., RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L., RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C., RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J., RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.; RT "The secreted protein discovery initiative (SPDI), a large-scale effort to RT identify novel human secreted and transmembrane proteins: a bioinformatics RT assessment."; RL Genome Res. 13:2265-2270(2003). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT SER-179. RC TISSUE=Placenta, and Trachea; 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] (ISOFORM 1). RC TISSUE=Kidney; RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.; RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT SER-179. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3), AND VARIANT RP SER-179. RC TISSUE=Lung, Skin, and Testis; 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 [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 403-1204 (ISOFORM 1). RC TISSUE=Placenta; RX PubMed=16303743; DOI=10.1093/dnares/12.2.117; RA Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J., RA Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S., RA Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y., RA Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S., RA Isogai T.; RT "Signal sequence and keyword trap in silico for selection of full-length RT human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA RT libraries."; RL DNA Res. 12:117-126(2005). RN [8] RP NUCLEOTIDE SEQUENCE [MRNA] OF 710-1204 (ISOFORM 1). RA Wang L., Li K., Cheng J.; RL Submitted (SEP-2002) to the EMBL/GenBank/DDBJ databases. RN [9] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 728-1204 (ISOFORM 1). RC TISSUE=Melanoma; RX PubMed=17974005; DOI=10.1186/1471-2164-8-399; RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., RA Wiemann S., Schupp I.; RT "The full-ORF clone resource of the German cDNA consortium."; RL BMC Genomics 8:399-399(2007). RN [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-208 AND SER-1163, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. 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 [11] 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 [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-208, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [13] RP VARIANT [LARGE SCALE ANALYSIS] SER-927. RX PubMed=16959974; DOI=10.1126/science.1133427; RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V., RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., RA Velculescu V.E.; RT "The consensus coding sequences of human breast and colorectal cancers."; RL Science 314:268-274(2006). CC -!- FUNCTION: May be a positive regulator of adipogenesis. CC {ECO:0000269|PubMed:15564382}. CC -!- INTERACTION: CC Q53EP0-3; Q8NFV4-4: ABHD11; NbExp=3; IntAct=EBI-10242151, EBI-12318443; CC Q53EP0-3; Q96I13: ABHD8; NbExp=3; IntAct=EBI-10242151, EBI-17180442; CC Q53EP0-3; Q5BKX5-3: ACTMAP; NbExp=3; IntAct=EBI-10242151, EBI-11976299; CC Q53EP0-3; Q8IZF2: ADGRF5; NbExp=3; IntAct=EBI-10242151, EBI-7600130; CC Q53EP0-3; Q9BXC9: BBS2; NbExp=3; IntAct=EBI-10242151, EBI-748297; CC Q53EP0-3; Q6AI39: BICRAL; NbExp=3; IntAct=EBI-10242151, EBI-1012434; CC Q53EP0-3; Q9NSI6-4: BRWD1; NbExp=3; IntAct=EBI-10242151, EBI-10693038; CC Q53EP0-3; Q5SWW7: C10orf55; NbExp=3; IntAct=EBI-10242151, EBI-12809220; CC Q53EP0-3; Q8WYQ4-2: C22orf15; NbExp=3; IntAct=EBI-10242151, EBI-12030460; CC Q53EP0-3; Q13557: CAMK2D; NbExp=3; IntAct=EBI-10242151, EBI-351018; CC Q53EP0-3; Q6PRD7: CEMP1; NbExp=3; IntAct=EBI-10242151, EBI-12907646; CC Q53EP0-3; A0PJW8: DAPL1; NbExp=3; IntAct=EBI-10242151, EBI-12840152; CC Q53EP0-3; Q9Y6W6: DUSP10; NbExp=3; IntAct=EBI-10242151, EBI-3443946; CC Q53EP0-3; Q86XJ1: GAS2L3; NbExp=3; IntAct=EBI-10242151, EBI-9248152; CC Q53EP0-3; Q9GZV7: HAPLN2; NbExp=3; IntAct=EBI-10242151, EBI-11956675; CC Q53EP0-3; Q96G42: KLHDC7B; NbExp=3; IntAct=EBI-10242151, EBI-9478422; CC Q53EP0-3; Q8IUC1: KRTAP11-1; NbExp=3; IntAct=EBI-10242151, EBI-1052037; CC Q53EP0-3; Q96JM7-2: L3MBTL3; NbExp=3; IntAct=EBI-10242151, EBI-11985629; CC Q53EP0-3; Q8WWY6: MBD3L1; NbExp=3; IntAct=EBI-10242151, EBI-12516603; CC Q53EP0-3; P59942: MCCD1; NbExp=3; IntAct=EBI-10242151, EBI-11987923; CC Q53EP0-3; Q14764: MVP; NbExp=3; IntAct=EBI-10242151, EBI-2816254; CC Q53EP0-3; O14561: NDUFAB1; NbExp=5; IntAct=EBI-10242151, EBI-1246261; CC Q53EP0-3; Q99570: PIK3R4; NbExp=3; IntAct=EBI-10242151, EBI-1046979; CC Q53EP0-3; Q7Z3K3: POGZ; NbExp=6; IntAct=EBI-10242151, EBI-1389308; CC Q53EP0-3; P78424: POU6F2; NbExp=3; IntAct=EBI-10242151, EBI-12029004; CC Q53EP0-3; P54646: PRKAA2; NbExp=3; IntAct=EBI-10242151, EBI-1383852; CC Q53EP0-3; Q04864-2: REL; NbExp=3; IntAct=EBI-10242151, EBI-10829018; CC Q53EP0-3; Q9BVN2: RUSC1; NbExp=3; IntAct=EBI-10242151, EBI-6257312; CC Q53EP0-3; Q6ZNM6: SPMIP10; NbExp=3; IntAct=EBI-10242151, EBI-18115728; CC Q53EP0-3; Q8WW14-2: SPMIP5; NbExp=3; IntAct=EBI-10242151, EBI-12831628; CC Q53EP0-3; Q99619: SPSB2; NbExp=3; IntAct=EBI-10242151, EBI-2323209; CC Q53EP0-3; Q8NEQ6: SRARP; NbExp=3; IntAct=EBI-10242151, EBI-17858294; CC Q53EP0-3; Q8N801-2: STPG4; NbExp=3; IntAct=EBI-10242151, EBI-12871202; CC Q53EP0-3; P51687: SUOX; NbExp=3; IntAct=EBI-10242151, EBI-3921347; CC Q53EP0-3; Q96M29: TEKT5; NbExp=3; IntAct=EBI-10242151, EBI-10239812; CC Q53EP0-3; Q96N21: TEPSIN; NbExp=3; IntAct=EBI-10242151, EBI-11139477; CC Q53EP0-3; Q9Y4I5-2: TESMIN; NbExp=3; IntAct=EBI-10242151, EBI-12840664; CC Q53EP0-3; A0A1B0GUV7: TEX48; NbExp=3; IntAct=EBI-10242151, EBI-18583507; CC Q53EP0-3; O94842: TOX4; NbExp=6; IntAct=EBI-10242151, EBI-948613; CC Q53EP0-3; Q12933: TRAF2; NbExp=3; IntAct=EBI-10242151, EBI-355744; CC Q53EP0-3; Q9UPQ4-2: TRIM35; NbExp=3; IntAct=EBI-10242151, EBI-17716262; CC Q53EP0-3; Q8IWZ5: TRIM42; NbExp=3; IntAct=EBI-10242151, EBI-5235829; CC Q53EP0-3; Q15645: TRIP13; NbExp=6; IntAct=EBI-10242151, EBI-358993; CC Q53EP0-3; Q5T6F2: UBAP2; NbExp=3; IntAct=EBI-10242151, EBI-2514383; CC Q53EP0-3; Q70EL1-9: USP54; NbExp=3; IntAct=EBI-10242151, EBI-11975223; CC Q53EP0-3; Q08AM6: VAC14; NbExp=3; IntAct=EBI-10242151, EBI-2107455; CC Q53EP0-3; Q96E35: ZMYND19; NbExp=3; IntAct=EBI-10242151, EBI-746595; CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass membrane CC protein {ECO:0000250}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=Q53EP0-1; Sequence=Displayed; CC Name=2; CC IsoId=Q53EP0-2; Sequence=VSP_024741, VSP_024742; CC Name=3; CC IsoId=Q53EP0-3; Sequence=VSP_024739, VSP_024740; CC -!- TISSUE SPECIFICITY: Predominantly expressed in white adipose tissue CC (WAT) especially in the stromal vascular cells. Expressed in adipocyte CC differentiable 3T3-L1 cells but not in the non-adipogenic cell line CC NIH-3T3. Expression increased in the early stage of adipogenesis. CC {ECO:0000269|PubMed:15564382}. CC -!- SIMILARITY: Belongs to the FNDC3 family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAH12204.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC Sequence=AAH33635.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC Sequence=AAQ88513.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC Sequence=AAQ88733.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC Sequence=BAB15639.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC Sequence=BAC11480.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AB098597; BAC53727.1; -; mRNA. DR EMBL; AY358146; AAQ88513.1; ALT_INIT; mRNA. DR EMBL; AY358367; AAQ88733.1; ALT_INIT; mRNA. DR EMBL; AK027052; BAB15639.1; ALT_INIT; mRNA. DR EMBL; AK075220; BAC11480.1; ALT_INIT; mRNA. DR EMBL; AK127826; BAG54580.1; -; mRNA. DR EMBL; AK314478; BAG37083.1; -; mRNA. DR EMBL; AK223599; BAD97319.1; -; mRNA. DR EMBL; CH471052; EAW78476.1; -; Genomic_DNA. DR EMBL; CH471052; EAW78472.1; -; Genomic_DNA. DR EMBL; CH471052; EAW78474.1; -; Genomic_DNA. DR EMBL; CH471052; EAW78475.1; -; Genomic_DNA. DR EMBL; BC012204; AAH12204.1; ALT_INIT; mRNA. DR EMBL; BC033635; AAH33635.1; ALT_INIT; mRNA. DR EMBL; BC039297; AAH39297.1; -; mRNA. DR EMBL; AF543840; AAN65261.1; -; mRNA. DR EMBL; AL157482; CAB75672.1; -; mRNA. DR CCDS; CCDS3217.1; -. [Q53EP0-1] DR PIR; T46917; T46917. DR RefSeq; NP_001128567.1; NM_001135095.1. [Q53EP0-1] DR RefSeq; NP_073600.3; NM_022763.3. [Q53EP0-1] DR AlphaFoldDB; Q53EP0; -. DR SMR; Q53EP0; -. DR BioGRID; 122288; 105. DR IntAct; Q53EP0; 66. DR MINT; Q53EP0; -. DR STRING; 9606.ENSP00000411242; -. DR GlyGen; Q53EP0; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q53EP0; -. DR PhosphoSitePlus; Q53EP0; -. DR SwissPalm; Q53EP0; -. DR BioMuta; FNDC3B; -. DR DMDM; 146286181; -. DR EPD; Q53EP0; -. DR jPOST; Q53EP0; -. DR MassIVE; Q53EP0; -. DR MaxQB; Q53EP0; -. DR PaxDb; 9606-ENSP00000338523; -. DR PeptideAtlas; Q53EP0; -. DR ProteomicsDB; 62442; -. [Q53EP0-1] DR ProteomicsDB; 62443; -. [Q53EP0-2] DR ProteomicsDB; 62444; -. [Q53EP0-3] DR Pumba; Q53EP0; -. DR Antibodypedia; 2120; 150 antibodies from 23 providers. DR DNASU; 64778; -. DR Ensembl; ENST00000336824.8; ENSP00000338523.4; ENSG00000075420.13. [Q53EP0-1] DR Ensembl; ENST00000415807.7; ENSP00000411242.2; ENSG00000075420.13. [Q53EP0-1] DR Ensembl; ENST00000416957.5; ENSP00000389094.1; ENSG00000075420.13. [Q53EP0-1] DR Ensembl; ENST00000421757.5; ENSP00000408496.1; ENSG00000075420.13. [Q53EP0-3] DR Ensembl; ENST00000423424.5; ENSP00000392471.1; ENSG00000075420.13. [Q53EP0-3] DR GeneID; 64778; -. DR KEGG; hsa:64778; -. DR MANE-Select; ENST00000415807.7; ENSP00000411242.2; NM_022763.4; NP_073600.3. DR UCSC; uc003fhx.4; human. [Q53EP0-1] DR AGR; HGNC:24670; -. DR CTD; 64778; -. DR DisGeNET; 64778; -. DR GeneCards; FNDC3B; -. DR HGNC; HGNC:24670; FNDC3B. DR HPA; ENSG00000075420; Low tissue specificity. DR MIM; 611909; gene. DR neXtProt; NX_Q53EP0; -. DR OpenTargets; ENSG00000075420; -. DR PharmGKB; PA134936830; -. DR VEuPathDB; HostDB:ENSG00000075420; -. DR eggNOG; KOG0613; Eukaryota. DR GeneTree; ENSGT00940000157005; -. DR HOGENOM; CLU_2739328_0_0_1; -. DR InParanoid; Q53EP0; -. DR OMA; DTHFEIR; -. DR OrthoDB; 316463at2759; -. DR PhylomeDB; Q53EP0; -. DR TreeFam; TF316401; -. DR PathwayCommons; Q53EP0; -. DR SignaLink; Q53EP0; -. DR BioGRID-ORCS; 64778; 52 hits in 1182 CRISPR screens. DR ChiTaRS; FNDC3B; human. DR GenomeRNAi; 64778; -. DR Pharos; Q53EP0; Tbio. DR PRO; PR:Q53EP0; -. DR Proteomes; UP000005640; Chromosome 3. DR RNAct; Q53EP0; Protein. DR Bgee; ENSG00000075420; Expressed in cartilage tissue and 204 other cell types or tissues. DR ExpressionAtlas; Q53EP0; baseline and differential. DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell. DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB. DR CDD; cd00063; FN3; 9. DR Gene3D; 2.60.40.10; Immunoglobulins; 9. DR InterPro; IPR003961; FN3_dom. DR InterPro; IPR036116; FN3_sf. DR InterPro; IPR013783; Ig-like_fold. DR PANTHER; PTHR24099; E3 UBIQUITIN-PROTEIN LIGASE TRIM36-RELATED; 1. DR PANTHER; PTHR24099:SF11; FIBRONECTIN TYPE III DOMAIN-CONTAINING 3BA-RELATED; 1. DR Pfam; PF00041; fn3; 9. DR PRINTS; PR00014; FNTYPEIII. DR SMART; SM00060; FN3; 9. DR SUPFAM; SSF49265; Fibronectin type III; 5. DR PROSITE; PS50853; FN3; 9. DR Genevisible; Q53EP0; HS. PE 1: Evidence at protein level; KW Alternative splicing; Membrane; Phosphoprotein; Reference proteome; Repeat; KW Transmembrane; Transmembrane helix. FT CHAIN 1..1204 FT /note="Fibronectin type III domain-containing protein 3B" FT /id="PRO_0000284891" FT TRANSMEM 1182..1202 FT /note="Helical" FT /evidence="ECO:0000255" FT DOMAIN 278..377 FT /note="Fibronectin type-III 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316" FT DOMAIN 381..473 FT /note="Fibronectin type-III 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316" FT DOMAIN 477..570 FT /note="Fibronectin type-III 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316" FT DOMAIN 574..669 FT /note="Fibronectin type-III 4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316" FT DOMAIN 673..765 FT /note="Fibronectin type-III 5" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316" FT DOMAIN 766..859 FT /note="Fibronectin type-III 6" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316" FT DOMAIN 871..957 FT /note="Fibronectin type-III 7" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316" FT DOMAIN 958..1052 FT /note="Fibronectin type-III 8" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316" FT DOMAIN 1056..1153 FT /note="Fibronectin type-III 9" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316" FT REGION 185..215 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 228..262 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 186..203 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 245..262 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 208 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:23186163" FT MOD_RES 393 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q6NWW9" FT MOD_RES 1163 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT VAR_SEQ 63..71 FT /note="GPAEVPMMS -> DEVVKRACD (in isoform 3)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_024739" FT VAR_SEQ 72..1204 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_024740" FT VAR_SEQ 618..629 FT /note="ANQWEVAYSGSA -> GEVFGNCFIQIQ (in isoform 2)" FT /evidence="ECO:0000303|PubMed:12975309" FT /id="VSP_024741" FT VAR_SEQ 630..1204 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:12975309" FT /id="VSP_024742" FT VARIANT 179 FT /note="T -> S (in dbSNP:rs7652177)" FT /evidence="ECO:0000269|PubMed:12975309, FT ECO:0000269|PubMed:14702039, ECO:0000269|PubMed:15489334, FT ECO:0000269|PubMed:15564382, ECO:0000269|Ref.5" FT /id="VAR_031856" FT VARIANT 927 FT /note="P -> S (in a breast cancer sample; somatic FT mutation)" FT /evidence="ECO:0000269|PubMed:16959974" FT /id="VAR_035921" FT VARIANT 1080 FT /note="M -> V (in dbSNP:rs2276806)" FT /id="VAR_047814" FT CONFLICT 37 FT /note="Q -> H (in Ref. 2; AAQ88733)" FT /evidence="ECO:0000305" FT CONFLICT 208 FT /note="S -> R (in Ref. 1; BAC53727)" FT /evidence="ECO:0000305" FT CONFLICT 212 FT /note="S -> A (in Ref. 1; BAC53727)" FT /evidence="ECO:0000305" FT CONFLICT 360 FT /note="N -> D (in Ref. 3; BAG37083)" FT /evidence="ECO:0000305" FT CONFLICT 393 FT /note="S -> G (in Ref. 3; BAG37083)" FT /evidence="ECO:0000305" FT CONFLICT 448 FT /note="T -> A (in Ref. 3; BAG37083)" FT /evidence="ECO:0000305" FT CONFLICT 481 FT /note="P -> L (in Ref. 2; AAQ88513)" FT /evidence="ECO:0000305" FT CONFLICT 545 FT /note="K -> T (in Ref. 1; BAC53727)" FT /evidence="ECO:0000305" FT CONFLICT 676 FT /note="P -> S (in Ref. 4; BAD97319)" FT /evidence="ECO:0000305" FT CONFLICT 854 FT /note="C -> W (in Ref. 6; AAH39297)" FT /evidence="ECO:0000305" FT CONFLICT 895 FT /note="N -> D (in Ref. 3; BAC11480)" FT /evidence="ECO:0000305" FT CONFLICT 1067 FT /note="G -> V (in Ref. 2; AAQ88513)" FT /evidence="ECO:0000305" FT CONFLICT 1083 FT /note="D -> G (in Ref. 3; BAG37083)" FT /evidence="ECO:0000305" SQ SEQUENCE 1204 AA; 132888 MW; 7E883F4566276CE7 CRC64; MYVTMMMTDQ IPLELPPLLN GEVAMMPHLV NGDAAQQVIL VQVNPGETFT IRAEDGTLQC IQGPAEVPMM SPNGSIPPIH VPPGYISQVI EDSTGVRRVV VTPQSPECYP PSYPSAMSPT HHLPPYLTHH PHFIHNSHTA YYPPVTGPGD MPPQFFPQHH LPHTIYGEQE IIPFYGMSTY ITREDQYSKP PHKKLKDRQI DRQNRLNSPP SSIYKSSCTT VYNGYGKGHS GGSGGGGSGS GPGIKKTERR ARSSPKSNDS DLQEYELEVK RVQDILSGIE KPQVSNIQAR AVVLSWAPPV GLSCGPHSGL SFPYSYEVAL SDKGRDGKYK IIYSGEELEC NLKDLRPATD YHVRVYAMYN SVKGSCSEPV SFTTHSCAPE CPFPPKLAHR SKSSLTLQWK APIDNGSKIT NYLLEWDEGK RNSGFRQCFF GSQKHCKLTK LCPAMGYTFR LAARNDIGTS GYSQEVVCYT LGNIPQMPSA PRLVRAGITW VTLQWSKPEG CSPEEVITYT LEIQEDENDN LFHPKYTGED LTCTVKNLKR STQYKFRLTA SNTEGKSCPS EVLVCTTSPD RPGPPTRPLV KGPVTSHGFS VKWDPPKDNG GSEILKYLLE ITDGNSEANQ WEVAYSGSAT EYTFTHLKPG TLYKLRACCI STGGHSQCSE SLPVRTLSIA PGQCRPPRVL GRPKHKEVHL EWDVPASESG CEVSEYSVEM TEPEDVASEV YHGPELECTV GNLLPGTVYR FRVRALNDGG YGPYSDVSEI TTAAGPPGQC KAPCISCTPD GCVLVGWESP DSSGADISEY RLEWGEDEES LELIYHGTDT RFEIRDLLPA AQYCCRLQAF NQAGAGPYSE LVLCQTPASA PDPVSTLCVL EEEPLDAYPD SPSACLVLNW EEPCNNGSEI LAYTIDLGDT SITVGNTTMH VMKDLLPETT YRIRIQAINE IGAGPFSQFI KAKTRPLPPL PPRLECAAAG PQSLKLKWGD SNSKTHAAED IVYTLQLEDR NKRFISIYRG PSHTYKVQRL TEFTCYSFRI QAASEAGEGP FSETYTFSTT KSVPPTIKAP RVTQLEGNSC EILWETVPSM KGDPVNYILQ VLVGRESEYK QVYKGEEATF QISGLQTNTD YRFRVCACRR CLDTSQELSG AFSPSAAFVL QRSEVMLTGD MGSLDDPKMK SMMPTDEQFA AIIVLGFATL SILFAFILQY FLMK //