F107A_HUMAN
ID F107A_HUMAN Reviewed; 144 AA.
AC O95990; B3KNQ4; B7ZAY5; J3KR61; Q96NH4;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Actin-associated protein FAM107A {ECO:0000305};
DE AltName: Full=Down-regulated in renal cell carcinoma 1 {ECO:0000303|PubMed:10564580};
DE AltName: Full=Protein TU3A {ECO:0000303|PubMed:10702698};
GN Name=FAM107A {ECO:0000312|HGNC:HGNC:30827};
GN Synonyms=DRR1 {ECO:0000303|PubMed:10564580}, TU3A;
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), FUNCTION, SUBCELLULAR LOCATION,
RP TISSUE SPECIFICITY, AND VARIANTS MET-15 AND LEU-19.
RC TISSUE=Ovary;
RX PubMed=10564580;
RX DOI=10.1002/(sici)1098-2264(200001)27:1<1::aid-gcc1>3.0.co;2-6;
RA Wang L., Darling J., Zhang J.-S., Liu W., Qian J., Bostwick D.,
RA Hartmann L., Jenkins R., Bardenhauer W., Schutte J., Opalka B., Smith D.I.;
RT "Loss of expression of the DRR1 gene at chromosomal segment 3p21.1 in renal
RT cell carcinoma.";
RL Genes Chromosomes Cancer 27:1-10(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=10702698; DOI=10.1159/000015452;
RA Yamato T., Orikasa K., Fukushige S., Orikasa S., Horii A.;
RT "Isolation and characterization of the novel gene, TU3A, in a commonly
RT deleted region on 3p14.3->p14.2 in renal cell carcinoma.";
RL Cytogenet. Cell Genet. 87:291-295(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=11230166; DOI=10.1101/gr.gr1547r;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J.,
RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W.,
RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B.,
RA Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and analysis of
RT 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2; 3 AND 4).
RC TISSUE=Fetal brain;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [7]
RP SUBCELLULAR LOCATION.
RX PubMed=11256614; DOI=10.1093/embo-reports/kvd058;
RA Simpson J.C., Wellenreuther R., Poustka A., Pepperkok R., Wiemann S.;
RT "Systematic subcellular localization of novel proteins identified by large-
RT scale cDNA sequencing.";
RL EMBO Rep. 1:287-292(2000).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND MUTAGENESIS OF
RP 48-HIS--GLU-50; 65-PRO-GLU-66 AND 122-PRO-GLU-123.
RX PubMed=20543869; DOI=10.1038/onc.2010.216;
RA Le P.U., Angers-Loustau A., de Oliveira R.M., Ajlan A., Brassard C.L.,
RA Dudley A., Brent H., Siu V., Trinh G., Moelenkamp G., Wang J.,
RA Seyed Sadr M., Bedell B., Del Maestro R.F., Petrecca K.;
RT "DRR drives brain cancer invasion by regulating cytoskeletal-focal adhesion
RT dynamics.";
RL Oncogene 29:4636-4647(2010).
RN [9]
RP INTERACTION WITH ACTB AND PRDX1.
RX PubMed=21969592; DOI=10.1073/pnas.1103318108;
RA Schmidt M.V., Schuelke J.P., Liebl C., Stiess M., Avrabos C., Bock J.,
RA Wochnik G.M., Davies H.A., Zimmermann N., Scharf S.H., Truembach D.,
RA Wurst W., Zieglgaensberger W., Turck C., Holsboer F., Stewart M.G.,
RA Bradke F., Eder M., Mueller M.B., Rein T.;
RT "Tumor suppressor down-regulated in renal cell carcinoma 1 (DRR1) is a
RT stress-induced actin bundling factor that modulates synaptic efficacy and
RT cognition.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:17213-17218(2011).
RN [10]
RP FUNCTION, INTERACTION WITH ACTB AND COMMD1, SUBCELLULAR LOCATION, AND
RP MUTAGENESIS OF 65-PRO-GLU-66; 74-ARG--ARG-76; 81-LYS--LYS-84 AND
RP 122-PRO-GLU-123.
RX PubMed=28604741; DOI=10.1038/onc.2017.181;
RA Mu P., Akashi T., Lu F., Kishida S., Kadomatsu K.;
RT "A novel nuclear complex of DRR1, F-actin and COMMD1 involved in NF-kappaB
RT degradation and cell growth suppression in neuroblastoma.";
RL Oncogene 36:5745-5756(2017).
CC -!- FUNCTION: Stress-inducible actin-binding protein that plays a role in
CC synaptic and cognitive functions by modulating actin filamentous (F-
CC actin) dynamics. Mediates polymerization of globular actin to F-actin.
CC Also binds to, stabilizes and bundles F-actin. Involved in synaptic
CC function by regulating neurite outgrowth in an actin-dependent manner
CC and for the acquisition of hippocampus-dependent cognitive function,
CC such as learning and long-term memory (By similarity). Plays a role in
CC the actin and microtubule cytoskeleton organization; negatively
CC regulates focal adhesion (FA) assembly promoting malignant glial cell
CC migration in an actin-, microtubule- and MAP1A-dependent manner
CC (PubMed:20543869). Also involved in neuroblastoma G1/S phase cell cycle
CC progression and cell proliferation inhibition by stimulating
CC ubiquitination of NF-kappa-B subunit RELA and NF-kappa-B degradation in
CC a COMMD1- and actin-dependent manner (PubMed:10564580,
CC PubMed:28604741). May play a role in tumor development
CC (PubMed:10564580). {ECO:0000250|UniProtKB:Q78TU8,
CC ECO:0000269|PubMed:10564580, ECO:0000269|PubMed:20543869,
CC ECO:0000269|PubMed:28604741}.
CC -!- SUBUNIT: Interacts with ACTB (PubMed:21969592, PubMed:28604741).
CC Interacts with COMMD1; this interaction stabilizes COMMD1 in the
CC nucleus (PubMed:28604741). Interacts with MAP1A (PubMed:20543869).
CC Interacts with PRDX1 (PubMed:21969592). Interacts with F-actin (By
CC similarity). {ECO:0000250|UniProtKB:Q78TU8,
CC ECO:0000269|PubMed:20543869, ECO:0000269|PubMed:21969592,
CC ECO:0000269|PubMed:28604741}.
CC -!- INTERACTION:
CC O95990-3; Q96JN2-2: CCDC136; NbExp=3; IntAct=EBI-10192902, EBI-10171416;
CC O95990-3; A1L4K1: FSD2; NbExp=3; IntAct=EBI-10192902, EBI-5661036;
CC O95990-3; Q6A162: KRT40; NbExp=3; IntAct=EBI-10192902, EBI-10171697;
CC O95990-3; Q9BRK4: LZTS2; NbExp=3; IntAct=EBI-10192902, EBI-741037;
CC O95990-3; Q9UJV3-2: MID2; NbExp=3; IntAct=EBI-10192902, EBI-10172526;
CC O95990-3; Q8ND90: PNMA1; NbExp=3; IntAct=EBI-10192902, EBI-302345;
CC O95990-3; Q6NUQ1: RINT1; NbExp=3; IntAct=EBI-10192902, EBI-726876;
CC O95990-3; O94972: TRIM37; NbExp=3; IntAct=EBI-10192902, EBI-741602;
CC O95990-3; Q8N6Y0: USHBP1; NbExp=3; IntAct=EBI-10192902, EBI-739895;
CC O95990-4; Q86Z20: CCDC125; NbExp=3; IntAct=EBI-11977223, EBI-11977221;
CC O95990-4; Q2TAC2-2: CCDC57; NbExp=3; IntAct=EBI-11977223, EBI-10961624;
CC O95990-4; P62508-3: ESRRG; NbExp=3; IntAct=EBI-11977223, EBI-12001340;
CC O95990-4; A6NEM1: GOLGA6L9; NbExp=3; IntAct=EBI-11977223, EBI-5916454;
CC O95990-4; O75031: HSF2BP; NbExp=3; IntAct=EBI-11977223, EBI-7116203;
CC O95990-4; Q7Z3Y8: KRT27; NbExp=3; IntAct=EBI-11977223, EBI-3044087;
CC O95990-4; Q5JR59-3: MTUS2; NbExp=3; IntAct=EBI-11977223, EBI-11522433;
CC O95990-4; Q8NI38: NFKBID; NbExp=3; IntAct=EBI-11977223, EBI-10271199;
CC O95990-4; Q12933: TRAF2; NbExp=3; IntAct=EBI-11977223, EBI-355744;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10564580,
CC ECO:0000269|PubMed:11256614, ECO:0000269|PubMed:20543869,
CC ECO:0000269|PubMed:28604741}. Cytoplasm, cytoskeleton, stress fiber
CC {ECO:0000269|PubMed:20543869, ECO:0000269|PubMed:28604741}. Cell
CC junction, focal adhesion {ECO:0000269|PubMed:20543869}. Cell
CC projection, ruffle membrane {ECO:0000269|PubMed:20543869}. Synapse
CC {ECO:0000250|UniProtKB:Q78TU8}. Note=Colocalizes with F-actin and
CC COMMD1 in the nucleus (PubMed:28604741). Colocalizes with MAP1A along
CC actin stress fibers and membrane ruffles (PubMed:20543869).
CC {ECO:0000269|PubMed:20543869, ECO:0000269|PubMed:28604741}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=O95990-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O95990-2; Sequence=VSP_009232;
CC Name=3;
CC IsoId=O95990-3; Sequence=VSP_054803;
CC Name=4;
CC IsoId=O95990-4; Sequence=VSP_054804;
CC -!- TISSUE SPECIFICITY: Widely expressed (PubMed:10564580). Expressed in
CC neurons (PubMed:20543869). Expressed in malignant glial tumors
CC (PubMed:20543869). Expression is reduced or absent in a number of
CC cancer cell lines (PubMed:10564580). {ECO:0000269|PubMed:10564580,
CC ECO:0000269|PubMed:20543869}.
CC -!- MISCELLANEOUS: [Isoform 2]: May be due to an intron retention.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the FAM107 family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/FAM107AID42728ch3p14.html";
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DR EMBL; AF089854; AAD16094.1; -; mRNA.
DR EMBL; AF089853; AAD16093.1; -; mRNA.
DR EMBL; AB023810; BAA83072.1; -; Genomic_DNA.
DR EMBL; AB023811; BAA82845.1; -; mRNA.
DR EMBL; AL050264; CAB43366.1; -; mRNA.
DR EMBL; AK054720; BAG51416.1; -; mRNA.
DR EMBL; AK055443; BAB70924.1; -; mRNA.
DR EMBL; AK316450; BAH14821.1; -; mRNA.
DR EMBL; AC116036; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC119424; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471055; EAW65380.1; -; Genomic_DNA.
DR EMBL; BC010561; AAH10561.1; -; mRNA.
DR CCDS; CCDS2892.1; -. [O95990-1]
DR CCDS; CCDS63672.1; -. [O95990-3]
DR CCDS; CCDS63673.1; -. [O95990-4]
DR PIR; T08666; T08666.
DR RefSeq; NP_001070246.1; NM_001076778.2. [O95990-1]
DR RefSeq; NP_001269642.1; NM_001282713.1. [O95990-3]
DR RefSeq; NP_001269643.1; NM_001282714.1. [O95990-4]
DR RefSeq; NP_009108.1; NM_007177.3. [O95990-1]
DR AlphaFoldDB; O95990; -.
DR SMR; O95990; -.
DR BioGRID; 116341; 69.
DR IntAct; O95990; 33.
DR STRING; 9606.ENSP00000419124; -.
DR iPTMnet; O95990; -.
DR PhosphoSitePlus; O95990; -.
DR BioMuta; FAM107A; -.
DR MassIVE; O95990; -.
DR PaxDb; O95990; -.
DR PeptideAtlas; O95990; -.
DR PRIDE; O95990; -.
DR ProteomicsDB; 51166; -. [O95990-1]
DR ProteomicsDB; 51167; -. [O95990-2]
DR Antibodypedia; 31675; 137 antibodies from 21 providers.
DR DNASU; 11170; -.
DR Ensembl; ENST00000360997.7; ENSP00000354270.2; ENSG00000168309.18. [O95990-1]
DR Ensembl; ENST00000394481.5; ENSP00000377991.1; ENSG00000168309.18. [O95990-1]
DR Ensembl; ENST00000447756.2; ENSP00000400858.2; ENSG00000168309.18. [O95990-3]
DR Ensembl; ENST00000464064.5; ENSP00000419529.1; ENSG00000168309.18. [O95990-2]
DR Ensembl; ENST00000474531.5; ENSP00000419124.1; ENSG00000168309.18. [O95990-4]
DR Ensembl; ENST00000649301.1; ENSP00000497152.1; ENSG00000168309.18. [O95990-1]
DR GeneID; 11170; -.
DR KEGG; hsa:11170; -.
DR MANE-Select; ENST00000360997.7; ENSP00000354270.2; NM_001076778.3; NP_001070246.1.
DR UCSC; uc003dko.5; human. [O95990-1]
DR CTD; 11170; -.
DR DisGeNET; 11170; -.
DR GeneCards; FAM107A; -.
DR HGNC; HGNC:30827; FAM107A.
DR HPA; ENSG00000168309; Group enriched (brain, choroid plexus).
DR MIM; 608295; gene.
DR neXtProt; NX_O95990; -.
DR OpenTargets; ENSG00000168309; -.
DR PharmGKB; PA143485464; -.
DR VEuPathDB; HostDB:ENSG00000168309; -.
DR eggNOG; ENOG502RZJK; Eukaryota.
DR GeneTree; ENSGT00390000011228; -.
DR InParanoid; O95990; -.
DR PhylomeDB; O95990; -.
DR TreeFam; TF325943; -.
DR PathwayCommons; O95990; -.
DR SignaLink; O95990; -.
DR SIGNOR; O95990; -.
DR BioGRID-ORCS; 11170; 21 hits in 1069 CRISPR screens.
DR ChiTaRS; FAM107A; human.
DR GeneWiki; FAM107A; -.
DR GenomeRNAi; 11170; -.
DR Pharos; O95990; Tbio.
DR PRO; PR:O95990; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; O95990; protein.
DR Bgee; ENSG00000168309; Expressed in CA1 field of hippocampus and 195 other tissues.
DR ExpressionAtlas; O95990; baseline and differential.
DR Genevisible; O95990; HS.
DR GO; GO:0015629; C:actin cytoskeleton; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005925; C:focal adhesion; IDA:UniProtKB.
DR GO; GO:0043005; C:neuron projection; ISS:UniProtKB.
DR GO; GO:0016607; C:nuclear speck; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0032587; C:ruffle membrane; IDA:UniProtKB.
DR GO; GO:0001725; C:stress fiber; IDA:UniProtKB.
DR GO; GO:0045202; C:synapse; ISS:UniProtKB.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0051017; P:actin filament bundle assembly; ISS:UniProtKB.
DR GO; GO:0030041; P:actin filament polymerization; ISS:UniProtKB.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0071385; P:cellular response to glucocorticoid stimulus; ISS:UniProtKB.
DR GO; GO:0031669; P:cellular response to nutrient levels; ISS:UniProtKB.
DR GO; GO:0050890; P:cognition; ISS:UniProtKB.
DR GO; GO:0051895; P:negative regulation of focal adhesion assembly; IMP:UniProtKB.
DR GO; GO:2000134; P:negative regulation of G1/S transition of mitotic cell cycle; IMP:UniProtKB.
DR GO; GO:1900272; P:negative regulation of long-term synaptic potentiation; ISS:UniProtKB.
DR GO; GO:0030335; P:positive regulation of cell migration; IMP:UniProtKB.
DR GO; GO:0031398; P:positive regulation of protein ubiquitination; IMP:UniProtKB.
DR GO; GO:0032956; P:regulation of actin cytoskeleton organization; IMP:UniProtKB.
DR GO; GO:0001558; P:regulation of cell growth; IDA:UniProtKB.
DR GO; GO:0070507; P:regulation of microtubule cytoskeleton organization; IMP:UniProtKB.
DR GO; GO:0031647; P:regulation of protein stability; IMP:UniProtKB.
DR InterPro; IPR009533; FAM107.
DR PANTHER; PTHR16768; PTHR16768; 1.
DR Pfam; PF06625; DUF1151; 1.
PE 1: Evidence at protein level;
KW Actin-binding; Alternative splicing; Cell cycle; Cell junction;
KW Cell membrane; Cell projection; Coiled coil; Cytoplasm; Cytoskeleton;
KW Growth regulation; Membrane; Nucleus; Reference proteome; Stress response;
KW Synapse.
FT CHAIN 1..144
FT /note="Actin-associated protein FAM107A"
FT /id="PRO_0000080014"
FT REGION 105..124
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 66..112
FT /evidence="ECO:0000255"
FT MOTIF 74..84
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000269|PubMed:28604741"
FT VAR_SEQ 1
FT /note="M -> MAQRLGEWARGPSDATGLYRAVLLRSAAM (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_054803"
FT VAR_SEQ 1
FT /note="M -> MGAAQGKKKTYSPQARFHSENEKQRRNGSAAM (in isoform
FT 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_054804"
FT VAR_SEQ 110..144
FT /note="LEKPPEKEEDHAPEFIKVRENLRRIATLTSEEREL -> VGDGHPAGTTHPP
FT GLSSREELCCGHS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_009232"
FT VARIANT 15
FT /note="L -> M (in ovarian cancer and renal cell carcinoma
FT cell lines)"
FT /evidence="ECO:0000269|PubMed:10564580"
FT /id="VAR_017238"
FT VARIANT 19
FT /note="P -> L (in renal cell carcinoma cell line)"
FT /evidence="ECO:0000269|PubMed:10564580"
FT /id="VAR_017239"
FT VARIANT 89
FT /note="A -> S (in dbSNP:rs1043942)"
FT /id="VAR_049016"
FT VARIANT 141
FT /note="E -> Q (in dbSNP:rs11539086)"
FT /id="VAR_049017"
FT MUTAGEN 48..50
FT /note="Missing: Increases nuclear and diffused cytoplasm
FT localization, decreases interaction with MAP1A, alters
FT actin cytoskeleton organization and decreases focal
FT adhesion (FA) disassembly and cell migration."
FT /evidence="ECO:0000269|PubMed:20543869"
FT MUTAGEN 65..66
FT /note="PE->AA: Increases diffused cytoplasm localization,
FT loss of interaction with ACTB and colocalization with
FT nuclear F-actin, decreases COMMD1 protein stability and
FT ubiquitination of NF-kappa-B subunit RELA and decreases
FT focal adhesion (FA) disassembly and cell migration; when
FT associated with 122-A-A-123."
FT /evidence="ECO:0000269|PubMed:28604741"
FT MUTAGEN 74..76
FT /note="RRR->AAA: Decreases nuclear localization and
FT ubiquitination of NF-kappa-B subunit RELA."
FT /evidence="ECO:0000269|PubMed:28604741"
FT MUTAGEN 81..84
FT /note="KKKK->AAAA: Decreases nuclear localization."
FT /evidence="ECO:0000269|PubMed:28604741"
FT MUTAGEN 122..123
FT /note="PE->AA: Increases diffused cytoplasm localization,
FT loss of interaction with ACTB and colocalization with
FT nuclear F-actin, decreases COMMD1 protein stability and
FT ubiquitination of NF-kappa-B subunit RELA and decreases
FT focal adhesion (FA) disassembly and cell migration; when
FT associated with 65-A-A-66."
FT /evidence="ECO:0000269|PubMed:28604741"
FT CONFLICT O95990-4:26
FT /note="R -> Q (in Ref. 4; BAG51416)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 144 AA; 17455 MW; 90C192C723D68A36 CRC64;
MYSEIQRERA DIGGLMARPE YREWNPELIK PKKLLNPVKA SRSHQELHRE LLMNHRRGLG
VDSKPELQRV LEHRRRNQLI KKKKEELEAK RLQCPFEQEL LRRQQRLNQL EKPPEKEEDH
APEFIKVREN LRRIATLTSE EREL
