F110C_MOUSE
ID F110C_MOUSE Reviewed; 421 AA.
AC Q8VE94; Q9D322;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Protein FAM110C;
GN Name=Fam110c;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Colon;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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 [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-350, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, and Pancreas;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: May play a role in microtubule organization. May play a role
CC in cell spreading and cell migration of epithelial cells; the function
CC may involve the AKT1 signaling pathway. {ECO:0000250|UniProtKB:Q1W6H9}.
CC -!- SUBUNIT: Interacts with AKT1; the interaction is transient and follows
CC AKT1 activation. Interacts with PPP2CA and alpha-tubulin.
CC {ECO:0000250|UniProtKB:Q1W6H9}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:Q1W6H9}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome {ECO:0000250|UniProtKB:Q1W6H9}.
CC Cytoplasm, cytoskeleton, spindle pole {ECO:0000250|UniProtKB:Q1W6H9}.
CC Nucleus {ECO:0000250|UniProtKB:Q1W6H9}. Note=Colocalizes with
CC microtubules during interphase. Detected at the mitotic spindle poles.
CC Colocalizes with AKT1 at the cell cortex.
CC {ECO:0000250|UniProtKB:Q1W6H9}.
CC -!- SIMILARITY: Belongs to the FAM110 family. {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; AK018545; BAB31266.1; -; mRNA.
DR EMBL; AK160079; BAE35611.1; -; mRNA.
DR EMBL; BC019466; AAH19466.1; -; mRNA.
DR EMBL; BC085288; AAH85288.1; -; mRNA.
DR CCDS; CCDS25860.1; -.
DR RefSeq; NP_082104.2; NM_027828.2.
DR AlphaFoldDB; Q8VE94; -.
DR SMR; Q8VE94; -.
DR STRING; 10090.ENSMUSP00000041563; -.
DR iPTMnet; Q8VE94; -.
DR PhosphoSitePlus; Q8VE94; -.
DR jPOST; Q8VE94; -.
DR MaxQB; Q8VE94; -.
DR PaxDb; Q8VE94; -.
DR PRIDE; Q8VE94; -.
DR ProteomicsDB; 275957; -.
DR Antibodypedia; 49861; 27 antibodies from 11 providers.
DR Ensembl; ENSMUST00000041133; ENSMUSP00000041563; ENSMUSG00000036136.
DR GeneID; 104943; -.
DR KEGG; mmu:104943; -.
DR UCSC; uc007nhb.1; mouse.
DR CTD; 642273; -.
DR MGI; MGI:1918813; Fam110c.
DR VEuPathDB; HostDB:ENSMUSG00000036136; -.
DR eggNOG; ENOG502S0DB; Eukaryota.
DR GeneTree; ENSGT00950000183056; -.
DR HOGENOM; CLU_050540_0_0_1; -.
DR InParanoid; Q8VE94; -.
DR OMA; IAINIRS; -.
DR OrthoDB; 745936at2759; -.
DR PhylomeDB; Q8VE94; -.
DR TreeFam; TF330964; -.
DR BioGRID-ORCS; 104943; 1 hit in 73 CRISPR screens.
DR ChiTaRS; Fam110c; mouse.
DR PRO; PR:Q8VE94; -.
DR Proteomes; UP000000589; Chromosome 12.
DR RNAct; Q8VE94; protein.
DR Bgee; ENSMUSG00000036136; Expressed in primary oocyte and 106 other tissues.
DR Genevisible; Q8VE94; MM.
DR GO; GO:0005938; C:cell cortex; ISS:UniProtKB.
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:0000922; C:spindle pole; IEA:UniProtKB-SubCell.
DR GO; GO:0043014; F:alpha-tubulin binding; ISS:UniProtKB.
DR GO; GO:0030335; P:positive regulation of cell migration; ISS:UniProtKB.
DR GO; GO:0051897; P:positive regulation of protein kinase B signaling; ISS:UniProtKB.
DR GO; GO:0060491; P:regulation of cell projection assembly; ISS:UniProtKB.
DR InterPro; IPR025740; FAM110.
DR InterPro; IPR025741; FAM110_C.
DR PANTHER; PTHR14758; PTHR14758; 2.
DR Pfam; PF14160; FAM110_C; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Cytoskeleton; Microtubule; Nucleus; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..421
FT /note="Protein FAM110C"
FT /id="PRO_0000293462"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 51..80
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 141..266
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 141..155
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 188..202
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 235..249
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 350
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CONFLICT 327
FT /note="F -> L (in Ref. 1; BAB31266)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 421 AA; 45319 MW; CA3128F9C10FBEBA CRC64;
MRALPTLDSL ARMRPPLGDP RAAEDTLTPR PANKSAVERL AADRAKYVRS TLGSSRGPVS
EHRVPEAPGV QHRNPIPSAL APAPVARRAI ARKPLRPDSL VIYRQKCEFV RGSDADCSRV
GLMKKFFQGS GKDKMAVAPE TTRVADEDKT TKETEATWTK SSQAAAARPA SMLPPPTPVV
AVKSPAEKTR VANEDKTTKE TEATWTKSSQ AAAARPASML PPPTPVVAVK SPAEKTRVAN
EDKTTKETEA TWTKSSQAAA TRPASMLPPP TPVVAVKSPA LPFEVAPRVP VGCSGVQLRV
SRSKGLQRSQ SDLSSRYSIA KAESDTFFKY CGLDPDVVEA LGRENFSAGS DCVTLKVRSV
SMAASDSSFS RHSEDGLQEE ELLEQVPSTT SVVERNARII KWLFTCKKAK ETPSQKLQGP
A
