F110C_HUMAN
ID F110C_HUMAN Reviewed; 321 AA.
AC Q1W6H9;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 2.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Protein FAM110C;
GN Name=FAM110C;
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], FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=17499476; DOI=10.1016/j.ygeno.2007.03.002;
RA Hauge H., Patzke S., Aasheim H.-C.;
RT "Characterization of the FAM110 gene family.";
RL Genomics 90:14-27(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [3]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH AKT1; PPP2CA AND
RP ALPHA-TUBULIN.
RX PubMed=19698782; DOI=10.1016/j.cellsig.2009.08.001;
RA Hauge H., Fjelland K.E., Sioud M., Aasheim H.C.;
RT "Evidence for the involvement of FAM110C protein in cell spreading and
RT migration.";
RL Cell. Signal. 21:1866-1873(2009).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-241, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
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).
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:0000269|PubMed:17499476,
CC ECO:0000269|PubMed:19698782}.
CC -!- SUBUNIT: Interacts with AKT1; the interaction is transient and follows
CC AKT1 activation. Interacts with PPP2CA and alpha-tubulin.
CC {ECO:0000269|PubMed:19698782}.
CC -!- INTERACTION:
CC Q1W6H9; P31749: AKT1; NbExp=2; IntAct=EBI-3942563, EBI-296087;
CC Q1W6H9; P49674: CSNK1E; NbExp=3; IntAct=EBI-3942563, EBI-749343;
CC Q1W6H9; P31750: Akt1; Xeno; NbExp=3; IntAct=EBI-3942563, EBI-298707;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:17499476, ECO:0000269|PubMed:19698782}. Cytoplasm,
CC cytoskeleton, microtubule organizing center, centrosome
CC {ECO:0000269|PubMed:17499476, ECO:0000269|PubMed:19698782}. Cytoplasm,
CC cytoskeleton, spindle pole {ECO:0000269|PubMed:17499476,
CC ECO:0000269|PubMed:19698782}. Nucleus {ECO:0000269|PubMed:17499476,
CC ECO:0000269|PubMed:19698782}. Note=Colocalizes with microtubules during
CC interphase (PubMed:17499476). Detected at the mitotic spindle poles
CC (PubMed:17499476). Colocalizes with AKT1 at the cell cortex
CC (PubMed:19698782). {ECO:0000269|PubMed:17499476,
CC ECO:0000269|PubMed:19698782}.
CC -!- TISSUE SPECIFICITY: Detected in stomach, thyroid, trachea, adrenal
CC gland and testis, and at low levels in prostate, ovary, intestine,
CC colon, spinal cord and lymph node. {ECO:0000269|PubMed:17499476}.
CC -!- SIMILARITY: Belongs to the FAM110 family. {ECO:0000305}.
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DR EMBL; DQ431183; ABD92775.1; -; mRNA.
DR EMBL; AC097643; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS42645.1; -.
DR RefSeq; NP_001071178.2; NM_001077710.2.
DR AlphaFoldDB; Q1W6H9; -.
DR BioGRID; 567837; 13.
DR IntAct; Q1W6H9; 8.
DR MINT; Q1W6H9; -.
DR STRING; 9606.ENSP00000328347; -.
DR iPTMnet; Q1W6H9; -.
DR PhosphoSitePlus; Q1W6H9; -.
DR BioMuta; FAM110C; -.
DR DMDM; 296434495; -.
DR EPD; Q1W6H9; -.
DR jPOST; Q1W6H9; -.
DR MassIVE; Q1W6H9; -.
DR MaxQB; Q1W6H9; -.
DR PaxDb; Q1W6H9; -.
DR PeptideAtlas; Q1W6H9; -.
DR PRIDE; Q1W6H9; -.
DR ProteomicsDB; 61250; -.
DR Antibodypedia; 49861; 27 antibodies from 11 providers.
DR DNASU; 642273; -.
DR Ensembl; ENST00000327669.5; ENSP00000328347.4; ENSG00000184731.6.
DR GeneID; 642273; -.
DR KEGG; hsa:642273; -.
DR MANE-Select; ENST00000327669.5; ENSP00000328347.4; NM_001077710.3; NP_001071178.2.
DR UCSC; uc010yim.3; human.
DR CTD; 642273; -.
DR GeneCards; FAM110C; -.
DR HGNC; HGNC:33340; FAM110C.
DR HPA; ENSG00000184731; Tissue enhanced (esophagus).
DR MIM; 611395; gene.
DR neXtProt; NX_Q1W6H9; -.
DR OpenTargets; ENSG00000184731; -.
DR PharmGKB; PA162385674; -.
DR VEuPathDB; HostDB:ENSG00000184731; -.
DR eggNOG; ENOG502S0DB; Eukaryota.
DR GeneTree; ENSGT00950000183056; -.
DR HOGENOM; CLU_050540_0_0_1; -.
DR InParanoid; Q1W6H9; -.
DR OMA; IAINIRS; -.
DR OrthoDB; 745936at2759; -.
DR PhylomeDB; Q1W6H9; -.
DR TreeFam; TF330964; -.
DR PathwayCommons; Q1W6H9; -.
DR SignaLink; Q1W6H9; -.
DR BioGRID-ORCS; 642273; 13 hits in 1076 CRISPR screens.
DR ChiTaRS; FAM110C; human.
DR GenomeRNAi; 642273; -.
DR Pharos; Q1W6H9; Tbio.
DR PRO; PR:Q1W6H9; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q1W6H9; protein.
DR Bgee; ENSG00000184731; Expressed in pancreatic ductal cell and 144 other tissues.
DR Genevisible; Q1W6H9; HS.
DR GO; GO:0005938; C:cell cortex; IDA: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; IDA:UniProtKB.
DR GO; GO:0030335; P:positive regulation of cell migration; IMP:UniProtKB.
DR GO; GO:0051897; P:positive regulation of protein kinase B signaling; IMP:UniProtKB.
DR GO; GO:0060491; P:regulation of cell projection assembly; IMP:UniProtKB.
DR InterPro; IPR025740; FAM110.
DR InterPro; IPR025741; FAM110_C.
DR InterPro; IPR025739; FAM110_N.
DR PANTHER; PTHR14758; PTHR14758; 1.
DR Pfam; PF14160; FAM110_C; 1.
DR Pfam; PF14161; FAM110_N; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Cytoskeleton; Microtubule; Nucleus; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..321
FT /note="Protein FAM110C"
FT /id="PRO_0000293461"
FT REGION 1..84
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 111..203
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 18..50
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 241
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT CONFLICT 164
FT /note="I -> T (in Ref. 1; ABD92775)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 321 AA; 33863 MW; 148150E2770C7D8D CRC64;
MRALAALSAP PNERLLPRDP AATRDPDAAR PARRSAVERL AADRAKYVRG RPGTGRGVAS
EGSGPGAIKC PGNDPGPPAR APAPVARRAI ARKPLRPDSL IIYRQKCEFV RGSGADGPRA
SLVKKLFQGP GKDKAPVPRT GDEGKAGNPE TVPTTPGPAA DPAIPETPAP AARSAAPSSV
PAAPPGPEPR VVRRRGLQRS QSDLSSRYSA ALAESDTFFQ YCGLDPEVVE ALGRENFTAG
SDCVTLKVRS VSVATSGSGF SRHSGGDDEG LQEEELIEQV PSTTSVIERN ARIIKWLYTC
KKAKETPSQE QSRTRGSKPS R
