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Database: UniProt
Entry: F110B_HUMAN
LinkDB: F110B_HUMAN
Original site: F110B_HUMAN 
ID   F110B_HUMAN             Reviewed;         370 AA.
AC   Q8TC76; Q5BM08; Q9Y4K2;
DT   01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   24-JAN-2024, entry version 147.
DE   RecName: Full=Protein FAM110B;
GN   Name=FAM110B; Synonyms=C8orf72;
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].
RC   TISSUE=Colon carcinoma;
RA   Li X.-N., Li Y.-L., Liu G.-B., Ding Y.-Q.;
RT   "Molecular cloning and bioinformatic analysis of a novel tumor-associated
RT   gene MGC39325.";
RL   Shi Jie Hua Ren Xiao Hua Za Zhi 13:1059-1064(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND TISSUE 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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=9110174; DOI=10.1101/gr.7.4.353;
RA   Yu W., Andersson B., Worley K.C., Muzny D.M., Ding Y., Liu W.,
RA   Ricafrente J.Y., Wentland M.A., Lennon G., Gibbs R.A.;
RT   "Large-scale concatenation cDNA sequencing.";
RL   Genome Res. 7:353-358(1997).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Spleen;
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   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-301, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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., Mann M.;
RT   "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT   site occupancy during mitosis.";
RL   Sci. Signal. 3:RA3-RA3(2010).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-301, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA   Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA   Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT   "System-wide temporal characterization of the proteome and phosphoproteome
RT   of human embryonic stem cell differentiation.";
RL   Sci. Signal. 4:RS3-RS3(2011).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-301, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=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   [8]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA   Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT   phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [9]
RP   VARIANT [LARGE SCALE ANALYSIS] SER-214.
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 involved in tumor progression.
CC   -!- INTERACTION:
CC       Q8TC76; O75031: HSF2BP; NbExp=3; IntAct=EBI-2558383, EBI-7116203;
CC       Q8TC76; Q99687-3: MEIS3; NbExp=3; IntAct=EBI-2558383, EBI-18582591;
CC       Q8TC76; P55347: PKNOX1; NbExp=3; IntAct=EBI-2558383, EBI-1373569;
CC       Q8TC76; Q96KN3: PKNOX2; NbExp=5; IntAct=EBI-2558383, EBI-2692890;
CC       Q8TC76; P62258: YWHAE; NbExp=2; IntAct=EBI-2558383, EBI-356498;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17499476}.
CC       Cytoplasm, cytoskeleton, microtubule organizing center, centrosome
CC       {ECO:0000269|PubMed:17499476}.
CC   -!- TISSUE SPECIFICITY: Detected in thyroid, spleen and testis, and at
CC       lower levels in stomach, spinal cord, lymph node, trachea, adrenal
CC       gland, prostate, ovary and intestine. {ECO:0000269|PubMed:17499476}.
CC   -!- SIMILARITY: Belongs to the FAM110 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAB50224.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AY937246; AAX28928.1; -; mRNA.
DR   EMBL; DQ431182; ABD92774.1; -; mRNA.
DR   EMBL; U79298; AAB50224.1; ALT_INIT; mRNA.
DR   EMBL; BC024294; AAH24294.1; -; mRNA.
DR   CCDS; CCDS6170.1; -.
DR   RefSeq; NP_671722.1; NM_147189.2.
DR   RefSeq; XP_005251381.1; XM_005251324.2.
DR   RefSeq; XP_005251382.1; XM_005251325.3.
DR   RefSeq; XP_005251383.1; XM_005251326.2.
DR   RefSeq; XP_016869437.1; XM_017013948.1.
DR   AlphaFoldDB; Q8TC76; -.
DR   BioGRID; 124703; 69.
DR   IntAct; Q8TC76; 14.
DR   MINT; Q8TC76; -.
DR   STRING; 9606.ENSP00000355204; -.
DR   iPTMnet; Q8TC76; -.
DR   PhosphoSitePlus; Q8TC76; -.
DR   BioMuta; FAM110B; -.
DR   DMDM; 74730569; -.
DR   MassIVE; Q8TC76; -.
DR   PaxDb; 9606-ENSP00000355204; -.
DR   PeptideAtlas; Q8TC76; -.
DR   ProteomicsDB; 74097; -.
DR   Pumba; Q8TC76; -.
DR   Antibodypedia; 2031; 113 antibodies from 13 providers.
DR   DNASU; 90362; -.
DR   Ensembl; ENST00000361488.7; ENSP00000355204.3; ENSG00000169122.12.
DR   Ensembl; ENST00000519262.6; ENSP00000509301.1; ENSG00000169122.12.
DR   GeneID; 90362; -.
DR   KEGG; hsa:90362; -.
DR   MANE-Select; ENST00000519262.6; ENSP00000509301.1; NM_001377989.1; NP_001364918.1.
DR   UCSC; uc003xtj.2; human.
DR   AGR; HGNC:28587; -.
DR   CTD; 90362; -.
DR   DisGeNET; 90362; -.
DR   GeneCards; FAM110B; -.
DR   HGNC; HGNC:28587; FAM110B.
DR   HPA; ENSG00000169122; Low tissue specificity.
DR   MIM; 611394; gene.
DR   neXtProt; NX_Q8TC76; -.
DR   OpenTargets; ENSG00000169122; -.
DR   PharmGKB; PA162385659; -.
DR   VEuPathDB; HostDB:ENSG00000169122; -.
DR   eggNOG; ENOG502R37V; Eukaryota.
DR   GeneTree; ENSGT00950000183056; -.
DR   HOGENOM; CLU_050540_0_0_1; -.
DR   InParanoid; Q8TC76; -.
DR   OMA; IASMKSP; -.
DR   OrthoDB; 5407076at2759; -.
DR   PhylomeDB; Q8TC76; -.
DR   TreeFam; TF330964; -.
DR   PathwayCommons; Q8TC76; -.
DR   SignaLink; Q8TC76; -.
DR   BioGRID-ORCS; 90362; 18 hits in 1154 CRISPR screens.
DR   ChiTaRS; FAM110B; human.
DR   GenomeRNAi; 90362; -.
DR   Pharos; Q8TC76; Tbio.
DR   PRO; PR:Q8TC76; -.
DR   Proteomes; UP000005640; Chromosome 8.
DR   RNAct; Q8TC76; Protein.
DR   Bgee; ENSG00000169122; Expressed in cortical plate and 166 other cell types or tissues.
DR   ExpressionAtlas; Q8TC76; baseline and differential.
DR   Genevisible; Q8TC76; HS.
DR   GO; GO:0005813; C:centrosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005829; C:cytosol; IDA:HPA.
DR   GO; GO:0005739; C:mitochondrion; IDA:HPA.
DR   InterPro; IPR025740; FAM110.
DR   InterPro; IPR025741; FAM110_C.
DR   InterPro; IPR025739; FAM110_N.
DR   PANTHER; PTHR14758; AGAP005440-PA; 1.
DR   PANTHER; PTHR14758:SF2; PROTEIN FAM110B; 1.
DR   Pfam; PF14160; FAM110_C; 1.
DR   Pfam; PF14161; FAM110_N; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Cytoskeleton; Phosphoprotein; Reference proteome.
FT   CHAIN           1..370
FT                   /note="Protein FAM110B"
FT                   /id="PRO_0000285651"
FT   REGION          127..151
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          237..256
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          317..337
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         238
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8C739"
FT   MOD_RES         301
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:20068231,
FT                   ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT   VARIANT         214
FT                   /note="A -> S (in a colorectal cancer sample; somatic
FT                   mutation; dbSNP:rs150740446)"
FT                   /evidence="ECO:0000269|PubMed:16959974"
FT                   /id="VAR_036319"
FT   CONFLICT        41
FT                   /note="A -> T (in Ref. 1; AAX28928)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        296
FT                   /note="F -> Y (in Ref. 1; AAX28928)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        345
FT                   /note="I -> N (in Ref. 1; AAX28928)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   370 AA;  40728 MW;  7D0F066083AE6C1B CRC64;
     MPTETLQTGS MVKPVSPAGT FTSAVPLRIL NKGPDYFRRQ AEPNPKRLSA VERLEADKAK
     YVKSQEVINA KQEPVKPAVL AKPPVCPAAK RALGSPTLKV FGNHAKTESG VQRENLKLEI
     LKNIINSSEG SSSGSGHKHS SRNWPPHRSE ATDLHRHSFA ESLKVYPTQG RRSPQEGGSH
     VGRRLLEQSA ESFLHVSHSS SDIRKVTSVK PLKAIPCSSS APPLPPKPKI AAIASMKSPE
     ADPVEPACGV SRRPSLQRSK SDLSDRYFRV DADVERFFNY CGLDPEELEN LGMENFARAN
     SDIISLNFRS ASMISSDCEQ SQDSNSDLRN DDSANDRVPY GISAIERNAR IIKWLYSIKQ
     ARESQKVSHV
//
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