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Protein

Protein FAM110C

Gene

FAM110C

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

May play a role in microtubule organization. May play a role in cell spreading and cell migration of epithelial cells; the function may involve the AKT1 signaling pathway.2 Publications

GO - Molecular functioni

  • alpha-tubulin binding Source: UniProtKB

GO - Biological processi

  • positive regulation of cell migration Source: UniProtKB
  • positive regulation of protein kinase B signaling Source: UniProtKB
  • regulation of cell projection assembly Source: UniProtKB
Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
Protein FAM110C
Gene namesi
Name:FAM110C
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 2

Organism-specific databases

HGNCiHGNC:33340. FAM110C.

Subcellular locationi

GO - Cellular componenti

  • cell cortex Source: UniProtKB
  • cytoplasm Source: HPA
  • microtubule Source: UniProtKB-KW
  • microtubule organizing center Source: UniProtKB-SubCell
  • nucleoplasm Source: HPA
  • spindle pole Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Microtubule, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA162385674.

Polymorphism and mutation databases

BioMutaiFAM110C.
DMDMi296434495.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 321321Protein FAM110CPRO_0000293461Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei241 – 2411PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ1W6H9.
MaxQBiQ1W6H9.
PaxDbiQ1W6H9.
PeptideAtlasiQ1W6H9.
PRIDEiQ1W6H9.

PTM databases

iPTMnetiQ1W6H9.
PhosphoSiteiQ1W6H9.

Expressioni

Tissue specificityi

Detected in stomach, thyroid, trachea, adrenal gland and testis, and at low levels in prostate, ovary, intestine, colon, spinal cord and lymph node.1 Publication

Gene expression databases

BgeeiQ1W6H9.
CleanExiHS_FAM110C.
GenevisibleiQ1W6H9. HS.

Organism-specific databases

HPAiHPA036144.
HPA036145.

Interactioni

Subunit structurei

Interacts with AKT1; the interaction is transient and follows AKT1 activation. Interacts with PPP2CA and alpha-tubulin.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
AKT1P317492EBI-3942563,EBI-296087
Akt1P317503EBI-3942563,EBI-298707From a different organism.

GO - Molecular functioni

  • alpha-tubulin binding Source: UniProtKB

Protein-protein interaction databases

BioGridi567837. 5 interactions.
IntActiQ1W6H9. 3 interactions.
STRINGi9606.ENSP00000328347.

Structurei

3D structure databases

ProteinModelPortaliQ1W6H9.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the FAM110 family.Curated

Phylogenomic databases

eggNOGiENOG410IE0E. Eukaryota.
ENOG4111MR4. LUCA.
GeneTreeiENSGT00530000063395.
HOVERGENiHBG103770.
InParanoidiQ1W6H9.
OMAiPGAIKCP.
OrthoDBiEOG7NGQCF.
PhylomeDBiQ1W6H9.
TreeFamiTF330964.

Family and domain databases

InterProiIPR025740. FAM110.
IPR025741. FAM110_C.
IPR025739. FAM110_N.
[Graphical view]
PANTHERiPTHR14758. PTHR14758. 1 hit.
PfamiPF14160. FAM110_C. 1 hit.
PF14161. FAM110_N. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q1W6H9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRALAALSAP PNERLLPRDP AATRDPDAAR PARRSAVERL AADRAKYVRG
60 70 80 90 100
RPGTGRGVAS EGSGPGAIKC PGNDPGPPAR APAPVARRAI ARKPLRPDSL
110 120 130 140 150
IIYRQKCEFV RGSGADGPRA SLVKKLFQGP GKDKAPVPRT GDEGKAGNPE
160 170 180 190 200
TVPTTPGPAA DPAIPETPAP AARSAAPSSV PAAPPGPEPR VVRRRGLQRS
210 220 230 240 250
QSDLSSRYSA ALAESDTFFQ YCGLDPEVVE ALGRENFTAG SDCVTLKVRS
260 270 280 290 300
VSVATSGSGF SRHSGGDDEG LQEEELIEQV PSTTSVIERN ARIIKWLYTC
310 320
KKAKETPSQE QSRTRGSKPS R
Length:321
Mass (Da):33,863
Last modified:May 18, 2010 - v2
Checksum:i148150E2770C7D8D
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti164 – 1641I → T in ABD92775 (PubMed:17499476).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ431183 mRNA. Translation: ABD92775.1.
AC097643 Genomic DNA. No translation available.
CCDSiCCDS42645.1.
RefSeqiNP_001071178.2. NM_001077710.2.
UniGeneiHs.8379.

Genome annotation databases

EnsembliENST00000327669; ENSP00000328347; ENSG00000184731.
GeneIDi642273.
KEGGihsa:642273.
UCSCiuc010yim.3. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ431183 mRNA. Translation: ABD92775.1.
AC097643 Genomic DNA. No translation available.
CCDSiCCDS42645.1.
RefSeqiNP_001071178.2. NM_001077710.2.
UniGeneiHs.8379.

3D structure databases

ProteinModelPortaliQ1W6H9.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi567837. 5 interactions.
IntActiQ1W6H9. 3 interactions.
STRINGi9606.ENSP00000328347.

PTM databases

iPTMnetiQ1W6H9.
PhosphoSiteiQ1W6H9.

Polymorphism and mutation databases

BioMutaiFAM110C.
DMDMi296434495.

Proteomic databases

EPDiQ1W6H9.
MaxQBiQ1W6H9.
PaxDbiQ1W6H9.
PeptideAtlasiQ1W6H9.
PRIDEiQ1W6H9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000327669; ENSP00000328347; ENSG00000184731.
GeneIDi642273.
KEGGihsa:642273.
UCSCiuc010yim.3. human.

Organism-specific databases

CTDi642273.
GeneCardsiFAM110C.
H-InvDBHIX0001776.
HGNCiHGNC:33340. FAM110C.
HPAiHPA036144.
HPA036145.
MIMi611395. gene.
neXtProtiNX_Q1W6H9.
PharmGKBiPA162385674.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IE0E. Eukaryota.
ENOG4111MR4. LUCA.
GeneTreeiENSGT00530000063395.
HOVERGENiHBG103770.
InParanoidiQ1W6H9.
OMAiPGAIKCP.
OrthoDBiEOG7NGQCF.
PhylomeDBiQ1W6H9.
TreeFamiTF330964.

Miscellaneous databases

GenomeRNAii642273.
PROiQ1W6H9.
SOURCEiSearch...

Gene expression databases

BgeeiQ1W6H9.
CleanExiHS_FAM110C.
GenevisibleiQ1W6H9. HS.

Family and domain databases

InterProiIPR025740. FAM110.
IPR025741. FAM110_C.
IPR025739. FAM110_N.
[Graphical view]
PANTHERiPTHR14758. PTHR14758. 1 hit.
PfamiPF14160. FAM110_C. 1 hit.
PF14161. FAM110_N. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Characterization of the FAM110 gene family."
    Hauge H., Patzke S., Aasheim H.-C.
    Genomics 90:14-27(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  2. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
    Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
    , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
    Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "Evidence for the involvement of FAM110C protein in cell spreading and migration."
    Hauge H., Fjelland K.E., Sioud M., Aasheim H.C.
    Cell. Signal. 21:1866-1873(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH AKT1; PPP2CA AND ALPHA-TUBULIN.
  4. "Toward a comprehensive characterization of a human cancer cell phosphoproteome."
    Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., Mohammed S.
    J. Proteome Res. 12:260-271(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-241, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.

Entry informationi

Entry nameiF110C_HUMAN
AccessioniPrimary (citable) accession number: Q1W6H9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 10, 2007
Last sequence update: May 18, 2010
Last modified: July 6, 2016
This is version 74 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.