Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q86VR2 (F134C_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 71. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Protein FAM134C
Gene names
Name:FAM134C
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length466 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Subcellular location

Membrane; Multi-pass membrane protein Potential.

Sequence similarities

Belongs to the FAM134 family.

Ontologies

Keywords
   Cellular componentMembrane
   DomainTransmembrane
Transmembrane helix
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Cellular_componentintegral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.3
Chain2 – 466465Protein FAM134C
PRO_0000288469

Regions

Transmembrane81 – 10121Helical; Potential
Transmembrane164 – 18421Helical; Potential
Transmembrane187 – 20721Helical; Potential

Amino acid modifications

Modified residue21N-acetylalanine Ref.3 Ref.5 Ref.8
Modified residue101Phosphothreonine Ref.5
Modified residue261Phosphoserine Ref.7
Modified residue2581Phosphoserine Ref.2 Ref.4 Ref.5 Ref.7
Modified residue2601Phosphoserine Ref.2 Ref.4 Ref.5 Ref.7
Modified residue2831Phosphothreonine Ref.2
Modified residue2851Phosphoserine Ref.2
Modified residue2881Phosphoserine By similarity
Modified residue3031Phosphoserine By similarity
Modified residue3071Phosphothreonine Ref.2 Ref.4
Modified residue3101Phosphothreonine Ref.2
Modified residue3131Phosphoserine Ref.2 Ref.4
Modified residue3201Phosphoserine Ref.2 Ref.4 Ref.7
Modified residue3601Phosphoserine Ref.2
Modified residue4401Phosphothreonine Ref.2 Ref.4

Sequences

Sequence LengthMass (Da)Tools
Q86VR2 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: F9D468353C13A14B

FASTA46651,396
        10         20         30         40         50         60 
MAEAEGVPTT PGPASGSTFR GRRDVSGSWE RDQQVEAAQR ALVEVLGPYE PLLSRVQAAL 

        70         80         90        100        110        120 
VWERPARSAL WCLGLNAAFW FFALTSLRLV FLLAFGLMII VCIDQWKNKI WPEIKVPRPD 

       130        140        150        160        170        180 
ALDNESWGFV HPRLLSVPEL CHHVAEVWVS GTIFIRNVLL FKKQNPGKFC LLSCGILTFL 

       190        200        210        220        230        240 
AVLGRYVPGL LLSYLMLVTV MMWPLAVYHR LWDRAYVRLK PALQRLDFSV RGYMMSKQRE 

       250        260        270        280        290        300 
RQLRRRALHP ERAMDNHSDS EEELAAFCPQ LDDSTVAREL AITDSEHSDA EVSCTDNGTF 

       310        320        330        340        350        360 
NLSRGQTPLT EGSEDLDGHS DPEESFARDL PDFPSINMDP AGLDDEDDTS IGMPSLMYRS 

       370        380        390        400        410        420 
PPGAEEPQAP PASRDEAALP ELLLGALPVG SNLTSNLASL VSQGMIQLAL SGASQPGPSG 

       430        440        450        460 
APAQRATRGF LRSPSSDLDT DAEGDDFELL DQSELSQLDP ASSRSH 

« Hide

References

[1]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain.
[2]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-258; SER-260; THR-283; SER-285; THR-307; THR-310; SER-313; SER-320; SER-360 AND THR-440, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[3]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[4]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-258; SER-260; THR-307; SER-313; SER-320 AND THR-440, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[5]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-10; SER-258 AND SER-260, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[6]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[7]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-26; SER-258; SER-260 AND SER-320, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[8]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BC049370 mRNA. Translation: AAH49370.1.
CCDSCCDS11432.1.
RefSeqNP_835227.1. NM_178126.3.
UniGeneHs.632262.

3D structure databases

ProteinModelPortalQ86VR2.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid127817. 3 interactions.

PTM databases

PhosphoSiteQ86VR2.

Polymorphism databases

DMDM74727607.

Proteomic databases

MaxQBQ86VR2.
PaxDbQ86VR2.
PeptideAtlasQ86VR2.
PRIDEQ86VR2.

Protocols and materials databases

DNASU162427.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000309428; ENSP00000309432; ENSG00000141699.
GeneID162427.
KEGGhsa:162427.
UCSCuc002ial.2. human.

Organism-specific databases

CTD162427.
GeneCardsGC17M040731.
H-InvDBHIX0020377.
HGNCHGNC:27258. FAM134C.
HPAHPA016492.
neXtProtNX_Q86VR2.
PharmGKBPA162386207.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG26663.
HOGENOMHOG000050246.
HOVERGENHBG096339.
InParanoidQ86VR2.
OMAFCLLSCG.
PhylomeDBQ86VR2.
TreeFamTF329111.

Gene expression databases

ArrayExpressQ86VR2.
BgeeQ86VR2.
CleanExHS_FAM134C.
GenevestigatorQ86VR2.

Family and domain databases

ProtoNetSearch...

Other

ChiTaRSFAM134C. human.
GeneWikiFAM134C.
GenomeRNAi162427.
NextBio88169.
PROQ86VR2.

Entry information

Entry nameF134C_HUMAN
AccessionPrimary (citable) accession number: Q86VR2
Entry history
Integrated into UniProtKB/Swiss-Prot: May 29, 2007
Last sequence update: June 1, 2003
Last modified: July 9, 2014
This is version 71 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human chromosome 17

Human chromosome 17: entries, gene names and cross-references to MIM