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Protein

Protein FAM134C

Gene

FAM134C

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Names & Taxonomyi

Protein namesi
Recommended name:
Protein FAM134C
Gene namesi
Name:FAM134C
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 17

Organism-specific databases

HGNCiHGNC:27258. FAM134C.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei81 – 10121HelicalSequence AnalysisAdd
BLAST
Transmembranei164 – 18421HelicalSequence AnalysisAdd
BLAST
Transmembranei187 – 20721HelicalSequence AnalysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA162386207.

Polymorphism and mutation databases

BioMutaiFAM134C.
DMDMi74727607.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed3 Publications
Chaini2 – 466465Protein FAM134CPRO_0000288469Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine3 Publications
Modified residuei10 – 101Phosphothreonine1 Publication
Modified residuei26 – 261Phosphoserine1 Publication
Modified residuei258 – 2581Phosphoserine4 Publications
Modified residuei260 – 2601Phosphoserine4 Publications
Modified residuei283 – 2831Phosphothreonine1 Publication
Modified residuei285 – 2851Phosphoserine1 Publication
Modified residuei288 – 2881PhosphoserineBy similarity
Modified residuei303 – 3031PhosphoserineBy similarity
Modified residuei307 – 3071Phosphothreonine3 Publications
Modified residuei310 – 3101Phosphothreonine2 Publications
Modified residuei313 – 3131Phosphoserine3 Publications
Modified residuei320 – 3201Phosphoserine4 Publications
Modified residuei360 – 3601Phosphoserine1 Publication
Modified residuei440 – 4401Phosphothreonine2 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ86VR2.
PaxDbiQ86VR2.
PeptideAtlasiQ86VR2.
PRIDEiQ86VR2.

PTM databases

PhosphoSiteiQ86VR2.

Expressioni

Gene expression databases

BgeeiQ86VR2.
CleanExiHS_FAM134C.
ExpressionAtlasiQ86VR2. baseline and differential.
GenevisibleiQ86VR2. HS.

Organism-specific databases

HPAiHPA016492.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
ABHD16AO958703EBI-10192441,EBI-348517
ARL6IP1Q150413EBI-10192441,EBI-714543
GABARAPL1Q9H0R83EBI-10192441,EBI-3464833
MAP1LC3AQ9H4923EBI-10192441,EBI-720768
STAP1Q9ULZ23EBI-10192441,EBI-6083058

Protein-protein interaction databases

BioGridi127817. 47 interactions.
IntActiQ86VR2. 5 interactions.
STRINGi9606.ENSP00000309432.

Structurei

3D structure databases

ProteinModelPortaliQ86VR2.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the FAM134 family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG26663.
GeneTreeiENSGT00530000063240.
HOGENOMiHOG000050246.
HOVERGENiHBG096339.
InParanoidiQ86VR2.
OMAiWPLAVYH.
PhylomeDBiQ86VR2.
TreeFamiTF329111.

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q86VR2-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MAEAEGVPTT PGPASGSTFR GRRDVSGSWE RDQQVEAAQR ALVEVLGPYE
60 70 80 90 100
PLLSRVQAAL VWERPARSAL WCLGLNAAFW FFALTSLRLV FLLAFGLMII
110 120 130 140 150
VCIDQWKNKI WPEIKVPRPD ALDNESWGFV HPRLLSVPEL CHHVAEVWVS
160 170 180 190 200
GTIFIRNVLL FKKQNPGKFC LLSCGILTFL AVLGRYVPGL LLSYLMLVTV
210 220 230 240 250
MMWPLAVYHR LWDRAYVRLK PALQRLDFSV RGYMMSKQRE RQLRRRALHP
260 270 280 290 300
ERAMDNHSDS EEELAAFCPQ LDDSTVAREL AITDSEHSDA EVSCTDNGTF
310 320 330 340 350
NLSRGQTPLT EGSEDLDGHS DPEESFARDL PDFPSINMDP AGLDDEDDTS
360 370 380 390 400
IGMPSLMYRS PPGAEEPQAP PASRDEAALP ELLLGALPVG SNLTSNLASL
410 420 430 440 450
VSQGMIQLAL SGASQPGPSG APAQRATRGF LRSPSSDLDT DAEGDDFELL
460
DQSELSQLDP ASSRSH
Length:466
Mass (Da):51,396
Last modified:June 1, 2003 - v1
Checksum:iF9D468353C13A14B
GO
Isoform 2 (identifier: Q86VR2-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-195: Missing.

Note: No experimental confirmation available.
Show »
Length:271
Mass (Da):29,582
Checksum:i7361F5A0294F76BC
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 195195Missing in isoform 2. 1 PublicationVSP_056991Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK091125 mRNA. Translation: BAG52287.1.
AK294791 mRNA. Translation: BAG57914.1.
AC067852 Genomic DNA. No translation available.
CH471152 Genomic DNA. Translation: EAW60851.1.
BC049370 mRNA. Translation: AAH49370.1.
CCDSiCCDS11432.1. [Q86VR2-1]
RefSeqiNP_835227.1. NM_178126.3. [Q86VR2-1]
XP_006721792.1. XM_006721729.1. [Q86VR2-2]
UniGeneiHs.632262.

Genome annotation databases

EnsembliENST00000309428; ENSP00000309432; ENSG00000141699.
GeneIDi162427.
KEGGihsa:162427.
UCSCiuc002ial.2. human. [Q86VR2-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK091125 mRNA. Translation: BAG52287.1.
AK294791 mRNA. Translation: BAG57914.1.
AC067852 Genomic DNA. No translation available.
CH471152 Genomic DNA. Translation: EAW60851.1.
BC049370 mRNA. Translation: AAH49370.1.
CCDSiCCDS11432.1. [Q86VR2-1]
RefSeqiNP_835227.1. NM_178126.3. [Q86VR2-1]
XP_006721792.1. XM_006721729.1. [Q86VR2-2]
UniGeneiHs.632262.

3D structure databases

ProteinModelPortaliQ86VR2.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi127817. 47 interactions.
IntActiQ86VR2. 5 interactions.
STRINGi9606.ENSP00000309432.

PTM databases

PhosphoSiteiQ86VR2.

Polymorphism and mutation databases

BioMutaiFAM134C.
DMDMi74727607.

Proteomic databases

MaxQBiQ86VR2.
PaxDbiQ86VR2.
PeptideAtlasiQ86VR2.
PRIDEiQ86VR2.

Protocols and materials databases

DNASUi162427.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000309428; ENSP00000309432; ENSG00000141699.
GeneIDi162427.
KEGGihsa:162427.
UCSCiuc002ial.2. human. [Q86VR2-1]

Organism-specific databases

CTDi162427.
GeneCardsiGC17M040731.
H-InvDBHIX0020377.
HGNCiHGNC:27258. FAM134C.
HPAiHPA016492.
neXtProtiNX_Q86VR2.
PharmGKBiPA162386207.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG26663.
GeneTreeiENSGT00530000063240.
HOGENOMiHOG000050246.
HOVERGENiHBG096339.
InParanoidiQ86VR2.
OMAiWPLAVYH.
PhylomeDBiQ86VR2.
TreeFamiTF329111.

Miscellaneous databases

ChiTaRSiFAM134C. human.
GeneWikiiFAM134C.
GenomeRNAii162427.
NextBioi35469482.
PROiQ86VR2.

Gene expression databases

BgeeiQ86VR2.
CleanExiHS_FAM134C.
ExpressionAtlasiQ86VR2. baseline and differential.
GenevisibleiQ86VR2. HS.

Family and domain databases

ProtoNetiSearch...

Publicationsi

  1. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Brain and Tongue.
  2. "DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
    Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L.
    , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
    Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "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] (ISOFORM 1).
    Tissue: Brain.
  5. 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.
  6. "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].
  7. "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.
  8. "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], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "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].
  11. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  12. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-307; THR-310; SER-313 AND SER-320, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiF134C_HUMAN
AccessioniPrimary (citable) accession number: Q86VR2
Secondary accession number(s): B3KR75
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 29, 2007
Last sequence update: June 1, 2003
Last modified: July 22, 2015
This is version 80 of the entry and version 1 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 17
    Human chromosome 17: entries, gene names and cross-references to MIM
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.