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Protein

Protein FAM134A

Gene

FAM134A

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Names & Taxonomyi

Protein namesi
Recommended name:
Protein FAM134A
Gene namesi
Name:FAM134A
Synonyms:C2orf17
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 2

Organism-specific databases

HGNCiHGNC:28450. FAM134A.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei12 – 3221HelicalSequence analysisAdd
BLAST
Transmembranei100 – 12021HelicalSequence analysisAdd
BLAST
Transmembranei204 – 22421HelicalSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA162386165.

Polymorphism and mutation databases

BioMutaiFAM134A.
DMDMi296439357.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 543543Protein FAM134APRO_0000089346Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei279 – 2791PhosphothreonineCombined sources
Modified residuei281 – 2811PhosphoserineCombined sources
Modified residuei283 – 2831PhosphoserineCombined sources
Modified residuei291 – 2911PhosphoserineCombined sources
Modified residuei311 – 3111PhosphoserineCombined sources
Modified residuei334 – 3341PhosphothreonineBy similarity
Modified residuei337 – 3371PhosphoserineBy similarity
Modified residuei344 – 3441PhosphoserineCombined sources
Modified residuei347 – 3471PhosphoserineCombined sources
Modified residuei385 – 3851PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ8NC44.
MaxQBiQ8NC44.
PaxDbiQ8NC44.
PeptideAtlasiQ8NC44.
PRIDEiQ8NC44.

PTM databases

iPTMnetiQ8NC44.
PhosphoSiteiQ8NC44.

Expressioni

Gene expression databases

BgeeiQ8NC44.
CleanExiHS_FAM134A.
ExpressionAtlasiQ8NC44. baseline and differential.
GenevisibleiQ8NC44. HS.

Organism-specific databases

HPAiHPA011170.

Interactioni

Subunit structurei

Interacts with ATG8 family modifier proteins MAP1LC3A, MAP1LC3B, GABARAP, and GABARAPL1.1 Publication

Protein-protein interaction databases

BioGridi122558. 25 interactions.
DIPiDIP-56781N.
IntActiQ8NC44. 18 interactions.
MINTiMINT-1374706.
STRINGi9606.ENSP00000395249.

Structurei

3D structure databases

ProteinModelPortaliQ8NC44.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi490 – 4956LIR motif1 Publication

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi4 – 3128Gly-richAdd
BLAST
Compositional biasi97 – 1004Poly-Ser
Compositional biasi386 – 3905Poly-Glu
Compositional biasi482 – 4854Poly-Glu

Domaini

The LIR motif interacts with ATG8 family proteins.1 Publication

Sequence similaritiesi

Belongs to the FAM134 family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG410IE8D. Eukaryota.
ENOG4111EY9. LUCA.
GeneTreeiENSGT00530000063240.
HOGENOMiHOG000116418.
HOVERGENiHBG093247.
InParanoidiQ8NC44.
OMAiPDGVKCS.
OrthoDBiEOG7J70FV.
PhylomeDBiQ8NC44.
TreeFamiTF329111.

Sequencei

Sequence statusi: Complete.

Q8NC44-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASGGGGGNT GAGGGPGMGL SLGLGLGLSL GMSEATSEAE EEAATAEAVG
60 70 80 90 100
RLATTLWLRL RGWEAVLAAA QRLLVWEKPL HSLVTAAALN GLFWLLSSSS
110 120 130 140 150
LRPFFLLSVS LLAYFLLDLW QPRFLPDVSA SSPEEPHSDS EGAGSGARPH
160 170 180 190 200
LLSVPELCRY LAESWLTFQI HLQELLQYKR QNPAQFCVRV CSGCAVLAVL
210 220 230 240 250
GHYVPGIMIS YIVLLSILLW PLVVYHELIQ RMYTRLEPLL MQLDYSMKAE
260 270 280 290 300
ANALHHKHDK RKRQGKNAPP GGDEPLAETE SESEAELAGF SPVVDVKKTA
310 320 330 340 350
LALAITDSEL SDEEASILES GGFSVSRATT PQLTDVSEDL DQQSLPSEPE
360 370 380 390 400
ETLSRDLGEG EEGELAPPED LLGRPQALSR QALDSEEEEE DVAAKETLLR
410 420 430 440 450
LSSPLHFVNT HFNGAGSPPD GVKCSPGGPV ETLSPETVSG GLTALPGTLS
460 470 480 490 500
PPLCLVGSDP APSPSILPPV PQDSPQPLPA PEEEEALTTE DFELLDQGEL
510 520 530 540
EQLNAELGLE PETPPKPPDA PPLGPDIHSL VQSDQEAQAV AEP
Length:543
Mass (Da):57,830
Last modified:May 18, 2010 - v3
Checksum:i03DD659722BA9E5B
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti338 – 3381E → G in BAC11332 (PubMed:14702039).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti374 – 3741R → H.
Corresponds to variant rs3210652 [ dbSNP | Ensembl ].
VAR_033720
Natural varianti419 – 4191P → Q.Combined sources2 Publications
Corresponds to variant rs3731900 [ dbSNP | Ensembl ].
VAR_022835

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK074983 mRNA. Translation: BAC11332.1.
AC068946 Genomic DNA. No translation available.
BC064950 mRNA. Translation: AAH64950.1.
AL136758 mRNA. Translation: CAB66692.2.
CCDSiCCDS2434.1.
RefSeqiNP_077269.3. NM_024293.5.
UniGeneiHs.516707.

Genome annotation databases

EnsembliENST00000430297; ENSP00000395249; ENSG00000144567.
GeneIDi79137.
KEGGihsa:79137.
UCSCiuc002vjw.5. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK074983 mRNA. Translation: BAC11332.1.
AC068946 Genomic DNA. No translation available.
BC064950 mRNA. Translation: AAH64950.1.
AL136758 mRNA. Translation: CAB66692.2.
CCDSiCCDS2434.1.
RefSeqiNP_077269.3. NM_024293.5.
UniGeneiHs.516707.

3D structure databases

ProteinModelPortaliQ8NC44.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi122558. 25 interactions.
DIPiDIP-56781N.
IntActiQ8NC44. 18 interactions.
MINTiMINT-1374706.
STRINGi9606.ENSP00000395249.

PTM databases

iPTMnetiQ8NC44.
PhosphoSiteiQ8NC44.

Polymorphism and mutation databases

BioMutaiFAM134A.
DMDMi296439357.

Proteomic databases

EPDiQ8NC44.
MaxQBiQ8NC44.
PaxDbiQ8NC44.
PeptideAtlasiQ8NC44.
PRIDEiQ8NC44.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000430297; ENSP00000395249; ENSG00000144567.
GeneIDi79137.
KEGGihsa:79137.
UCSCiuc002vjw.5. human.

Organism-specific databases

CTDi79137.
GeneCardsiFAM134A.
H-InvDBHIX0002850.
HGNCiHGNC:28450. FAM134A.
HPAiHPA011170.
neXtProtiNX_Q8NC44.
PharmGKBiPA162386165.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IE8D. Eukaryota.
ENOG4111EY9. LUCA.
GeneTreeiENSGT00530000063240.
HOGENOMiHOG000116418.
HOVERGENiHBG093247.
InParanoidiQ8NC44.
OMAiPDGVKCS.
OrthoDBiEOG7J70FV.
PhylomeDBiQ8NC44.
TreeFamiTF329111.

Miscellaneous databases

ChiTaRSiFAM134A. human.
GenomeRNAii79137.
PROiQ8NC44.

Gene expression databases

BgeeiQ8NC44.
CleanExiHS_FAM134A.
ExpressionAtlasiQ8NC44. baseline and differential.
GenevisibleiQ8NC44. HS.

Family and domain databases

ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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], VARIANT GLN-419.
  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. "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] OF 262-543, VARIANT GLN-419.
    Tissue: Skin.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 431-543.
    Tissue: Testis.
  5. Cited for: SEQUENCE REVISION.
  6. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-311 AND SER-385, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-385, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Platelet.
  8. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-279; SER-281 AND SER-283, VARIANT [LARGE SCALE ANALYSIS] GLN-419, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. "Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography."
    Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., Zou H., Gu J.
    Proteomics 8:1346-1361(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-385, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  10. "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-344 AND SER-347, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  11. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-385, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. "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-385, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "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-385, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma and Erythroleukemia.
  14. "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 SER-291; SER-311; SER-347 AND SER-385, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  15. Cited for: INTERACTION WITH MAP1LC3A; MAP1LC3B; GABARAP AND GABARAPL1, DOMAIN.

Entry informationi

Entry nameiF134A_HUMAN
AccessioniPrimary (citable) accession number: Q8NC44
Secondary accession number(s): Q6P1P5, Q9H0K7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 5, 2005
Last sequence update: May 18, 2010
Last modified: July 6, 2016
This is version 105 of the entry and version 3 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. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. 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.