FA8A1_HUMAN
ID FA8A1_HUMAN Reviewed; 413 AA.
AC Q9UBU6; B2R725;
DT 25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Protein FAM8A1;
DE AltName: Full=Autosomal highly conserved protein;
GN Name=FAM8A1; Synonyms=AHCP;
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], AND TISSUE SPECIFICITY.
RX PubMed=11707071; DOI=10.1006/geno.2001.6642;
RA Jamain S., Girondot M., Leroy P., Clergue M., Quach H., Fellous M.,
RA Bourgeron T.;
RT "Transduction of the human gene FAM8A1 by endogenous retrovirus during
RT primate evolution.";
RL Genomics 78:38-45(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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 [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=15144186; DOI=10.1021/ac035352d;
RA Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M.,
RA Peters E.C.;
RT "Robust phosphoproteomic profiling of tyrosine phosphorylation sites from
RT human T cells using immobilized metal affinity chromatography and tandem
RT mass spectrometry.";
RL Anal. Chem. 76:2763-2772(2004).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-229, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-229, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and 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 [10]
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 [11]
RP FUNCTION, IDENTIFICATION IN THE HRD1 COMPLEX, AND MUTAGENESIS OF
RP 120-TRP--TRP-122 AND TRP-131.
RX PubMed=28827405; DOI=10.1242/jcs.206847;
RA Schulz J., Avci D., Queisser M.A., Gutschmidt A., Dreher L.S., Fenech E.J.,
RA Volkmar N., Hayashi Y., Hoppe T., Christianson J.C.;
RT "Conserved cytoplasmic domains promote Hrd1 ubiquitin ligase complex
RT formation for ER-associated degradation (ERAD).";
RL J. Cell Sci. 130:3322-3335(2017).
CC -!- FUNCTION: Plays a role in the assembly of the HRD1 complex, a complex
CC involved in the ubiquitin-proteasome-dependent process of ER-associated
CC degradation (ERAD). {ECO:0000269|PubMed:28827405}.
CC -!- SUBUNIT: Component of the HRD1 complex, which comprises at least
CC SYNV1/HRD1, FAM8A1, HERPUD1/HERP, OS9, SEL1L and UBE2J1. This
CC interaction stabilizes FAM8A1 protein, preventing its proteasomal
CC degradation. FAM8A1 binding to SYNV1 may promote recruitment of HERPUD1
CC to the HRD1 complex. {ECO:0000269|PubMed:28827405}.
CC -!- INTERACTION:
CC Q9UBU6; Q86TM6: SYVN1; NbExp=20; IntAct=EBI-6309101, EBI-947849;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed, with a higher level of
CC expression in testis. {ECO:0000269|PubMed:11707071}.
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DR EMBL; AF097027; AAF07850.1; -; mRNA.
DR EMBL; AK312814; BAG35672.1; -; mRNA.
DR EMBL; AL138824; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AF097026; AAF07849.1; -; Genomic_DNA.
DR EMBL; CH471087; EAW55382.1; -; Genomic_DNA.
DR EMBL; BC047881; AAH47881.1; -; mRNA.
DR CCDS; CCDS4540.1; -.
DR RefSeq; NP_057339.1; NM_016255.2.
DR AlphaFoldDB; Q9UBU6; -.
DR BioGRID; 119541; 93.
DR CORUM; Q9UBU6; -.
DR IntAct; Q9UBU6; 43.
DR MINT; Q9UBU6; -.
DR STRING; 9606.ENSP00000259963; -.
DR TCDB; 2.A.133.1.4; the rdd na+(li+)(k+)/h+ antiporter (rdd) family.
DR iPTMnet; Q9UBU6; -.
DR PhosphoSitePlus; Q9UBU6; -.
DR BioMuta; FAM8A1; -.
DR DMDM; 74753230; -.
DR EPD; Q9UBU6; -.
DR jPOST; Q9UBU6; -.
DR MassIVE; Q9UBU6; -.
DR MaxQB; Q9UBU6; -.
DR PaxDb; Q9UBU6; -.
DR PeptideAtlas; Q9UBU6; -.
DR PRIDE; Q9UBU6; -.
DR ProteomicsDB; 84070; -.
DR Antibodypedia; 68212; 102 antibodies from 16 providers.
DR DNASU; 51439; -.
DR Ensembl; ENST00000259963.4; ENSP00000259963.3; ENSG00000137414.7.
DR GeneID; 51439; -.
DR KEGG; hsa:51439; -.
DR MANE-Select; ENST00000259963.4; ENSP00000259963.3; NM_016255.3; NP_057339.1.
DR UCSC; uc003ncc.4; human.
DR CTD; 51439; -.
DR DisGeNET; 51439; -.
DR GeneCards; FAM8A1; -.
DR HGNC; HGNC:16372; FAM8A1.
DR HPA; ENSG00000137414; Low tissue specificity.
DR MIM; 618409; gene.
DR neXtProt; NX_Q9UBU6; -.
DR OpenTargets; ENSG00000137414; -.
DR PharmGKB; PA27986; -.
DR VEuPathDB; HostDB:ENSG00000137414; -.
DR eggNOG; KOG4647; Eukaryota.
DR GeneTree; ENSGT00390000007346; -.
DR HOGENOM; CLU_053631_1_0_1; -.
DR InParanoid; Q9UBU6; -.
DR OMA; GDHEPVP; -.
DR OrthoDB; 1123503at2759; -.
DR PhylomeDB; Q9UBU6; -.
DR TreeFam; TF314024; -.
DR PathwayCommons; Q9UBU6; -.
DR SignaLink; Q9UBU6; -.
DR SIGNOR; Q9UBU6; -.
DR BioGRID-ORCS; 51439; 9 hits in 1080 CRISPR screens.
DR GenomeRNAi; 51439; -.
DR Pharos; Q9UBU6; Tbio.
DR PRO; PR:Q9UBU6; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q9UBU6; protein.
DR Bgee; ENSG00000137414; Expressed in Brodmann (1909) area 23 and 209 other tissues.
DR ExpressionAtlas; Q9UBU6; baseline and differential.
DR Genevisible; Q9UBU6; HS.
DR GO; GO:0000836; C:Hrd1p ubiquitin ligase complex; IDA:FlyBase.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IC:FlyBase.
DR InterPro; IPR039871; FAM8A1.
DR InterPro; IPR010432; RDD.
DR PANTHER; PTHR13659; PTHR13659; 1.
DR Pfam; PF06271; RDD; 1.
PE 1: Evidence at protein level;
KW Membrane; Phosphoprotein; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..413
FT /note="Protein FAM8A1"
FT /id="PRO_0000087167"
FT TRANSMEM 257..277
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 304..324
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 371..391
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 242..408
FT /note="RDD"
FT REGION 1..105
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 107..139
FT /note="Necessary and sufficient to interact with SYVN1"
FT /evidence="ECO:0000269|PubMed:28827405"
FT REGION 217..236
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..18
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 30..50
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 229
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MUTAGEN 120..122
FT /note="WLW->ALA: Decreased interaction with SYVN1 and
FT HERPUD1."
FT /evidence="ECO:0000269|PubMed:28827405"
FT MUTAGEN 131
FT /note="W->A: Decreased interaction with HERPUD1; no effect
FT on interaction with SYVN1."
FT /evidence="ECO:0000269|PubMed:28827405"
SQ SEQUENCE 413 AA; 44123 MW; 35B92497907CCD2E CRC64;
MAEGPEEARG HPPGQDDGGG DHEPVPSLRG PPTTAVPCPR DDPQAEPQAP GRPTAPGLAA
AAAADKLEPP RELRKRGEAA SGSGAELQEQ AGCEAPEAAA PRERPARLSA REYSRQVHEW
LWQSYCGYLT WHSGLAAFPA YCSPQPSPQS FPSGGAAVPQ AAAPPPPQLG YYNPFYFLSP
GAAGPDPRTA AGISTPAPVA GLGPRAPHVQ ASVRATPVTR VGSAAPSRSP SETGRQAGRE
YVIPSLAHRF MAEMVDFFIL FFIKATIVLS IMHLSGIKDI SKFAMHYIIE EIDEDTSMED
LQKMMVVALI YRLLVCFYEI ICIWGAGGAT PGKFLLGLRV VTCDTSVLIA PSRVLVIPSS
NVSITTSTIR ALIKNFSIAS FFPAFITLLF FQHNRTAYDI VAGTIVVKRN GVR
