AL14E_HUMAN
ID AL14E_HUMAN Reviewed; 260 AA.
AC Q8N8R7; Q5HYH9;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=ARL14 effector protein;
DE AltName: Full=ARF7 effector protein;
GN Name=ARL14EP; Synonyms=ARF7EP, C11orf46;
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 [LARGE SCALE MRNA].
RC TISSUE=Teratocarcinoma;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Heart;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Skin;
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 [4]
RP FUNCTION, INTERACTION WITH ARL14 AND MYO1E, SUBCELLULAR LOCATION, AND
RP TISSUE SPECIFICITY.
RX PubMed=21458045; DOI=10.1016/j.cell.2011.03.023;
RA Paul P., van den Hoorn T., Jongsma M.L., Bakker M.J., Hengeveld R.,
RA Janssen L., Cresswell P., Egan D.A., van Ham M., Ten Brinke A., Ovaa H.,
RA Beijersbergen R.L., Kuijl C., Neefjes J.;
RT "A Genome-wide multidimensional RNAi screen reveals pathways controlling
RT MHC class II antigen presentation.";
RL Cell 145:268-283(2011).
RN [5]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-183, 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 [7]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-177, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
CC -!- FUNCTION: Through its interaction with ARL14 and MYO1E, may connect MHC
CC class II-containing cytoplasmic vesicles to the actin network and hence
CC controls the movement of these vesicles along the actin cytoskeleton in
CC dendritic cells. {ECO:0000269|PubMed:21458045}.
CC -!- SUBUNIT: Interacts with ARL14 and MYO1E. {ECO:0000269|PubMed:21458045}.
CC -!- INTERACTION:
CC Q8N8R7; Q8N4G2: ARL14; NbExp=3; IntAct=EBI-2807994, EBI-3921493;
CC Q8N8R7; Q63ZY3: KANK2; NbExp=3; IntAct=EBI-2807994, EBI-2556193;
CC Q8N8R7; Q12965: MYO1E; NbExp=2; IntAct=EBI-2807994, EBI-4279548;
CC Q8N8R7; Q96T68: SETDB2; NbExp=4; IntAct=EBI-2807994, EBI-1222089;
CC Q8N8R7; Q96T68-2: SETDB2; NbExp=6; IntAct=EBI-2807994, EBI-12346707;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21458045}.
CC -!- TISSUE SPECIFICITY: Expressed in the immune system.
CC {ECO:0000269|PubMed:21458045}.
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DR EMBL; AK096287; BAC04747.1; -; mRNA.
DR EMBL; BX647617; CAI46092.1; -; mRNA.
DR EMBL; BC047775; AAH47775.1; -; mRNA.
DR CCDS; CCDS7869.1; -.
DR RefSeq; NP_689529.1; NM_152316.2.
DR AlphaFoldDB; Q8N8R7; -.
DR BioGRID; 125690; 15.
DR IntAct; Q8N8R7; 12.
DR STRING; 9606.ENSP00000282032; -.
DR iPTMnet; Q8N8R7; -.
DR PhosphoSitePlus; Q8N8R7; -.
DR BioMuta; ARL14EP; -.
DR DMDM; 74729511; -.
DR EPD; Q8N8R7; -.
DR jPOST; Q8N8R7; -.
DR MassIVE; Q8N8R7; -.
DR MaxQB; Q8N8R7; -.
DR PaxDb; Q8N8R7; -.
DR PeptideAtlas; Q8N8R7; -.
DR PRIDE; Q8N8R7; -.
DR ProteomicsDB; 72456; -.
DR Antibodypedia; 53638; 118 antibodies from 19 providers.
DR DNASU; 120534; -.
DR Ensembl; ENST00000282032.4; ENSP00000282032.3; ENSG00000152219.5.
DR GeneID; 120534; -.
DR KEGG; hsa:120534; -.
DR MANE-Select; ENST00000282032.4; ENSP00000282032.3; NM_152316.3; NP_689529.1.
DR UCSC; uc001mso.2; human.
DR CTD; 120534; -.
DR DisGeNET; 120534; -.
DR GeneCards; ARL14EP; -.
DR HGNC; HGNC:26798; ARL14EP.
DR HPA; ENSG00000152219; Low tissue specificity.
DR MIM; 612295; gene.
DR neXtProt; NX_Q8N8R7; -.
DR OpenTargets; ENSG00000152219; -.
DR PharmGKB; PA142672291; -.
DR VEuPathDB; HostDB:ENSG00000152219; -.
DR eggNOG; KOG4850; Eukaryota.
DR GeneTree; ENSGT00940000156586; -.
DR HOGENOM; CLU_093502_0_0_1; -.
DR InParanoid; Q8N8R7; -.
DR OMA; CMQIING; -.
DR OrthoDB; 1056242at2759; -.
DR PhylomeDB; Q8N8R7; -.
DR TreeFam; TF333216; -.
DR PathwayCommons; Q8N8R7; -.
DR SignaLink; Q8N8R7; -.
DR BioGRID-ORCS; 120534; 20 hits in 1076 CRISPR screens.
DR ChiTaRS; ARL14EP; human.
DR GenomeRNAi; 120534; -.
DR Pharos; Q8N8R7; Tdark.
DR PRO; PR:Q8N8R7; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q8N8R7; protein.
DR Bgee; ENSG00000152219; Expressed in secondary oocyte and 179 other tissues.
DR ExpressionAtlas; Q8N8R7; baseline and differential.
DR Genevisible; Q8N8R7; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005925; C:focal adhesion; IDA:HPA.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR InterPro; IPR029264; ARF7EP_C.
DR InterPro; IPR026515; ARL14EP.
DR PANTHER; PTHR46536; PTHR46536; 1.
DR Pfam; PF14949; ARF7EP_C; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cytoplasm; Isopeptide bond; Phosphoprotein;
KW Reference proteome; Ubl conjugation.
FT CHAIN 1..260
FT /note="ARL14 effector protein"
FT /id="PRO_0000251892"
FT REGION 160..182
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 164..179
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 183
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT CROSSLNK 177
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VARIANT 180
FT /note="T -> P (in dbSNP:rs7940297)"
FT /id="VAR_033740"
FT CONFLICT 88
FT /note="K -> KK (in Ref. 2; CAI46092)"
FT /evidence="ECO:0000305"
FT CONFLICT 245
FT /note="Q -> QK (in Ref. 2; CAI46092)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 260 AA; 29338 MW; 18B70E7DB57B3252 CRC64;
MMDPCSVGVQ LRTTNECHKT YYTRHTGFKT LQELSSNDML LLQLRTGMTL SGNNTICFHH
VKIYIDRFED LQKSCCDPFN IHKKLAKKNL HVIDLDDATF LSAKFGRQLV PGWKLCPKCT
QIINGSVDVD TEDRQKRKPE SDGRTAKALR SLQFTNPGRQ TEFAPETGKR EKRRLTKNAT
AGSDRQVIPA KSKVYDSQGL LIFSGMDLCD CLDEDCLGCF YACPACGSTK CGAECRCDRK
WLYEQIEIEG GEIIHNKHAG
