AR6P4_HUMAN
ID AR6P4_HUMAN Reviewed; 237 AA.
AC Q66PJ3; A4UCR8; B3V0L0; B3V0L1; Q4F966; Q504R8; Q96BI2; Q9NR05; Q9P2R9;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT 23-FEB-2022, sequence version 3.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=ADP-ribosylation factor-like protein 6-interacting protein 4;
DE Short=ARL-6-interacting protein 4;
DE Short=Aip-4;
DE AltName: Full=HSP-975;
DE AltName: Full=HSVI-binding protein;
DE AltName: Full=SR-15;
DE AltName: Full=SRp25;
DE Short=SR-25;
DE AltName: Full=Splicing factor SRrp37;
GN Name=ARL6IP4;
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] (ISOFORMS 3 AND 7), FUNCTION, SUBCELLULAR
RP LOCATION, INTERACTION WITH SRSF2 AND ZCCHC17, ALTERNATIVE SPLICING, AND
RP TISSUE SPECIFICITY.
RX PubMed=19582790; DOI=10.1002/jcb.22255;
RA Ouyang P.;
RT "SRrp37, a novel splicing regulator located in the nuclear speckles and
RT nucleoli, interacts with SC35 and modulates alternative pre-mRNA splicing
RT in vivo.";
RL J. Cell. Biochem. 108:304-314(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
RA Zhou G., Nong W., Li H., Ke R., Shen C., Zhong G., Zheng Z., Liang M.,
RA Wen S., Lin L., Yang S.;
RL Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
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 [MRNA] (ISOFORM 1), AND PARTIAL NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] (ISOFORMS 2; 3 AND 4).
RC TISSUE=Brain, Eye, Skin, and Uterus;
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 PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 6), POSSIBLE FUNCTION,
RP PHOSPHORYLATION, DEVELOPMENTAL STAGE, AND INDUCTION.
RC TISSUE=Lung;
RX PubMed=11884129; DOI=10.1006/jmbi.2001.5318;
RA Li Q., Zhao H., Jiang L., Che Y., Dong C., Wang L., Wang J., Liu L.;
RT "An SR-protein induced by HSVI binding to cells functioning as a splicing
RT inhibitor of viral pre-mRNA.";
RL J. Mol. Biol. 316:887-894(2002).
RN [7]
RP PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
RX PubMed=10708573; DOI=10.1006/bbrc.2000.2301;
RA Sasahara K., Yamaoka T., Moritani M., Tanaka M., Iwahana H., Yoshimoto K.,
RA Miyagawa J., Kuroda Y., Itakura M.;
RT "Molecular cloning and expression analysis of a putative nuclear protein,
RT SR-25.";
RL Biochem. Biophys. Res. Commun. 269:444-450(2000).
RN [8]
RP PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RA Santana-Roman H., Curiel-Quesada E., Tapia-Ramirez J.;
RT "Searching for interaction partners of the transcription factor REST/NRSF
RT by two-hybrid screening.";
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-148, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-148, 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 [11]
RP RNA EDITING OF POSITION 286.
RX PubMed=18772245; DOI=10.1261/rna.816908;
RA Gommans W.M., Tatalias N.E., Sie C.P., Dupuis D., Vendetti N., Smith L.,
RA Kaushal R., Maas S.;
RT "Screening of human SNP database identifies recoding sites of A-to-I RNA
RT editing.";
RL RNA 14:2074-2085(2008).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-148, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-148, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-148, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [16]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-148, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-55; SER-148 AND SER-182, AND
RP IDENTIFICATION BY 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 [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-148, AND IDENTIFICATION BY
RP 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 [20]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-199, 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: Involved in modulating alternative pre-mRNA splicing with
CC either 5' distal site activation or preferential use of 3' proximal
CC site. In case of infection by Herpes simplex virus (HSVI), may act as a
CC splicing inhibitor of HSVI pre-mRNA. {ECO:0000269|PubMed:19582790}.
CC -!- SUBUNIT: Interacts with ARL6 (By similarity). Interacts with ZCCHC17.
CC Interacts with SRSF2. {ECO:0000250, ECO:0000269|PubMed:19582790}.
CC -!- INTERACTION:
CC Q66PJ3; Q9Y6K9: IKBKG; NbExp=2; IntAct=EBI-2683099, EBI-81279;
CC Q66PJ3; P78362: SRPK2; NbExp=2; IntAct=EBI-2683099, EBI-593303;
CC Q66PJ3-3; Q14498: RBM39; NbExp=3; IntAct=EBI-10248982, EBI-395290;
CC Q66PJ3-3; Q9H4P4: RNF41; NbExp=3; IntAct=EBI-10248982, EBI-2130266;
CC Q66PJ3-3; Q05519: SRSF11; NbExp=3; IntAct=EBI-10248982, EBI-1051785;
CC Q66PJ3-3; Q9NVV9: THAP1; NbExp=3; IntAct=EBI-10248982, EBI-741515;
CC Q66PJ3-4; P55212: CASP6; NbExp=3; IntAct=EBI-5280499, EBI-718729;
CC Q66PJ3-4; P06307: CCK; NbExp=3; IntAct=EBI-5280499, EBI-6624398;
CC Q66PJ3-4; O75460-2: ERN1; NbExp=3; IntAct=EBI-5280499, EBI-25852368;
CC Q66PJ3-4; P22607: FGFR3; NbExp=3; IntAct=EBI-5280499, EBI-348399;
CC Q66PJ3-4; Q0VDC6: FKBP1A; NbExp=3; IntAct=EBI-5280499, EBI-10226858;
CC Q66PJ3-4; P62993: GRB2; NbExp=2; IntAct=EBI-5280499, EBI-401755;
CC Q66PJ3-4; Q14957: GRIN2C; NbExp=3; IntAct=EBI-5280499, EBI-8285963;
CC Q66PJ3-4; Q5SUL5: HLA-A; NbExp=3; IntAct=EBI-5280499, EBI-8561769;
CC Q66PJ3-4; P30519: HMOX2; NbExp=3; IntAct=EBI-5280499, EBI-712096;
CC Q66PJ3-4; P54652: HSPA2; NbExp=3; IntAct=EBI-5280499, EBI-356991;
CC Q66PJ3-4; Q92993: KAT5; NbExp=3; IntAct=EBI-5280499, EBI-399080;
CC Q66PJ3-4; P13473-2: LAMP2; NbExp=3; IntAct=EBI-5280499, EBI-21591415;
CC Q66PJ3-4; Q8TAP4-4: LMO3; NbExp=3; IntAct=EBI-5280499, EBI-11742507;
CC Q66PJ3-4; O75489: NDUFS3; NbExp=3; IntAct=EBI-5280499, EBI-1224896;
CC Q66PJ3-4; Q92569: PIK3R3; NbExp=3; IntAct=EBI-5280499, EBI-79893;
CC Q66PJ3-4; P62937-2: PPIA; NbExp=3; IntAct=EBI-5280499, EBI-25884072;
CC Q66PJ3-4; P17252: PRKCA; NbExp=3; IntAct=EBI-5280499, EBI-1383528;
CC Q66PJ3-4; O75400-2: PRPF40A; NbExp=3; IntAct=EBI-5280499, EBI-5280197;
CC Q66PJ3-4; P62826: RAN; NbExp=3; IntAct=EBI-5280499, EBI-286642;
CC Q66PJ3-4; Q15047-2: SETDB1; NbExp=3; IntAct=EBI-5280499, EBI-9090795;
CC Q66PJ3-4; P53985-2: SLC16A1; NbExp=3; IntAct=EBI-5280499, EBI-25891616;
CC Q66PJ3-4; Q05519: SRSF11; NbExp=3; IntAct=EBI-5280499, EBI-1051785;
CC Q66PJ3-4; Q9UMX0: UBQLN1; NbExp=3; IntAct=EBI-5280499, EBI-741480;
CC Q66PJ3-4; P61981: YWHAG; NbExp=3; IntAct=EBI-5280499, EBI-359832;
CC Q66PJ3-4; Q9Y649; NbExp=3; IntAct=EBI-5280499, EBI-25900580;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:19582790}.
CC Nucleus speckle {ECO:0000269|PubMed:19582790}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=10;
CC Name=8;
CC IsoId=Q66PJ3-8; Sequence=Displayed;
CC Name=1;
CC IsoId=Q66PJ3-1; Sequence=VSP_061424;
CC Name=2;
CC IsoId=Q66PJ3-2; Sequence=VSP_061424, VSP_061428;
CC Name=3;
CC IsoId=Q66PJ3-3; Sequence=VSP_061424, VSP_061425;
CC Name=4;
CC IsoId=Q66PJ3-4; Sequence=VSP_061424, VSP_061425, VSP_061431;
CC Name=5;
CC IsoId=Q66PJ3-5; Sequence=VSP_061428, VSP_061430;
CC Name=6;
CC IsoId=Q66PJ3-6; Sequence=VSP_061424, VSP_061427, VSP_061429;
CC Name=7; Synonyms=SRrp37-2;
CC IsoId=Q66PJ3-7; Sequence=VSP_061426;
CC Name=9;
CC IsoId=Q66PJ3-9; Sequence=VSP_061425;
CC Name=10;
CC IsoId=Q66PJ3-10; Sequence=VSP_061425, VSP_061431;
CC -!- TISSUE SPECIFICITY: Isoforms 3 and 7 were identified in brain,
CC pancreas, prostate, and testis, but little or no message could be
CC detected in other tissues. {ECO:0000269|PubMed:19582790}.
CC -!- DEVELOPMENTAL STAGE: Expressed only in G1/S phase.
CC {ECO:0000269|PubMed:11884129}.
CC -!- INDUCTION: In case of Herpes simplex virus (HSVI)-binding to cells.
CC {ECO:0000269|PubMed:11884129}.
CC -!- RNA EDITING: Modified_positions=102 {ECO:0000269|PubMed:18772245};
CC Note=Partially edited. In the brain, edited at about 68%.;
CC -!- SIMILARITY: Belongs to the ARL6IP4 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF76892.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAH01958.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAH15569.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAH15909.2; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAH94839.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=ACF07995.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAA94744.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC -!- SEQUENCE CAUTION: [Isoform 6]:
CC Sequence=AAF76892.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; EU624490; ACF07995.1; ALT_INIT; mRNA.
DR EMBL; EU624491; ACF07996.1; -; mRNA.
DR EMBL; DQ099385; AAZ13761.1; -; mRNA.
DR EMBL; AC026362; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471054; EAW98374.1; -; Genomic_DNA.
DR EMBL; CH471054; EAW98376.1; -; Genomic_DNA.
DR EMBL; BC001958; AAH01958.1; ALT_INIT; mRNA.
DR EMBL; BC015569; AAH15569.1; ALT_INIT; mRNA.
DR EMBL; BC015909; AAH15909.2; ALT_INIT; mRNA.
DR EMBL; BC094839; AAH94839.1; ALT_INIT; mRNA.
DR EMBL; AF267748; AAF76892.1; ALT_SEQ; mRNA.
DR EMBL; AB035384; BAA94744.1; ALT_INIT; mRNA.
DR EMBL; EF036485; ABO65071.1; -; mRNA.
DR CCDS; CCDS31923.2; -. [Q66PJ3-8]
DR CCDS; CCDS53843.2; -. [Q66PJ3-9]
DR CCDS; CCDS61273.1; -. [Q66PJ3-7]
DR PIR; JC7220; JC7220.
DR RefSeq; NP_001002251.2; NM_001002251.2. [Q66PJ3-2]
DR RefSeq; NP_001002252.2; NM_001002252.2. [Q66PJ3-4]
DR RefSeq; NP_001265307.1; NM_001278378.1. [Q66PJ3-5]
DR RefSeq; NP_001265308.1; NM_001278379.1.
DR RefSeq; NP_001265309.1; NM_001278380.1. [Q66PJ3-7]
DR RefSeq; NP_057722.3; NM_016638.3. [Q66PJ3-3]
DR RefSeq; NP_061164.3; NM_018694.3. [Q66PJ3-1]
DR AlphaFoldDB; Q66PJ3; -.
DR BioGRID; 119477; 78.
DR IntAct; Q66PJ3; 66.
DR MINT; Q66PJ3; -.
DR STRING; 9606.ENSP00000313422; -.
DR GlyGen; Q66PJ3; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q66PJ3; -.
DR PhosphoSitePlus; Q66PJ3; -.
DR SwissPalm; Q66PJ3; -.
DR BioMuta; ARL6IP4; -.
DR DMDM; 74736329; -.
DR EPD; Q66PJ3; -.
DR jPOST; Q66PJ3; -.
DR MassIVE; Q66PJ3; -.
DR MaxQB; Q66PJ3; -.
DR PaxDb; Q66PJ3; -.
DR PeptideAtlas; Q66PJ3; -.
DR PRIDE; Q66PJ3; -.
DR ProteomicsDB; 3839; -.
DR ProteomicsDB; 65965; -. [Q66PJ3-1]
DR ProteomicsDB; 65966; -. [Q66PJ3-2]
DR ProteomicsDB; 65967; -. [Q66PJ3-3]
DR ProteomicsDB; 65968; -. [Q66PJ3-4]
DR ProteomicsDB; 65969; -. [Q66PJ3-5]
DR ProteomicsDB; 65970; -. [Q66PJ3-6]
DR Antibodypedia; 31741; 93 antibodies from 23 providers.
DR DNASU; 51329; -.
DR Ensembl; ENST00000315580.10; ENSP00000313422.7; ENSG00000182196.14. [Q66PJ3-8]
DR Ensembl; ENST00000357866.4; ENSP00000350532.4; ENSG00000182196.14. [Q66PJ3-5]
DR Ensembl; ENST00000392435.7; ENSP00000376230.4; ENSG00000182196.14. [Q66PJ3-10]
DR Ensembl; ENST00000426960.6; ENSP00000406036.2; ENSG00000182196.14. [Q66PJ3-9]
DR Ensembl; ENST00000454885.6; ENSP00000396723.2; ENSG00000182196.14. [Q66PJ3-7]
DR Ensembl; ENST00000456762.3; ENSP00000391598.3; ENSG00000182196.14. [Q66PJ3-10]
DR Ensembl; ENST00000543566.6; ENSP00000442718.3; ENSG00000182196.14. [Q66PJ3-9]
DR GeneID; 51329; -.
DR KEGG; hsa:51329; -.
DR MANE-Select; ENST00000315580.10; ENSP00000313422.7; NM_018694.4; NP_061164.4.
DR UCSC; uc001uec.5; human. [Q66PJ3-8]
DR CTD; 51329; -.
DR GeneCards; ARL6IP4; -.
DR HGNC; HGNC:18076; ARL6IP4.
DR HPA; ENSG00000182196; Low tissue specificity.
DR MIM; 607668; gene.
DR neXtProt; NX_Q66PJ3; -.
DR OpenTargets; ENSG00000182196; -.
DR PharmGKB; PA134879338; -.
DR VEuPathDB; HostDB:ENSG00000182196; -.
DR eggNOG; ENOG502RYBZ; Eukaryota.
DR GeneTree; ENSGT00390000009670; -.
DR HOGENOM; CLU_055563_0_0_1; -.
DR InParanoid; Q66PJ3; -.
DR OMA; FQMRTGM; -.
DR OrthoDB; 1047670at2759; -.
DR TreeFam; TF350468; -.
DR PathwayCommons; Q66PJ3; -.
DR SignaLink; Q66PJ3; -.
DR BioGRID-ORCS; 51329; 8 hits in 641 CRISPR screens.
DR ChiTaRS; ARL6IP4; human.
DR GeneWiki; ARL6IP4; -.
DR GenomeRNAi; 51329; -.
DR Pharos; Q66PJ3; Tbio.
DR PRO; PR:Q66PJ3; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q66PJ3; protein.
DR Bgee; ENSG00000182196; Expressed in pituitary gland and 95 other tissues.
DR ExpressionAtlas; Q66PJ3; baseline and differential.
DR Genevisible; Q66PJ3; HS.
DR GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; TAS:ProtInc.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0008380; P:RNA splicing; TAS:ProtInc.
DR InterPro; IPR019532; Nucl_RNA-splicing_assoc_SR-25.
DR Pfam; PF10500; SR-25; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Isopeptide bond; mRNA processing; mRNA splicing;
KW Nucleus; Phosphoprotein; Reference proteome; RNA editing; Ubl conjugation.
FT CHAIN 1..237
FT /note="ADP-ribosylation factor-like protein 6-interacting
FT protein 4"
FT /id="PRO_0000312270"
FT REGION 1..161
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..31
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 34..48
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 73..98
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 104..125
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 146..160
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 55
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 148
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19369195,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 182
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT CROSSLNK 199
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1
FT /note="M -> MPRCTYQLEQNPGFLPDGPGVHARAHCQDLSGPYGHEFATSESLGGR
FT VGKTRAPQSGARSRMERAGPAGEEGGAREGRLLPRAPGAWVLRACAERAALEVGAASAD
FT TGVRGCGARGPAPLLASAGGGRARDGTWGVRTKGSGAALPSRPASRAAPRPEASSPPLP
FT LEKARGGLSGPQGGRARGAM (in isoform 1, isoform 2, isoform 3,
FT isoform 6 and isoform 4)"
FT /id="VSP_061424"
FT VAR_SEQ 43..61
FT /note="Missing (in isoform 3, isoform 4, isoform 9 and
FT isoform 10)"
FT /id="VSP_061425"
FT VAR_SEQ 43..53
FT /note="Missing (in isoform 7)"
FT /id="VSP_061426"
FT VAR_SEQ 49..92
FT /note="APGAEASPSPCITERSKQKARRRTRSSSSSSSSSSSSSSSSSSS -> VPGA
FT EVLLAPLLPPRPPPLPPVMAGRSGGSTRTRGGRRRRRGRS (in isoform 6)"
FT /id="VSP_061427"
FT VAR_SEQ 54..61
FT /note="Missing (in isoform 2 and isoform 5)"
FT /id="VSP_061428"
FT VAR_SEQ 93..237
FT /note="Missing (in isoform 6)"
FT /id="VSP_061429"
FT VAR_SEQ 133..180
FT /note="Missing (in isoform 5)"
FT /id="VSP_061430"
FT VAR_SEQ 220..237
FT /note="QATRGDCLAFQMRAGLLP -> VGVAPLPAIRPQLCL (in isoform 4
FT and isoform 10)"
FT /id="VSP_061431"
FT VARIANT 102
FT /note="K -> R (in RNA edited version)"
FT /evidence="ECO:0000269|PubMed:18772245"
FT /id="VAR_058333"
FT CONFLICT 49
FT /note="A -> V (in Ref. 6; AAF76892)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 237 AA; 26375 MW; D2D0FE5374CFB802 CRC64;
MAHVGSRKRS RSRSRSRGRG SEKRKKKSRK DTSRNCSAST SQGRKASTAP GAEASPSPCI
TERSKQKARR RTRSSSSSSS SSSSSSSSSS SSSSSSSSDG RKKRGKYKDK RRKKKKKRKK
LKKKGKEKAE AQQVEALPGP SLDQWHRSAG EEEDGPVLTD EQKSRIQAMK PMTKEEWDAR
QSIIRKVVDP ETGRTRLIKG DGEVLEEIVT KERHREINKQ ATRGDCLAFQ MRAGLLP
