Full text data of ARFIP1
ARFIP1
[Confidence: low (only semi-automatic identification from reviews)]
Arfaptin-1 (ADP-ribosylation factor-interacting protein 1)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Arfaptin-1 (ADP-ribosylation factor-interacting protein 1)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
P53367
ID ARFP1_HUMAN Reviewed; 373 AA.
AC P53367; Q2M2X4; Q3SYL4; Q9Y2X6;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
read moreDT 27-MAY-2002, sequence version 2.
DT 22-JAN-2014, entry version 111.
DE RecName: Full=Arfaptin-1;
DE AltName: Full=ADP-ribosylation factor-interacting protein 1;
GN Name=ARFIP1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A).
RX PubMed=9038142; DOI=10.1074/jbc.272.9.5421;
RA Kanoh H., Williger B.-T., Exton J.H.;
RT "Arfaptin 1, a putative cytosolic target protein of ADP-ribosylation
RT factor, is recruited to Golgi membranes.";
RL J. Biol. Chem. 272:5421-5429(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B).
RC TISSUE=Liver;
RA Premont R.T., Lefkowitz R.J.;
RT "Arfaptin-1b, a long splice variant of arfaptin-1.";
RL Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
RC TISSUE=Brain;
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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS A AND B).
RC TISSUE=Brain, 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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP INTERACTION WITH ARF1; ARF3; ARF5 AND ARF6.
RX PubMed=10413101; DOI=10.1016/S0014-5793(99)00771-1;
RA Williger B.-T., Provost J.J., Ho W.-T., Milstine J., Exton J.H.;
RT "Arfaptin 1 forms a complex with ADP-ribosylation factor and inhibits
RT phospholipase D.";
RL FEBS Lett. 454:85-89(1999).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-69 AND SER-132, AND MASS
RP SPECTROMETRY.
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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-361, AND MASS
RP SPECTROMETRY.
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 [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE
RP SCALE ANALYSIS] AT SER-5; SER-69 AND SER-79, MASS SPECTROMETRY, AND
RP CLEAVAGE OF INITIATOR METHIONINE.
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [10]
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.,
RA Buerckstuemmer T., 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 [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE
RP SCALE ANALYSIS] AT SER-132, AND MASS SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
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.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Putative target protein of ADP-ribosylation factor.
CC -!- SUBUNIT: Interacts with non-myristoylated GTP-bound ARF3, but not
CC to GDP-bound ARF3, and also to ARF1. Binds with lower affinity to
CC ARF5 and with very little affinity to ARF6.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=B; Synonyms=1b;
CC IsoId=P53367-1; Sequence=Displayed;
CC Name=A; Synonyms=1a;
CC IsoId=P53367-2; Sequence=VSP_004088;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed. Higher levels in
CC liver, pancreas, placenta, skeletal muscle and heart.
CC -!- SIMILARITY: Contains 1 AH domain.
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DR EMBL; U52521; AAA97923.1; -; mRNA.
DR EMBL; AF124489; AAD29390.1; -; mRNA.
DR EMBL; AK290472; BAF83161.1; -; mRNA.
DR EMBL; CH471056; EAX04968.1; -; Genomic_DNA.
DR EMBL; CH471056; EAX04969.1; -; Genomic_DNA.
DR EMBL; BC103759; AAI03760.1; -; mRNA.
DR EMBL; BC105114; AAI05115.1; -; mRNA.
DR EMBL; BC105116; AAI05117.1; -; mRNA.
DR EMBL; BC143675; AAI43676.1; -; mRNA.
DR PIR; G02515; G02515.
DR RefSeq; NP_001020764.1; NM_001025593.1.
DR RefSeq; NP_001020766.1; NM_001025595.1.
DR RefSeq; NP_055262.1; NM_014447.2.
DR RefSeq; XP_005262985.1; XM_005262928.1.
DR RefSeq; XP_005262986.1; XM_005262929.1.
DR UniGene; Hs.416089; -.
DR ProteinModelPortal; P53367; -.
DR SMR; P53367; 151-351.
DR IntAct; P53367; 2.
DR MINT; MINT-3019815; -.
DR STRING; 9606.ENSP00000296557; -.
DR PhosphoSite; P53367; -.
DR DMDM; 21264399; -.
DR PaxDb; P53367; -.
DR PRIDE; P53367; -.
DR Ensembl; ENST00000353617; ENSP00000296557; ENSG00000164144.
DR Ensembl; ENST00000356064; ENSP00000348360; ENSG00000164144.
DR Ensembl; ENST00000405727; ENSP00000384189; ENSG00000164144.
DR Ensembl; ENST00000451320; ENSP00000395083; ENSG00000164144.
DR GeneID; 27236; -.
DR KEGG; hsa:27236; -.
DR UCSC; uc003imz.3; human.
DR CTD; 27236; -.
DR GeneCards; GC04P153701; -.
DR HGNC; HGNC:21496; ARFIP1.
DR HPA; CAB005080; -.
DR MIM; 605928; gene.
DR neXtProt; NX_P53367; -.
DR PharmGKB; PA134920621; -.
DR eggNOG; NOG302946; -.
DR HOGENOM; HOG000236308; -.
DR HOVERGEN; HBG050564; -.
DR InParanoid; P53367; -.
DR OMA; TKNPAME; -.
DR OrthoDB; EOG7VQJD9; -.
DR PhylomeDB; P53367; -.
DR ChiTaRS; ARFIP1; human.
DR GeneWiki; ARFIP1; -.
DR GenomeRNAi; 27236; -.
DR NextBio; 50103; -.
DR PRO; PR:P53367; -.
DR ArrayExpress; P53367; -.
DR Bgee; P53367; -.
DR CleanEx; HS_ARFIP1; -.
DR Genevestigator; P53367; -.
DR GO; GO:0005829; C:cytosol; IDA:MGI.
DR GO; GO:0000139; C:Golgi membrane; IDA:UniProtKB.
DR GO; GO:0006886; P:intracellular protein transport; IDA:MGI.
DR GO; GO:0050708; P:regulation of protein secretion; IDA:MGI.
DR Gene3D; 1.20.1270.60; -; 1.
DR InterPro; IPR027267; AH/BAR-dom.
DR InterPro; IPR010504; AH_dom.
DR Pfam; PF06456; Arfaptin; 1.
DR SMART; SM01015; Arfaptin; 1.
DR PROSITE; PS50870; AH; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Complete proteome; Phosphoprotein;
KW Reference proteome.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 373 Arfaptin-1.
FT /FTId=PRO_0000064665.
FT DOMAIN 153 353 AH.
FT MOD_RES 2 2 N-acetylalanine.
FT MOD_RES 5 5 Phosphoserine.
FT MOD_RES 69 69 Phosphoserine.
FT MOD_RES 79 79 Phosphoserine.
FT MOD_RES 132 132 Phosphoserine.
FT MOD_RES 361 361 Phosphothreonine.
FT VAR_SEQ 69 100 Missing (in isoform A).
FT /FTId=VSP_004088.
SQ SEQUENCE 373 AA; 41738 MW; 7A315D0E67DECDBF CRC64;
MAQESPKNSA AEIPVTSNGE VDDSREHSFN RDLKHSLPSG LGLSETQITS HGFDNTKEGV
IEAGAFQGSP APPLPSVMSP SRVAASRLAQ QGSDLIVPAG GQRTQTKSGP VILADEIKNP
AMEKLELVRK WSLNTYKCTR QIISEKLGRG SRTVDLELEA QIDILRDNKK KYENILKLAQ
TLSTQLFQMV HTQRQLGDAF ADLSLKSLEL HEEFGYNADT QKLLAKNGET LLGAINFFIA
SVNTLVNKTI EDTLMTVKQY ESARIEYDAY RTDLEELNLG PRDANTLPKI EQSQHLFQAH
KEKYDKMRND VSVKLKFLEE NKVKVLHNQL VLFHNAIAAY FAGNQKQLEQ TLKQFHIKLK
TPGVDAPSWL EEQ
//
ID ARFP1_HUMAN Reviewed; 373 AA.
AC P53367; Q2M2X4; Q3SYL4; Q9Y2X6;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
read moreDT 27-MAY-2002, sequence version 2.
DT 22-JAN-2014, entry version 111.
DE RecName: Full=Arfaptin-1;
DE AltName: Full=ADP-ribosylation factor-interacting protein 1;
GN Name=ARFIP1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A).
RX PubMed=9038142; DOI=10.1074/jbc.272.9.5421;
RA Kanoh H., Williger B.-T., Exton J.H.;
RT "Arfaptin 1, a putative cytosolic target protein of ADP-ribosylation
RT factor, is recruited to Golgi membranes.";
RL J. Biol. Chem. 272:5421-5429(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B).
RC TISSUE=Liver;
RA Premont R.T., Lefkowitz R.J.;
RT "Arfaptin-1b, a long splice variant of arfaptin-1.";
RL Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
RC TISSUE=Brain;
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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS A AND B).
RC TISSUE=Brain, 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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP INTERACTION WITH ARF1; ARF3; ARF5 AND ARF6.
RX PubMed=10413101; DOI=10.1016/S0014-5793(99)00771-1;
RA Williger B.-T., Provost J.J., Ho W.-T., Milstine J., Exton J.H.;
RT "Arfaptin 1 forms a complex with ADP-ribosylation factor and inhibits
RT phospholipase D.";
RL FEBS Lett. 454:85-89(1999).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-69 AND SER-132, AND MASS
RP SPECTROMETRY.
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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-361, AND MASS
RP SPECTROMETRY.
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 [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE
RP SCALE ANALYSIS] AT SER-5; SER-69 AND SER-79, MASS SPECTROMETRY, AND
RP CLEAVAGE OF INITIATOR METHIONINE.
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [10]
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.,
RA Buerckstuemmer T., 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 [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE
RP SCALE ANALYSIS] AT SER-132, AND MASS SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
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.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Putative target protein of ADP-ribosylation factor.
CC -!- SUBUNIT: Interacts with non-myristoylated GTP-bound ARF3, but not
CC to GDP-bound ARF3, and also to ARF1. Binds with lower affinity to
CC ARF5 and with very little affinity to ARF6.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=B; Synonyms=1b;
CC IsoId=P53367-1; Sequence=Displayed;
CC Name=A; Synonyms=1a;
CC IsoId=P53367-2; Sequence=VSP_004088;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed. Higher levels in
CC liver, pancreas, placenta, skeletal muscle and heart.
CC -!- SIMILARITY: Contains 1 AH domain.
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DR EMBL; U52521; AAA97923.1; -; mRNA.
DR EMBL; AF124489; AAD29390.1; -; mRNA.
DR EMBL; AK290472; BAF83161.1; -; mRNA.
DR EMBL; CH471056; EAX04968.1; -; Genomic_DNA.
DR EMBL; CH471056; EAX04969.1; -; Genomic_DNA.
DR EMBL; BC103759; AAI03760.1; -; mRNA.
DR EMBL; BC105114; AAI05115.1; -; mRNA.
DR EMBL; BC105116; AAI05117.1; -; mRNA.
DR EMBL; BC143675; AAI43676.1; -; mRNA.
DR PIR; G02515; G02515.
DR RefSeq; NP_001020764.1; NM_001025593.1.
DR RefSeq; NP_001020766.1; NM_001025595.1.
DR RefSeq; NP_055262.1; NM_014447.2.
DR RefSeq; XP_005262985.1; XM_005262928.1.
DR RefSeq; XP_005262986.1; XM_005262929.1.
DR UniGene; Hs.416089; -.
DR ProteinModelPortal; P53367; -.
DR SMR; P53367; 151-351.
DR IntAct; P53367; 2.
DR MINT; MINT-3019815; -.
DR STRING; 9606.ENSP00000296557; -.
DR PhosphoSite; P53367; -.
DR DMDM; 21264399; -.
DR PaxDb; P53367; -.
DR PRIDE; P53367; -.
DR Ensembl; ENST00000353617; ENSP00000296557; ENSG00000164144.
DR Ensembl; ENST00000356064; ENSP00000348360; ENSG00000164144.
DR Ensembl; ENST00000405727; ENSP00000384189; ENSG00000164144.
DR Ensembl; ENST00000451320; ENSP00000395083; ENSG00000164144.
DR GeneID; 27236; -.
DR KEGG; hsa:27236; -.
DR UCSC; uc003imz.3; human.
DR CTD; 27236; -.
DR GeneCards; GC04P153701; -.
DR HGNC; HGNC:21496; ARFIP1.
DR HPA; CAB005080; -.
DR MIM; 605928; gene.
DR neXtProt; NX_P53367; -.
DR PharmGKB; PA134920621; -.
DR eggNOG; NOG302946; -.
DR HOGENOM; HOG000236308; -.
DR HOVERGEN; HBG050564; -.
DR InParanoid; P53367; -.
DR OMA; TKNPAME; -.
DR OrthoDB; EOG7VQJD9; -.
DR PhylomeDB; P53367; -.
DR ChiTaRS; ARFIP1; human.
DR GeneWiki; ARFIP1; -.
DR GenomeRNAi; 27236; -.
DR NextBio; 50103; -.
DR PRO; PR:P53367; -.
DR ArrayExpress; P53367; -.
DR Bgee; P53367; -.
DR CleanEx; HS_ARFIP1; -.
DR Genevestigator; P53367; -.
DR GO; GO:0005829; C:cytosol; IDA:MGI.
DR GO; GO:0000139; C:Golgi membrane; IDA:UniProtKB.
DR GO; GO:0006886; P:intracellular protein transport; IDA:MGI.
DR GO; GO:0050708; P:regulation of protein secretion; IDA:MGI.
DR Gene3D; 1.20.1270.60; -; 1.
DR InterPro; IPR027267; AH/BAR-dom.
DR InterPro; IPR010504; AH_dom.
DR Pfam; PF06456; Arfaptin; 1.
DR SMART; SM01015; Arfaptin; 1.
DR PROSITE; PS50870; AH; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Complete proteome; Phosphoprotein;
KW Reference proteome.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 373 Arfaptin-1.
FT /FTId=PRO_0000064665.
FT DOMAIN 153 353 AH.
FT MOD_RES 2 2 N-acetylalanine.
FT MOD_RES 5 5 Phosphoserine.
FT MOD_RES 69 69 Phosphoserine.
FT MOD_RES 79 79 Phosphoserine.
FT MOD_RES 132 132 Phosphoserine.
FT MOD_RES 361 361 Phosphothreonine.
FT VAR_SEQ 69 100 Missing (in isoform A).
FT /FTId=VSP_004088.
SQ SEQUENCE 373 AA; 41738 MW; 7A315D0E67DECDBF CRC64;
MAQESPKNSA AEIPVTSNGE VDDSREHSFN RDLKHSLPSG LGLSETQITS HGFDNTKEGV
IEAGAFQGSP APPLPSVMSP SRVAASRLAQ QGSDLIVPAG GQRTQTKSGP VILADEIKNP
AMEKLELVRK WSLNTYKCTR QIISEKLGRG SRTVDLELEA QIDILRDNKK KYENILKLAQ
TLSTQLFQMV HTQRQLGDAF ADLSLKSLEL HEEFGYNADT QKLLAKNGET LLGAINFFIA
SVNTLVNKTI EDTLMTVKQY ESARIEYDAY RTDLEELNLG PRDANTLPKI EQSQHLFQAH
KEKYDKMRND VSVKLKFLEE NKVKVLHNQL VLFHNAIAAY FAGNQKQLEQ TLKQFHIKLK
TPGVDAPSWL EEQ
//
MIM
605928
*RECORD*
*FIELD* NO
605928
*FIELD* TI
*605928 ADP-RIBOSYLATION FACTOR-INTERACTING PROTEIN 1; ARFIP1
;;ARFAPTIN 1
*FIELD* TX
read more
DESCRIPTION
ADP-ribosylation factors, or ARFs (e.g., ARF1; 103180), enhance the ADP
ribosyltransferase activity of cholera toxin and are implicated in
vesicle transport between endoplasmic reticulum and the Golgi complex.
Arfaptin-1 interacts with class I ARFs only in their GTP-bound
conformation and is recruited to Golgi membranes by GTP-bound ARF (Kanoh
et al., 1997).
CLONING
A gln71-to-leu (Q71L) or gln71-to-ile (Q71I) mutation in the ARF1 gene
slows the rate of GTP hydrolysis, thereby making the mutant
constitutively active (Teal et al., 1994). Using a yeast 2-hybrid screen
of an HL60 cDNA library with an ARF3 (103190) Q71L mutant as bait, Kanoh
et al. (1997) obtained cDNAs encoding arfaptin-1 and arfaptin-2 (601638)
(the name arfaptin derives from ARF and the Greek word 'apto,' meaning
'I bind to'). Sequence analysis predicted that the 341-amino acid
arfaptin-1 protein, which is 60% identical to arfaptin-2, contains a
leucine zipper motif, which is interrupted with a met at position 157,
and several potential phosphorylation sites. Northern blot analysis
revealed ubiquitous expression of a 3.4-kb transcript that was
relatively higher in liver, pancreas, placenta, skeletal muscle, and
heart. In vitro binding analysis showed that arfaptin-1 binds to
nonmyristoylated GTP-bound ARF3, but not to GDP-bound ARF3, and also to
ARF1, another class I ARF. It binds with lower affinity to ARF5
(103188), a class II ARF, and with very little affinity to ARF6
(600464), a class III ARF. Immunoblot analysis indicated that arfaptin-1
is recruited from the cytosol to Golgi membranes by ARFs in a guanosine
5-prime-O-(3-thiotriphosphate)-dependent and brefeldin A-sensitive
manner but is not a constituent of coatomer (see COPB; 600959).
GENE FUNCTION
Williger et al. (1999) found increased association of arfaptin-1 with
membranes in the presence of myristoylated ARF (myrARF). Mutation
analysis established that residues 64 to 116 and 266 to 341 of
arfaptin-1 are required for ARF binding. Both binding sites are required
for arfaptin-1 inhibition of PLD1 (602382) activation by myrARF3 in
vitro.
*FIELD* RF
1. Kanoh, H.; Williger, B.-T.; Exton, J. H.: Arfaptin 1, a putative
cytosolic target protein of ADP-ribosylation factor, is recruited
to Golgi membranes. J. Biol. Chem. 272: 5421-5429, 1997.
2. Teal, S. B.; Hsu, V. W.; Peters, P. J.; Klausner, R. D.; Donaldson,
J. G.: An activating mutation in ARF1 stabilizes coatomer binding
to Golgi membranes. J. Biol. Chem. 269: 3135-3138, 1994.
3. Williger, B.-T.; Provost, J. J.; Ho, W.-T.; Milstine, J.; Exton,
J. H.: Arfaptin 1 forms a complex with ADP-ribosylation factor and
inhibits phospholipase D. FEBS Lett. 454: 85-89, 1999.
*FIELD* CD
Paul J. Converse: 5/14/2001
*FIELD* ED
alopez: 03/22/2012
alopez: 10/20/2005
mgross: 5/14/2001
*RECORD*
*FIELD* NO
605928
*FIELD* TI
*605928 ADP-RIBOSYLATION FACTOR-INTERACTING PROTEIN 1; ARFIP1
;;ARFAPTIN 1
*FIELD* TX
read more
DESCRIPTION
ADP-ribosylation factors, or ARFs (e.g., ARF1; 103180), enhance the ADP
ribosyltransferase activity of cholera toxin and are implicated in
vesicle transport between endoplasmic reticulum and the Golgi complex.
Arfaptin-1 interacts with class I ARFs only in their GTP-bound
conformation and is recruited to Golgi membranes by GTP-bound ARF (Kanoh
et al., 1997).
CLONING
A gln71-to-leu (Q71L) or gln71-to-ile (Q71I) mutation in the ARF1 gene
slows the rate of GTP hydrolysis, thereby making the mutant
constitutively active (Teal et al., 1994). Using a yeast 2-hybrid screen
of an HL60 cDNA library with an ARF3 (103190) Q71L mutant as bait, Kanoh
et al. (1997) obtained cDNAs encoding arfaptin-1 and arfaptin-2 (601638)
(the name arfaptin derives from ARF and the Greek word 'apto,' meaning
'I bind to'). Sequence analysis predicted that the 341-amino acid
arfaptin-1 protein, which is 60% identical to arfaptin-2, contains a
leucine zipper motif, which is interrupted with a met at position 157,
and several potential phosphorylation sites. Northern blot analysis
revealed ubiquitous expression of a 3.4-kb transcript that was
relatively higher in liver, pancreas, placenta, skeletal muscle, and
heart. In vitro binding analysis showed that arfaptin-1 binds to
nonmyristoylated GTP-bound ARF3, but not to GDP-bound ARF3, and also to
ARF1, another class I ARF. It binds with lower affinity to ARF5
(103188), a class II ARF, and with very little affinity to ARF6
(600464), a class III ARF. Immunoblot analysis indicated that arfaptin-1
is recruited from the cytosol to Golgi membranes by ARFs in a guanosine
5-prime-O-(3-thiotriphosphate)-dependent and brefeldin A-sensitive
manner but is not a constituent of coatomer (see COPB; 600959).
GENE FUNCTION
Williger et al. (1999) found increased association of arfaptin-1 with
membranes in the presence of myristoylated ARF (myrARF). Mutation
analysis established that residues 64 to 116 and 266 to 341 of
arfaptin-1 are required for ARF binding. Both binding sites are required
for arfaptin-1 inhibition of PLD1 (602382) activation by myrARF3 in
vitro.
*FIELD* RF
1. Kanoh, H.; Williger, B.-T.; Exton, J. H.: Arfaptin 1, a putative
cytosolic target protein of ADP-ribosylation factor, is recruited
to Golgi membranes. J. Biol. Chem. 272: 5421-5429, 1997.
2. Teal, S. B.; Hsu, V. W.; Peters, P. J.; Klausner, R. D.; Donaldson,
J. G.: An activating mutation in ARF1 stabilizes coatomer binding
to Golgi membranes. J. Biol. Chem. 269: 3135-3138, 1994.
3. Williger, B.-T.; Provost, J. J.; Ho, W.-T.; Milstine, J.; Exton,
J. H.: Arfaptin 1 forms a complex with ADP-ribosylation factor and
inhibits phospholipase D. FEBS Lett. 454: 85-89, 1999.
*FIELD* CD
Paul J. Converse: 5/14/2001
*FIELD* ED
alopez: 03/22/2012
alopez: 10/20/2005
mgross: 5/14/2001