ID   AR2BP_HUMAN             Reviewed;         163 AA.
AC   Q9Y2Y0; B3KQJ5; Q504R0;
DT   15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   05-OCT-2010, entry version 64.
DE   RecName: Full=ADP-ribosylation factor-like protein 2-binding protein;
DE            Short=ARF-like 2-binding protein;
DE   AltName: Full=Binder of ARF2 protein 1;
GN   Name=ARL2BP; Synonyms=BART, BART1;
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 1), INTERACTION WITH ARL2, AND
RP   TISSUE SPECIFICITY.
RX   MEDLINE=99419033; PubMed=10488091; DOI=10.1074/jbc.274.39.27553;
RA   Sharer J.D., Kahn R.A.;
RT   "The ARF-like 2 (ARL2)-binding protein, BART. Purification, cloning,
RT   and initial characterization.";
RL   J. Biol. Chem. 274:27553-27561(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Ovary;
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   TISSUE=Brain, and Mammary gland;
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   [5]
RP   INTERACTION WITH ARL2 AND ARL3.
RX   MEDLINE=21303655; PubMed=11303027; DOI=10.1074/jbc.M102359200;
RA   Van Valkenburgh H., Shern J.F., Sharer J.D., Zhu X., Kahn R.A.;
RT   "ADP-ribosylation factors (ARFs) and ARF-like 1 (ARL1) have both
RT   specific and shared effectors: characterizing ARL1-binding proteins.";
RL   J. Biol. Chem. 276:22826-22837(2001).
RN   [6]
RP   SUBCELLULAR LOCATION, AND INTERACTION WITH ANT1.
RX   PubMed=11809823; DOI=10.1091/mbc.01-05-0245;
RA   Sharer J.D., Shern J.F., Van Valkenburgh H., Wallace D.C., Kahn R.A.;
RT   "ARL2 and BART enter mitochondria and bind the adenine nucleotide
RT   transporter.";
RL   Mol. Biol. Cell 13:71-83(2002).
RN   [7]
RP   SUBCELLULAR LOCATION.
RX   PubMed=16525022; DOI=10.1091/mbc.E05-10-0929;
RA   Zhou C., Cunningham L., Marcus A.I., Li Y., Kahn R.A.;
RT   "Arl2 and Arl3 regulate different microtubule-dependent processes.";
RL   Mol. Biol. Cell 17:2476-2487(2006).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-157, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic kidney;
RX   PubMed=17525332; DOI=10.1126/science.1140321;
RA   Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,
RA   Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,
RA   Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
RT   "ATM and ATR substrate analysis reveals extensive protein networks
RT   responsive to DNA damage.";
RL   Science 316:1160-1166(2007).
RN   [9]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RA   Colinge J., Superti-Furga G., Bennett K.L.;
RL   Submitted (OCT-2008) to UniProtKB.
CC   -!- FUNCTION: May play a role as an effector of the ADP-ribosylation
CC       factor-like protein 2, ARL2.
CC   -!- SUBUNIT: Interacts with GTP bound ARL2 and ARL3; the complex ARL2-
CC       ARL2BP as well as ARL2BP alone, binds to ANT1.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Mitochondrion intermembrane
CC       space. Cytoplasm, cytoskeleton, centrosome.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9Y2Y0-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9Y2Y0-2; Sequence=VSP_025317, VSP_025318;
CC         Note=No experimental confirmation available;
CC   -!- TISSUE SPECIFICITY: Ubiquitous.
CC   -!- PTM: Phosphorylated upon DNA damage, probably by ATM or ATR.
CC   -!- SIMILARITY: Belongs to the ARL2BP family.
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DR   EMBL; AF126062; AAD20633.1; -; mRNA.
DR   EMBL; AK075050; BAG52057.1; -; mRNA.
DR   EMBL; CH471092; EAW82913.1; -; Genomic_DNA.
DR   EMBL; BC003087; AAH03087.1; -; mRNA.
DR   EMBL; BC094878; AAH94878.1; -; mRNA.
DR   IPI; IPI00015866; -.
DR   IPI; IPI00845377; -.
DR   RefSeq; NP_036238.1; -.
DR   UniGene; Hs.632873; -.
DR   UniGene; Hs.723856; -.
DR   PDB; 2K9A; NMR; -; A=1-136.
DR   PDB; 3DOE; X-ray; 2.25 A; B=1-163.
DR   PDB; 3DOF; X-ray; 3.30 A; B=1-163.
DR   PDBsum; 2K9A; -.
DR   PDBsum; 3DOE; -.
DR   PDBsum; 3DOF; -.
DR   ProteinModelPortal; Q9Y2Y0; -.
DR   DIP; DIP-48323N; -.
DR   STRING; Q9Y2Y0; -.
DR   PhosphoSite; Q9Y2Y0; -.
DR   PRIDE; Q9Y2Y0; -.
DR   Ensembl; ENST00000219204; ENSP00000219204; ENSG00000102931.
DR   GeneID; 23568; -.
DR   KEGG; hsa:23568; -.
DR   UCSC; uc002elf.1; human.
DR   CTD; 23568; -.
DR   GeneCards; GC16P057279; -.
DR   HGNC; HGNC:17146; ARL2BP.
DR   PharmGKB; PA134904608; -.
DR   eggNOG; prNOG18020; -.
DR   HOGENOM; HBG281257; -.
DR   HOVERGEN; HBG105565; -.
DR   InParanoid; Q9Y2Y0; -.
DR   OMA; CIEDIIM; -.
DR   OrthoDB; EOG9B5RQV; -.
DR   PhylomeDB; Q9Y2Y0; -.
DR   NextBio; 46168; -.
DR   ArrayExpress; Q9Y2Y0; -.
DR   Bgee; Q9Y2Y0; -.
DR   CleanEx; HS_ARL2BP; -.
DR   Genevestigator; Q9Y2Y0; -.
DR   GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
DR   GO; GO:0005758; C:mitochondrial intermembrane space; IEA:UniProtKB-SubCell.
DR   GO; GO:0005083; F:small GTPase regulator activity; TAS:ProtInc.
DR   GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR   InterPro; IPR021606; ARL2_Bind_BART.
DR   Pfam; PF11527; ARL2_Bind_BART; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Complete proteome; Cytoplasm;
KW   Cytoskeleton; Mitochondrion; Phosphoprotein; Polymorphism.
FT   CHAIN         1    163       ADP-ribosylation factor-like protein 2-
FT                                binding protein.
FT                                /FTId=PRO_0000287113.
FT   MOD_RES     157    157       Phosphoserine.
FT   VAR_SEQ       1     11       Missing (in isoform 2).
FT                                /FTId=VSP_025317.
FT   VAR_SEQ      12     13       SF -> MR (in isoform 2).
FT                                /FTId=VSP_025318.
FT   VARIANT      87     87       E -> K (in dbSNP:rs7198865).
FT                                /FTId=VAR_053904.
FT   CONFLICT     27     27       Y -> C (in Ref. 4; AAH94878).
FT   CONFLICT     50     50       L -> Q (in Ref. 4; AAH94878).
FT   CONFLICT     61     61       I -> T (in Ref. 4; AAH94878).
FT   CONFLICT     83     83       Q -> E (in Ref. 4; AAH94878).
FT   CONFLICT     87     87       E -> G (in Ref. 4; AAH94878).
FT   CONFLICT    154    154       L -> T (in Ref. 4; AAH94878).
FT   HELIX        20     24
FT   HELIX        28     32
FT   STRAND       33     35
FT   HELIX        36     48
FT   HELIX        49     51
FT   STRAND       54     57
FT   HELIX        62     84
FT   HELIX        90     97
FT   TURN         98    100
FT   HELIX       109    114
FT   HELIX       118    132
SQ   SEQUENCE   163 AA;  18822 MW;  E35EB5AC73FC1FEC CRC64;
     MDALEGESFA LSFSSASDAE FDAVVGYLED IIMDDEFQLL QRNFMDKYYL EFEDTEENKL
     IYTPIFNEYI SLVEKYIEEQ LLQRIPEFNM AAFTTTLQHH KDEVAGDIFD MLLTFTDFLA
     FKEMFLDYRA EKEGRGLDLS SGLVVTSLCK SSSLPASQNN LRH
//