Q9Y2Y0 (AR2BP_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
ADP-ribosylation factor-like protein 2-binding protein
Short name=ARF-like 2-binding protein

Alternative name(s):
Binder of ARF2 protein 1

Gene names

Name:	ARL2BP
Synonyms:	BART, BART1

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	163 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Together with ARL2, plays a role in the nuclear translocation, retention and transcriptional activity of STAT3. May play a role as an effector of ARL2. Ref.10
Subunit structure	Found in a complex with ARL2BP, ARL2 and SLC25A6. Found in a complex with ARL2, ARL2BP and SLC25A4. Interacts with STAT2, STAT3 and STAT4. Interacts with ARL2 By similarity. Interacts with GTP bound ARL2 and ARL3; the complex ARL2-ARL2BP as well as ARL2BP alone, binds to ANT1. Interacts with STAT3; interaction is enhanced with ARL2. Ref.1 Ref.5 Ref.6 Ref.7 Ref.10 Ref.12 Ref.13
Subcellular location	Cytoplasm. Mitochondrion intermembrane space. Cytoplasm › cytoskeleton › centrosome. Nucleus. Cytoplasm › cytoskeleton › spindle. Note: The complex formed with ARL2BP, ARL2 and SLC25A4 is expressed in mitochondria By similarity. Detected in the midbody matrix. Not detected in the Golgi, nucleus and on the mitotic spindle. Centrosome-associated throughout the cell cycle. Not detected to interphase microtubules. Ref.7 Ref.8 Ref.10
Tissue specificity	Ubiquitous. Ref.1
Post-translational modification	Phosphorylated upon DNA damage, probably by ATM or ATR. Ref.9
Sequence similarities	Belongs to the ARL2BP family.

Ontologies

Keywords
Cellular component	Cytoplasm Cytoskeleton Mitochondrion Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	maintenance of protein location in nucleus Inferred from mutant phenotype Ref.10. Source: UniProtKB positive regulation of tyrosine phosphorylation of Stat3 protein Inferred from mutant phenotype Ref.10. Source: UniProtKB signal transduction Traceable author statement. Source: ProtInc
Cellular component	centrosome Inferred from direct assay Ref.8. Source: UniProtKB midbody Inferred from direct assay Ref.8. Source: UniProtKB mitochondrial intermembrane space Inferred from direct assay Ref.7. Source: UniProtKB nucleus Inferred from mutant phenotype Ref.10. Source: GOC spindle Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	protein binding Inferred from physical interaction Ref.6Ref.10Ref.13. Source: UniProtKB small GTPase regulator activity Traceable author statement. Source: ProtInc transcription coactivator activity Inferred from mutant phenotype Ref.10. Source: UniProtKB
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q9Y2Y0-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: Q9Y2Y0-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-11: Missing.
     12-13: SF → MR

Note: No experimental confirmation available.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 163

163

ADP-ribosylation factor-like protein 2-binding protein

PRO_0000287113

Amino acid modifications

Modified residue

157

1

Phosphoserine Ref.9

Natural variations

Alternative sequence

1 – 11

11

Missing in isoform 2.

VSP_025317

Alternative sequence

12 – 13

2

SF → MR in isoform 2.

VSP_025318

Natural variant

87

1

E → K.
Corresponds to variant rs7198865 [ dbSNP | Ensembl ].

VAR_053904

Experimental info

Mutagenesis

56

1

E → A: Decreases interaction with ARL2. Ref.13

Mutagenesis

57

1

E → A: Decreases interaction with ARL2. Ref.13

Mutagenesis

60

1

L → A: Decreases interaction with ARL2.

Mutagenesis

74

1

E → A: Decreases interaction with ARL2. Ref.13

Mutagenesis

76

1

Y → A: Decreases interaction with ARL2. Ref.13

Mutagenesis

109

1

F → A: Decreases interaction with ARL2. Ref.13

Mutagenesis

110

1

D → A: Decreases interaction with ARL2. Ref.13

Mutagenesis

111

1

M → A: Does not decrease interaction with ARL2. Ref.13

Mutagenesis

112

1

L → A: Decreases interaction with ARL2. Ref.13

Mutagenesis

115

1

F → A: Decreases interaction with ARL2. Ref.13

Sequence conflict

27

1

Y → C in AAH94878. Ref.4

Sequence conflict

50

1

L → Q in AAH94878. Ref.4

Sequence conflict

61

1

I → T in AAH94878. Ref.4

Sequence conflict

83

1

Q → E in AAH94878. Ref.4

Sequence conflict

87

1

E → G in AAH94878. Ref.4

Sequence conflict

154

1

L → T in AAH94878. Ref.4

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

163

Helix Strand Turn

Details...

Helix

20 – 24

5

Helix

28 – 32

5

Beta strand

33 – 35

3

Helix

36 – 48

13

Helix

49 – 51

3

Beta strand

54 – 57

4

Helix

62 – 84

23

Helix

90 – 97

8

Turn

98 – 100

3

Helix

109 – 114

6

Helix

118 – 132

15

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified November 1, 1999. Version 1. Checksum: E35EB5AC73FC1FEC	FASTA	163	18,822
	10 20 30 40 50 60 MDALEGESFA LSFSSASDAE FDAVVGYLED IIMDDEFQLL QRNFMDKYYL EFEDTEENKL 70 80 90 100 110 120 IYTPIFNEYI SLVEKYIEEQ LLQRIPEFNM AAFTTTLQHH KDEVAGDIFD MLLTFTDFLA 130 140 150 160 FKEMFLDYRA EKEGRGLDLS SGLVVTSLCK SSSLPASQNN LRH
	Isoform 2 [UniParc]. Checksum: 6CC6B4C0A11D35F4	FASTA	152	17,711
	10 20 30 40 50 60 MRSSASDAEF DAVVGYLEDI IMDDEFQLLQ RNFMDKYYLE FEDTEENKLI YTPIFNEYIS 70 80 90 100 110 120 LVEKYIEEQL LQRIPEFNMA AFTTTLQHHK DEVAGDIFDM LLTFTDFLAF KEMFLDYRAE 130 140 150 KEGRGLDLSS GLVVTSLCKS SSLPASQNNL RH

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The ARF-like 2 (ARL2)-binding protein, BART. Purification, cloning, and initial characterization." Sharer J.D., Kahn R.A. J. Biol. Chem. 274:27553-27561(1999) [PubMed: 10488091] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH ARL2, TISSUE SPECIFICITY.
[2]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Ovary.
[3]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). Tissue: Brain and Mammary gland.
[5]	"ADP-ribosylation factors (ARFs) and ARF-like 1 (ARL1) have both specific and shared effectors: characterizing ARL1-binding proteins." Van Valkenburgh H., Shern J.F., Sharer J.D., Zhu X., Kahn R.A. J. Biol. Chem. 276:22826-22837(2001) [PubMed: 11303027] [Abstract] Cited for: INTERACTION WITH ARL2 AND ARL3.
[6]	"Functional overlap between retinitis pigmentosa 2 protein and the tubulin-specific chaperone cofactor C." Bartolini F., Bhamidipati A., Thomas S., Schwahn U., Lewis S.A., Cowan N.J. J. Biol. Chem. 277:14629-14634(2002) [PubMed: 11847227] [Abstract] Cited for: INTERACTION WITH ARL2 AND ARL3.
[7]	"ARL2 and BART enter mitochondria and bind the adenine nucleotide transporter." Sharer J.D., Shern J.F., Van Valkenburgh H., Wallace D.C., Kahn R.A. Mol. Biol. Cell 13:71-83(2002) [PubMed: 11809823] [Abstract] Cited for: SUBCELLULAR LOCATION, INTERACTION WITH ANT1.
[8]	"Arl2 and Arl3 regulate different microtubule-dependent processes." Zhou C., Cunningham L., Marcus A.I., Li Y., Kahn R.A. Mol. Biol. Cell 17:2476-2487(2006) [PubMed: 16525022] [Abstract] Cited for: SUBCELLULAR LOCATION.
[9]	"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage." Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J. Science 316:1160-1166(2007) [PubMed: 17525332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-157, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[10]	"BART is essential for nuclear retention of STAT3." Muromoto R., Sekine Y., Imoto S., Ikeda O., Okayama T., Sato N., Matsuda T. Int. Immunol. 20:395-403(2008) [PubMed: 18234692] [Abstract] Cited for: FUNCTION, INTERACTION WITH STAT3 AND ARL2, SUBCELLULAR LOCATION.
[11]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]	"The structure of binder of Arl2 (BART) reveals a novel G protein binding domain: implications for function." Bailey L.K., Campbell L.J., Evetts K.A., Littlefield K., Rajendra E., Nietlispach D., Owen D., Mott H.R. J. Biol. Chem. 284:992-999(2009) [PubMed: 18981177] [Abstract] Cited for: STRUCTURE BY NMR OF 1-136, INTERACTION WITH ARL2.
[13]	"Crystal structure of the ARL2-GTP-BART complex reveals a novel recognition and binding mode of small GTPase with effector." Zhang T., Li S., Zhang Y., Zhong C., Lai Z., Ding J. Structure 17:602-610(2009) [PubMed: 19368893] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) IN A COMPLEX WITH ARL2; GTP AND MAGNESIUM IONS, INTERACTION WITH ARL2, MUTAGENESIS OF GLU-56; GLU-57; GLU-74; TYR-76; PHE-109; ASP-110; MET-111; LEU-112 AND PHE-115.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF126062 mRNA. Translation: AAD20633.1.
AK075050 mRNA. Translation: BAG52057.1.
CH471092 Genomic DNA. Translation: EAW82913.1.
BC003087 mRNA. Translation: AAH03087.1.
BC094878 mRNA. Translation: AAH94878.1.

IPI

IPI00015866.
IPI00845377.

RefSeq

NP_036238.1. NM_012106.3.

UniGene

Hs.632873.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2K9A	NMR	-	A	1-136	[»]
3DOE	X-ray	2.25	B	1-163	[»]
3DOF	X-ray	3.30	B	1-163	[»]

ProteinModelPortal

Q9Y2Y0.

SMR

Q9Y2Y0. Positions 1-136.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-48323N.

IntAct

Q9Y2Y0. 4 interactions.

STRING

Q9Y2Y0.

PTM databases

PhosphoSite

Q9Y2Y0.

Polymorphism databases

DMDM

74735245.

Proteomic databases

PRIDE

Q9Y2Y0.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000219204; ENSP00000219204; ENSG00000102931.

GeneID

23568.

KEGG

hsa:23568.

UCSC

uc002elf.1. human.

Organism-specific databases

CTD

23568.

GeneCards

GC16P057279.

H-InvDB

HIX0202295.

HGNC

HGNC:17146. ARL2BP.

neXtProt

NX_Q9Y2Y0.

PharmGKB

PA134904608.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG18020.

GeneTree

ENSGT00390000015052.

HOGENOM

HBG281257.

HOVERGEN

HBG105565.

InParanoid

Q9Y2Y0.

OMA

CIEDIIM.

OrthoDB

EOG4K6G5F.

PhylomeDB

Q9Y2Y0.

Gene expression databases

ArrayExpress

Q9Y2Y0.

Bgee

Q9Y2Y0.

CleanEx

HS_ARL2BP.

Genevestigator

Q9Y2Y0.

Family and domain databases

InterPro

IPR023379. ARF-like_2-bdp_dom.
[Graphical view]

Gene3D

G3DSA:1.20.1520.10. G3DSA:1.20.1520.10. 1 hit.

Pfam

PF11527. ARL2_Bind_BART. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

NextBio

46168.

Entry information

Entry name

AR2BP_HUMAN

Accession

Primary (citable) accession number: Q9Y2Y0
Secondary accession number(s): B3KQJ5, Q504R0

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 15, 2007
Last sequence update:	November 1, 1999
Last modified:	January 25, 2012
This is version 76 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.