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Protein

ADP-ribosylation factor-like protein 2-binding protein

Gene

Arl2bp

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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 (By similarity).By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Enzyme and pathway databases

ReactomeiR-MMU-422356. Regulation of insulin secretion.

Names & Taxonomyi

Protein namesi
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 namesi
Name:Arl2bp
Synonyms:Bart, Bart1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 8

Organism-specific databases

MGIiMGI:1349429. Arl2bp.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell projection, Cilium, Cytoplasm, Cytoskeleton, Mitochondrion, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 163163ADP-ribosylation factor-like protein 2-binding proteinPRO_0000287115Add
BLAST

Proteomic databases

EPDiQ9D385.
MaxQBiQ9D385.
PaxDbiQ9D385.
PeptideAtlasiQ9D385.
PRIDEiQ9D385.

PTM databases

iPTMnetiQ9D385.
PhosphoSiteiQ9D385.

Expressioni

Tissue specificityi

Widely expressed, with most abundant activity in brain, especially in hippocampus and cortex. Also expressed in lung, cerebellum, liver, kidney, retina, spleen, muscle and heart (at protein level).4 Publications

Gene expression databases

BgeeiQ9D385.
CleanExiMM_ARL2BP.
GenevisibleiQ9D385. MM.

Interactioni

Subunit structurei

Interacts with GTP bound ARL2 and ARL3; the complex ARL2-ARL2BP as well as ARL2BP alone, binds to ANT1. Interaction with ARL2 may be required for targeting to cilia basal body (By similarity). Interacts with STAT3; interaction is enhanced with ARL2. Found in a complex with ARL2BP, ARL2 and SLC25A6 (By similarity). Found in a complex with ARL2, ARL2BP and SLC25A4. Interacts with STAT2, STAT3 and STAT4.By similarity2 Publications

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000034228.

Structurei

3D structure databases

ProteinModelPortaliQ9D385.
SMRiQ9D385. Positions 14-133.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ARL2BP family.Curated

Phylogenomic databases

eggNOGiENOG410IKTQ. Eukaryota.
ENOG4111IGT. LUCA.
GeneTreeiENSGT00390000015052.
HOGENOMiHOG000024955.
HOVERGENiHBG105565.
InParanoidiQ9D385.
KOiK16742.
OMAiFMAFKEM.
OrthoDBiEOG7BCNDK.
PhylomeDBiQ9D385.
TreeFamiTF315143.

Family and domain databases

Gene3Di1.20.1520.10. 1 hit.
InterProiIPR023379. ARF-like_2-bdp_dom.
[Graphical view]
PfamiPF11527. ARL2_Bind_BART. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9D385-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MDALEEESFA LSFSSASDAE FDAVVGCLED IIMDDEFQLL QRNFMDKYYQ
60 70 80 90 100
EFEDTEENKL TYTPIFNEYI SLVEKYIEEQ LLERIPGFNM AAFTTTLQHH
110 120 130 140 150
KDEVAGDIFD MLLTFTDFLA FKEMFLDYRA EKEGRGLDLS SGLVVTSLCK
160
SSSTPASQNN LRH
Length:163
Mass (Da):18,754
Last modified:June 1, 2001 - v1
Checksum:iAE489178C0382255
GO
Isoform 2 (identifier: Q9D385-2) [UniParc]FASTAAdd to basket

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

Show »
Length:152
Mass (Da):17,571
Checksum:i4DE5F01744ED1E58
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 1111Missing in isoform 2. 1 PublicationVSP_025320Add
BLAST
Alternative sequencei12 – 132SF → MR in isoform 2. 1 PublicationVSP_025319

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK006418 mRNA. Translation: BAB24578.1.
AK006646 mRNA. Translation: BAB24686.1.
AK018229 mRNA. Translation: BAB31126.1.
AK155242 mRNA. Translation: BAE33143.1.
AK161325 mRNA. Translation: BAE36323.1.
CT010168 mRNA. Translation: CAJ18376.1.
BC002131 mRNA. Translation: AAH02131.1.
BC024708 mRNA. Translation: AAH24708.1.
CCDSiCCDS22545.1. [Q9D385-1]
CCDS40440.1. [Q9D385-2]
RefSeqiNP_077153.1. NM_024191.2. [Q9D385-1]
NP_077231.1. NM_024269.4. [Q9D385-2]
UniGeneiMm.393247.

Genome annotation databases

EnsembliENSMUST00000034228; ENSMUSP00000034228; ENSMUSG00000031776. [Q9D385-1]
ENSMUST00000109527; ENSMUSP00000105153; ENSMUSG00000031776. [Q9D385-2]
GeneIDi107566.
KEGGimmu:107566.
UCSCiuc009mwt.3. mouse. [Q9D385-1]
uc009mwu.3. mouse. [Q9D385-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK006418 mRNA. Translation: BAB24578.1.
AK006646 mRNA. Translation: BAB24686.1.
AK018229 mRNA. Translation: BAB31126.1.
AK155242 mRNA. Translation: BAE33143.1.
AK161325 mRNA. Translation: BAE36323.1.
CT010168 mRNA. Translation: CAJ18376.1.
BC002131 mRNA. Translation: AAH02131.1.
BC024708 mRNA. Translation: AAH24708.1.
CCDSiCCDS22545.1. [Q9D385-1]
CCDS40440.1. [Q9D385-2]
RefSeqiNP_077153.1. NM_024191.2. [Q9D385-1]
NP_077231.1. NM_024269.4. [Q9D385-2]
UniGeneiMm.393247.

3D structure databases

ProteinModelPortaliQ9D385.
SMRiQ9D385. Positions 14-133.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000034228.

PTM databases

iPTMnetiQ9D385.
PhosphoSiteiQ9D385.

Proteomic databases

EPDiQ9D385.
MaxQBiQ9D385.
PaxDbiQ9D385.
PeptideAtlasiQ9D385.
PRIDEiQ9D385.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000034228; ENSMUSP00000034228; ENSMUSG00000031776. [Q9D385-1]
ENSMUST00000109527; ENSMUSP00000105153; ENSMUSG00000031776. [Q9D385-2]
GeneIDi107566.
KEGGimmu:107566.
UCSCiuc009mwt.3. mouse. [Q9D385-1]
uc009mwu.3. mouse. [Q9D385-2]

Organism-specific databases

CTDi23568.
MGIiMGI:1349429. Arl2bp.

Phylogenomic databases

eggNOGiENOG410IKTQ. Eukaryota.
ENOG4111IGT. LUCA.
GeneTreeiENSGT00390000015052.
HOGENOMiHOG000024955.
HOVERGENiHBG105565.
InParanoidiQ9D385.
KOiK16742.
OMAiFMAFKEM.
OrthoDBiEOG7BCNDK.
PhylomeDBiQ9D385.
TreeFamiTF315143.

Enzyme and pathway databases

ReactomeiR-MMU-422356. Regulation of insulin secretion.

Miscellaneous databases

PROiQ9D385.
SOURCEiSearch...

Gene expression databases

BgeeiQ9D385.
CleanExiMM_ARL2BP.
GenevisibleiQ9D385. MM.

Family and domain databases

Gene3Di1.20.1520.10. 1 hit.
InterProiIPR023379. ARF-like_2-bdp_dom.
[Graphical view]
PfamiPF11527. ARL2_Bind_BART. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
    Strain: C57BL/6J and NOD.
    Tissue: Medulla oblongata and Testis.
  2. "Cloning of mouse full open reading frames in Gateway(R) system entry vector (pDONR201)."
    Ebert L., Muenstermann E., Schatten R., Henze S., Bohn E., Mollenhauer J., Wiemann S., Schick M., Korn B.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  3. "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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Strain: FVB/N.
    Tissue: Mammary tumor.
  4. "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] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION, TISSUE SPECIFICITY.
  5. "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] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN A COMPLEX WITH ARL2 AND SLC25A4, INTERACTION WITH ARL2, TISSUE SPECIFICITY.
  6. Cited for: INTERACTION WITH STAT2; STAT3 AND STAT4, TISSUE SPECIFICITY.
  7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Heart, Kidney, Lung, Spleen and Testis.
  8. Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY.

Entry informationi

Entry nameiAR2BP_MOUSE
AccessioniPrimary (citable) accession number: Q9D385
Secondary accession number(s): Q9CQW6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 15, 2007
Last sequence update: June 1, 2001
Last modified: July 6, 2016
This is version 107 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.