UniProt Accession

 ARL8B_HUMAN; Q9NVJ2 

Genbank Protein ID

 AB118751; AK001564; CR457264; BC013131; BC063125 

Genbank Nucleotide ID

 BAD23992.1; BAA91759.1; CAG33545.1; AAH13131.1; AAH63125.1 

Protein Name

 ADP-ribosylation factor-like protein 8B 

Protein Synonyms/Alias

 ADP-ribosylation factor-like protein 10C; Novel small G protein indispensable for equal chromosome segregation 1 

Gene Name

 ARL8B 

Gene Synonyms/Alias

 ARL10C; GIE1 

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
68	TKGNVTIKIWDIGGQ	ubiquitination	[1]
141	LPNALDEKQLIEKMN	ubiquitination	[1, 2, 3, 4, 5, 6, 7, 8, 9, 10]
146	DEKQLIEKMNLSAIQ	ubiquitination	[1, 3, 9, 10]
182	QWLIQHSKSRRS***	ubiquitination	[3]

Reference

 [1] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
 [2] Mass spectrometric analysis of lysine ubiquitylation reveals promiscuity at site level.
 Danielsen JM, Sylvestersen KB, Bekker-Jensen S, Szklarczyk D, Poulsen JW, Horn H, Jensen LJ, Mailand N, Nielsen ML.
 Mol Cell Proteomics. 2011 Mar;10(3):M110.003590. [PMID: 21139048]
 [3] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [4] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [5] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
 [6] Ubiquitin ligase substrate identification through quantitative proteomics at both the protein and peptide levels.
 Lee KA, Hammerle LP, Andrews PS, Stokes MP, Mustelin T, Silva JC, Black RA, Doedens JR.
 J Biol Chem. 2011 Dec 2;286(48):41530-8. [PMID: 21987572]
 [7] Proteome-wide identification of ubiquitylation sites by conjugation of engineered lysine-less ubiquitin.
 Oshikawa K, Matsumoto M, Oyamada K, Nakayama KI.
 J Proteome Res. 2012 Feb 3;11(2):796-807. [PMID: 22053931]
 [8] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]
 [9] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [10] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302] 

Functional Description

 May play a role in lysosome motility (PubMed:16537643). May play a role in chromosome segregation (PubMed:15331635). 

Sequence Annotation

 NP_BIND 29 35 GTP.
 NP_BIND 71 75 GTP (By similarity).
 NP_BIND 130 133 GTP.
 MOD_RES 1 1 N-acetylmethionine.  

Keyword

 3D-structure; Acetylation; Cell cycle; Cell division; Complete proteome; Cytoplasm; Cytoskeleton; Direct protein sequencing; Endosome; GTP-binding; Lysosome; Membrane; Nucleotide-binding; Reference proteome. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 186 AA 

Protein Sequence

Gene Ontology

 GO:0005737; C:cytoplasm; IDA:UniProtKB.
 GO:0031902; C:late endosome membrane; IEA:UniProtKB-SubCell.
 GO:0005765; C:lysosomal membrane; IEA:UniProtKB-SubCell.
 GO:0030496; C:midbody; IDA:UniProtKB.
 GO:0051233; C:spindle midzone; IDA:UniProtKB.
 GO:0043014; F:alpha-tubulin binding; IDA:UniProtKB.
 GO:0048487; F:beta-tubulin binding; IDA:UniProtKB.
 GO:0019003; F:GDP binding; IDA:UniProtKB.
 GO:0005525; F:GTP binding; IDA:UniProtKB.
 GO:0003924; F:GTPase activity; NAS:UniProtKB.
 GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
 GO:0051301; P:cell division; IEA:UniProtKB-KW.
 GO:0007059; P:chromosome segregation; IMP:UniProtKB.
 GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro. 

Interpro

 IPR027417; P-loop_NTPase.
 IPR005225; Small_GTP-bd_dom.
 IPR024156; Small_GTPase_ARF.
 IPR006689; Small_GTPase_ARF/SAR. 

Pfam

 PF00025; Arf 

SMART

 SM00177; ARF 

PROSITE

 PS51417; ARF 

PRINTS

 PR00328; SAR1GTPBP.