UniProt ID | AR2BP_HUMAN | |
---|---|---|
UniProt AC | Q9Y2Y0 | |
Protein Name | ADP-ribosylation factor-like protein 2-binding protein | |
Gene Name | ARL2BP | |
Organism | Homo sapiens (Human). | |
Sequence Length | 163 | |
Subcellular Localization | Cytoplasm. Mitochondrion intermembrane space. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Nucleus. Cytoplasm, cytoskeleton, spindle. Cytoplasm, cytoskeleton, cilium basal body. The complex formed with ARL2BP, ARL2 and SLC25A4 | |
Protein Description | 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.. | |
Protein Sequence | MDALEGESFALSFSSASDAEFDAVVGYLEDIIMDDEFQLLQRNFMDKYYLEFEDTEENKLIYTPIFNEYISLVEKYIEEQLLQRIPEFNMAAFTTTLQHHKDEVAGDIFDMLLTFTDFLAFKEMFLDYRAEKEGRGLDLSSGLVVTSLCKSSSLPASQNNLRH | |
Overview of Protein Modification Sites with Functional and Structural Information | ||
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
48 | Phosphorylation | QRNFMDKYYLEFEDT HHHHHHHCCEEEECC | 14.71 | 26074081 | |
49 | Phosphorylation | RNFMDKYYLEFEDTE HHHHHHCCEEEECCC | 12.90 | 26074081 | |
55 | Phosphorylation | YYLEFEDTEENKLIY CCEEEECCCCCEEEE | 37.69 | 26074081 | |
62 | Phosphorylation | TEENKLIYTPIFNEY CCCCEEEEEHHHHHH | 19.52 | 26074081 | |
63 | Phosphorylation | EENKLIYTPIFNEYI CCCEEEEEHHHHHHH | 11.69 | 26074081 | |
69 | Phosphorylation | YTPIFNEYISLVEKY EEHHHHHHHHHHHHH | 9.27 | 29523821 | |
71 | Phosphorylation | PIFNEYISLVEKYIE HHHHHHHHHHHHHHH | 26.01 | 29523821 | |
128 | Phosphorylation | FKEMFLDYRAEKEGR HHHHHHHHHHHHCCC | 17.55 | - | |
140 | Phosphorylation | EGRGLDLSSGLVVTS CCCCCCCCCCEEEEH | 23.25 | 29743597 | |
141 | Phosphorylation | GRGLDLSSGLVVTSL CCCCCCCCCEEEEHH | 43.36 | 22199227 | |
150 | Ubiquitination | LVVTSLCKSSSLPAS EEEEHHHHHCCCCCH | 59.68 | - | |
151 | Phosphorylation | VVTSLCKSSSLPASQ EEEHHHHHCCCCCHH | 24.94 | 29978859 | |
152 | Phosphorylation | VTSLCKSSSLPASQN EEHHHHHCCCCCHHC | 22.76 | 29978859 | |
153 | Phosphorylation | TSLCKSSSLPASQNN EHHHHHCCCCCHHCC | 45.52 | 25159151 | |
157 | Phosphorylation | KSSSLPASQNNLRH- HHCCCCCHHCCCCC- | 31.34 | 17525332 | |
162 | Methylation | PASQNNLRH------ CCHHCCCCC------ | 35.28 | - |
Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
---|---|---|---|---|---|---|
Oops, there are no upstream regulatory protein records of AR2BP_HUMAN !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of AR2BP_HUMAN !! |
* Distance = the distance between SAP position and PTM sites.
Modified Location | Modification | Variant Position (Distance <= 10) |
Residue Change | SAP | Related Disease | Reference |
---|---|---|---|---|---|---|
Oops, there are no SNP-PTM records of AR2BP_HUMAN !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
ADT1_MOUSE | Slc25a4 | physical | 11809823 | |
KCC2D_HUMAN | CAMK2D | physical | 21988832 | |
MPP3_HUMAN | MPP3 | physical | 21988832 | |
ARL2_HUMAN | ARL2 | physical | 10488091 | |
ARL3_HUMAN | ARL3 | physical | 27173435 | |
CFA20_HUMAN | CFAP20 | physical | 27173435 |
Kegg Disease | ||||||
---|---|---|---|---|---|---|
There are no disease associations of PTM sites. | ||||||
OMIM Disease | ||||||
615434 | Retinitis pigmentosa with or without situs inversus (RPSI) | |||||
Kegg Drug | ||||||
There are no disease associations of PTM sites. | ||||||
DrugBank | ||||||
There are no disease associations of PTM sites. |
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Phosphorylation | |
Reference | PubMed |
"ATM and ATR substrate analysis reveals extensive protein networksresponsive 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). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-157, AND MASSSPECTROMETRY. |