AR2BP_HUMAN - dbPTM
AR2BP_HUMAN - PTM Information in dbPTM
Basic Information of Protein
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
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
48PhosphorylationQRNFMDKYYLEFEDT
HHHHHHHCCEEEECC
14.7126074081
49PhosphorylationRNFMDKYYLEFEDTE
HHHHHHCCEEEECCC
12.9026074081
55PhosphorylationYYLEFEDTEENKLIY
CCEEEECCCCCEEEE
37.6926074081
62PhosphorylationTEENKLIYTPIFNEY
CCCCEEEEEHHHHHH
19.5226074081
63PhosphorylationEENKLIYTPIFNEYI
CCCEEEEEHHHHHHH
11.6926074081
69PhosphorylationYTPIFNEYISLVEKY
EEHHHHHHHHHHHHH
9.2729523821
71PhosphorylationPIFNEYISLVEKYIE
HHHHHHHHHHHHHHH
26.0129523821
128PhosphorylationFKEMFLDYRAEKEGR
HHHHHHHHHHHHCCC
17.55-
140PhosphorylationEGRGLDLSSGLVVTS
CCCCCCCCCCEEEEH
23.2529743597
141PhosphorylationGRGLDLSSGLVVTSL
CCCCCCCCCEEEEHH
43.3622199227
150UbiquitinationLVVTSLCKSSSLPAS
EEEEHHHHHCCCCCH
59.68-
151PhosphorylationVVTSLCKSSSLPASQ
EEEHHHHHCCCCCHH
24.9429978859
152PhosphorylationVTSLCKSSSLPASQN
EEHHHHHCCCCCHHC
22.7629978859
153PhosphorylationTSLCKSSSLPASQNN
EHHHHHCCCCCHHCC
45.5225159151
157PhosphorylationKSSSLPASQNNLRH-
HHCCCCCHHCCCCC-
31.3417525332
162MethylationPASQNNLRH------
CCHHCCCCC------
35.28-

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
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 !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of AR2BP_HUMAN !!

Disease-associated PTM Sites based on SAP

* 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 !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ADT1_MOUSESlc25a4physical
11809823
KCC2D_HUMANCAMK2Dphysical
21988832
MPP3_HUMANMPP3physical
21988832
ARL2_HUMANARL2physical
10488091
ARL3_HUMANARL3physical
27173435
CFA20_HUMANCFAP20physical
27173435

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
615434Retinitis 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.
Regulatory Network of AR2BP_HUMAN

loading...

Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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.

TOP