RIP_HUMAN - dbPTM
RIP_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RIP_HUMAN
UniProt AC Q86UA6
Protein Name RPA-interacting protein
Gene Name RPAIN
Organism Homo sapiens (Human).
Sequence Length 219
Subcellular Localization Isoform 1: Cytoplasm. Nucleus.
Isoform 2: Nucleus, PML body.
Protein Description Mediates the import of RPA complex into the nucleus, possibly via some interaction with importin beta. Isoform 2 is sumoylated and mediates the localization of RPA complex into the PML body of the nucleus, thereby participating in RPA function in DNA metabolism..
Protein Sequence MAESLRSPRRSLYKLVGSPPWKEAFRQRCLERMRNSRDRLLNRYRQAGSSGPGNSQNSFLVQEVMEEEWNALQSVENCPEDLAQLEELIDMAVLEEIQQELINQEQSIISEYEKSLQFDEKCLSIMLAEWEANPLICPVCTKYNLRITSGVVVCQCGLSIPSHSSELTEQKLRACLEGSINEHSAHCPHTPEFSVTGGTEEKSSLLMSCLACDTWAVIL
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
4Phosphorylation----MAESLRSPRRS
----CCHHHCCCCHH
21.3930108239
6Methylation--MAESLRSPRRSLY
--CCHHHCCCCHHHH
54.62115368269
7Phosphorylation-MAESLRSPRRSLYK
-CCHHHCCCCHHHHH
28.2229255136
11PhosphorylationSLRSPRRSLYKLVGS
HHCCCCHHHHHHHCC
37.0126074081
13PhosphorylationRSPRRSLYKLVGSPP
CCCCHHHHHHHCCCH
11.97-
14 (in isoform 5)Ubiquitination-41.8321890473
14 (in isoform 1)Ubiquitination-41.8321890473
14 (in isoform 2)Ubiquitination-41.8321890473
14UbiquitinationSPRRSLYKLVGSPPW
CCCHHHHHHHCCCHH
41.8321890473
14 (in isoform 3)Ubiquitination-41.8321890473
14 (in isoform 4)Ubiquitination-41.8321890473
14 (in isoform 6)Ubiquitination-41.8321890473
14 (in isoform 7)Ubiquitination-41.8321890473
14UbiquitinationSPRRSLYKLVGSPPW
CCCHHHHHHHCCCHH
41.8321890473
18PhosphorylationSLYKLVGSPPWKEAF
HHHHHHCCCHHHHHH
21.9525159151
22UbiquitinationLVGSPPWKEAFRQRC
HHCCCHHHHHHHHHH
44.9621890473
22 (in isoform 5)Ubiquitination-44.9621890473
22 (in isoform 4)Ubiquitination-44.9621890473
22 (in isoform 3)Ubiquitination-44.9621890473
22 (in isoform 6)Ubiquitination-44.9621890473
22 (in isoform 7)Ubiquitination-44.9621890473
22 (in isoform 2)Ubiquitination-44.9621890473
22 (in isoform 1)Ubiquitination-44.9621890473
22UbiquitinationLVGSPPWKEAFRQRC
HHCCCHHHHHHHHHH
44.962189047
36PhosphorylationCLERMRNSRDRLLNR
HHHHHHHHHHHHHHH
25.7829978859
112 (in isoform 8)Phosphorylation-23.1327642862
114UbiquitinationSIISEYEKSLQFDEK
HHHHHHHHHHCCCHH
56.41-
121SumoylationKSLQFDEKCLSIMLA
HHHCCCHHHHHHHHH
42.1716135809
148PhosphorylationTKYNLRITSGVVVCQ
CCCCCEECCCEEEEE
17.0021406692
149PhosphorylationKYNLRITSGVVVCQC
CCCCEECCCEEEEEC
27.5021406692
159PhosphorylationVVCQCGLSIPSHSSE
EEEECCCCCCCCCHH
20.1021406692
162PhosphorylationQCGLSIPSHSSELTE
ECCCCCCCCCHHHHH
34.0421406692
164PhosphorylationGLSIPSHSSELTEQK
CCCCCCCCHHHHHHH
29.8221406692
165PhosphorylationLSIPSHSSELTEQKL
CCCCCCCHHHHHHHH
31.0721406692
168PhosphorylationPSHSSELTEQKLRAC
CCCCHHHHHHHHHHH
32.1121406692
171UbiquitinationSSELTEQKLRACLEG
CHHHHHHHHHHHHHC
33.44-
190PhosphorylationHSAHCPHTPEFSVTG
CCCCCCCCCCEEECC
15.06-

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 RIP_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
103KSumoylation

16135809

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 RIP_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RFA1_HUMANRPA1physical
26186194
RFA2_HUMANRPA2physical
26186194
UBR7_HUMANUBR7physical
26186194
RFA1_HUMANRPA1physical
28514442
UBR7_HUMANUBR7physical
28514442

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RIP_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18, AND MASSSPECTROMETRY.

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