RNBP6_HUMAN - dbPTM
RNBP6_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RNBP6_HUMAN
UniProt AC O60518
Protein Name Ran-binding protein 6
Gene Name RANBP6
Organism Homo sapiens (Human).
Sequence Length 1105
Subcellular Localization Cytoplasm. Nucleus.
Protein Description May function in nuclear protein import as nuclear transport receptor..
Protein Sequence MAATASAGVPATVSEKQEFYQLLKNLINPSCMVRRQAEEIYENIPGLCKTTFLLDAVRNRRAGYEVRQMAAALLRRLLSSGFEEVYPNLPADVQRDVKIELILAVKLETHASMRKKLCDIFAVLARNLIDEDGTNHWPEGLKFLIDSIYSKNVVLWEVALHVFWHFPGIFGTQERHDLDIIKRLLDQCIQDQEHPAIRTLSARAAAAFVLANENNIALFKDFADLLPGILQAVNDSCYQDDDSVLESLVEIADTVPKYLGPYLEDTLQLSLKLCGDSRLSNLQRQLALEVIVTLSETATPMLKKHTNIIAQAVPHILAMMVDLQDDEDWVNADEMEEDDFDSNAVAAESALDRLACGLGGKVVLPMTKEHIMQMLQSPDWKYRHAGLMALSAIGEGCHQQMESILDETVNSVLLFLQDPHPRVRAAACTTLGQMATDFAPNFQKKFHETVIAALLRTMENQGNQRVQSHAASALIIFIEDCPKSLLVLYVDSMVKNLHSVLVIKLQELIRNGTKLALEQLVTTIASVADTIEEKFVPYYDIFMPSLKHIVELAVQKELKLLRGKTIECISHIGLAVGKEKFMQDASNVMQLLLKTQSDLNNMEDDDPQTSYMVSAWARMCKILGKDFQQYLPLVIEPLIKTASAKPDVALLDTQDVENMSDDDGWQFVNLGDQQSFGIKTSGLEAKATACQMLVYYAKELREGFVEYTEQVVKLMVPLLKFYFHDNVRVAAAESMPFLLECARIRGPEYLAQMWQFICDPLIKAIGTEPDTDVLSEIMNSFAKSIEVMGDGCLNDEHLEELGGILKAKLEGHFKNQELRQVKRQEENYDQQVEMSLQDEDECDVYILTKVSDILHSLFSTYKEKILPWFEQLLPLIVNLICSSRPWPDRQWGLCIFDDIIEHCSPTSFKYVEYFRWPMLLNMRDNNPEVRQAAAYGLGVMAQFGGDDYRSLCSEAVPLLVKVIKCANSKTKKNVIATENCISAIGKILKFKPNCVNVDEVLPHWLSWLPLHEDKEEAIQTLSFLCDLIESNHPVVIGPNNSNLPKIISIIAEGKINETINYEDPCAKRLANVVRQVQTSEDLWLECVSQLDDEQQEALQELLNFA
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
2Acetylation------MAATASAGV
------CCCCCCCCC
25.4819413330
4Phosphorylation----MAATASAGVPA
----CCCCCCCCCCC
28.3620071362
6Phosphorylation--MAATASAGVPATV
--CCCCCCCCCCCCC
22.6225867546
12PhosphorylationASAGVPATVSEKQEF
CCCCCCCCCCCHHHH
20.6320071362
14PhosphorylationAGVPATVSEKQEFYQ
CCCCCCCCCHHHHHH
34.4221712546
16UbiquitinationVPATVSEKQEFYQLL
CCCCCCCHHHHHHHH
47.8521890473
112PhosphorylationVKLETHASMRKKLCD
EHHHHCHHHHHHHHH
16.12-
247PhosphorylationDDDSVLESLVEIADT
CCHHHHHHHHHHHHH
33.29-
280PhosphorylationLCGDSRLSNLQRQLA
HHCCHHHHHHHHHHH
34.09-
293PhosphorylationLALEVIVTLSETATP
HHHHHHHHHHHCCCH
17.2821406692
295PhosphorylationLEVIVTLSETATPML
HHHHHHHHHCCCHHH
24.4421406692
297PhosphorylationVIVTLSETATPMLKK
HHHHHHHCCCHHHHH
32.2421406692
299PhosphorylationVTLSETATPMLKKHT
HHHHHCCCHHHHHHH
19.3621406692
445UbiquitinationFAPNFQKKFHETVIA
CCHHHHHHHHHHHHH
40.96-
614PhosphorylationPQTSYMVSAWARMCK
HHHHHHHHHHHHHHH
11.10-
621UbiquitinationSAWARMCKILGKDFQ
HHHHHHHHHHCCCHH
31.46-
625UbiquitinationRMCKILGKDFQQYLP
HHHHHHCCCHHHHHH
52.50-
630PhosphorylationLGKDFQQYLPLVIEP
HCCCHHHHHHHHHHH
10.25-
641PhosphorylationVIEPLIKTASAKPDV
HHHHHHHHCCCCCCE
20.89-
653PhosphorylationPDVALLDTQDVENMS
CCEEEECCCCCCCCC
27.0029523821
660PhosphorylationTQDVENMSDDDGWQF
CCCCCCCCCCCCCEE
49.8529523821
707PhosphorylationLREGFVEYTEQVVKL
HHCCHHHHHHHHHHH
15.41-
708PhosphorylationREGFVEYTEQVVKLM
HCCHHHHHHHHHHHH
13.36-
720UbiquitinationKLMVPLLKFYFHDNV
HHHHHHHHHHCCCCC
45.78-
722PhosphorylationMVPLLKFYFHDNVRV
HHHHHHHHCCCCCCH
9.8326074081
734PhosphorylationVRVAAAESMPFLLEC
CCHHHHHCCCHHHHH
27.3326074081
808UbiquitinationLGGILKAKLEGHFKN
HHHHHHHHHHHHCCC
45.55-
814UbiquitinationAKLEGHFKNQELRQV
HHHHHHCCCHHHHHH
52.63-
819MethylationHFKNQELRQVKRQEE
HCCCHHHHHHHHHHH
38.19-
835PhosphorylationYDQQVEMSLQDEDEC
CHHHHHHHHCCCCCC
14.9030177828
845PhosphorylationDEDECDVYILTKVSD
CCCCCCEEEEEHHHH
4.1330177828
848PhosphorylationECDVYILTKVSDILH
CCCEEEEEHHHHHHH
21.6030177828
851PhosphorylationVYILTKVSDILHSLF
EEEEEHHHHHHHHHH
22.0829759185
856PhosphorylationKVSDILHSLFSTYKE
HHHHHHHHHHHHHHH
27.8829759185
859PhosphorylationDILHSLFSTYKEKIL
HHHHHHHHHHHHHHH
35.8029759185
961AcetylationEAVPLLVKVIKCANS
HHHHHHHHHHHHCCC
37.9125953088
986UbiquitinationNCISAIGKILKFKPN
HHHHHHHHHHCCCCC
38.46-
1048PhosphorylationSNLPKIISIIAEGKI
CCHHHHHHHHHCCCC
16.0620068231
1058PhosphorylationAEGKINETINYEDPC
HCCCCCCCCCCCCHH
15.2720068231
1061PhosphorylationKINETINYEDPCAKR
CCCCCCCCCCHHHHH
20.1929514088
1067UbiquitinationNYEDPCAKRLANVVR
CCCCHHHHHHHHHHH
55.45-

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 RNBP6_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RNBP6_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 RNBP6_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SYK_HUMANKARSphysical
22863883
KCD12_HUMANKCTD12physical
22863883
PEX5_HUMANPEX5physical
22863883
CLH1_HUMANCLTCphysical
26344197
COPB_HUMANCOPB1physical
26344197
MCM7_HUMANMCM7physical
26344197
ATP9A_HUMANATP9Aphysical
28514442
ARMX3_HUMANARMCX3physical
28514442
STEA3_HUMANSTEAP3physical
28514442
AT2B3_HUMANATP2B3physical
28514442
S27A2_HUMANSLC27A2physical
28514442
CC033_HUMANC3orf33physical
28514442
EXOG_HUMANEXOGphysical
28514442
TYW1B_HUMANTYW1Bphysical
28514442
SMIM8_HUMANSMIM8physical
28514442
MUL1_HUMANMUL1physical
28514442
PMGT1_HUMANPOMGNT1physical
28514442
ZFPL1_HUMANZFPL1physical
28514442
LNP_HUMANKIAA1715physical
28514442
MICU2_HUMANMICU2physical
28514442
PM34_HUMANSLC25A17physical
28514442
TV23C_HUMANTVP23Cphysical
28514442
PGES2_HUMANPTGES2physical
28514442
MA1B1_HUMANMAN1B1physical
28514442
TIM14_HUMANDNAJC19physical
28514442
DAAM1_HUMANDAAM1physical
28514442
TIM16_HUMANPAM16physical
28514442
TM186_HUMANTMEM186physical
28514442
NOG2_HUMANGNL2physical
28514442
DHR13_HUMANDHRS13physical
28514442
MCL1_HUMANMCL1physical
28514442
MICU1_HUMANMICU1physical
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 RNBP6_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.

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