RANB9_HUMAN - dbPTM
RANB9_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RANB9_HUMAN
UniProt AC Q96S59
Protein Name Ran-binding protein 9
Gene Name RANBP9
Organism Homo sapiens (Human).
Sequence Length 729
Subcellular Localization Cytoplasm . Nucleus . Cell membrane
Peripheral membrane protein . The unphosphorylated form is predominantly cytoplasmic. A phosphorylated form is associated with the plasma membrane.
Protein Description May act as an adapter protein to couple membrane receptors to intracellular signaling pathways. May be involved in signaling of ITGB2/LFA-1 and other integrins. Enhances HGF-MET signaling by recruiting Sos and activating the Ras pathway. Enhances dihydrotestosterone-induced transactivation activity of AR, as well as dexamethasone-induced transactivation activity of NR3C1, but not affect estrogen-induced transactivation. Stabilizes TP73 isoform Alpha, probably by inhibiting its ubiquitination, and increases its proapoptotic activity. Inhibits the kinase activity of DYRK1A and DYRK1B. Inhibits FMR1 binding to RNA..
Protein Sequence MSGQPPPPPPQQQQQQQQLSPPPPAALAPVSGVVLPAPPAVSAGSSPAGSPGGGAGGEGLGAAAAALLLHPPPPPPPATAAPPPPPPPPPPPASAAAPASGPPAPPGLAAGPGPAGGAPTPALVAGSSAAAPFPHGDSALNEQEKELQRRLKRLYPAVDEQETPLPRSWSPKDKFSYIGLSQNNLRVHYKGHGKTPKDAASVRATHPIPAACGIYYFEVKIVSKGRDGYMGIGLSAQGVNMNRLPGWDKHSYGYHGDDGHSFCSSGTGQPYGPTFTTGDVIGCCVNLINNTCFYTKNGHSLGIAFTDLPPNLYPTVGLQTPGEVVDANFGQHPFVFDIEDYMREWRTKIQAQIDRFPIGDREGEWQTMIQKMVSSYLVHHGYCATAEAFARSTDQTVLEELASIKNRQRIQKLVLAGRMGEAIETTQQLYPSLLERNPNLLFTLKVRQFIEMVNGTDSEVRCLGGRSPKSQDSYPVSPRPFSSPSMSPSHGMNIHNLASGKGSTAHFSGFESCSNGVISNKAHQSYCHSNKHQSSNLNVPELNSINMSRSQQVNNFTSNDVDMETDHYSNGVGETSSNGFLNGSSKHDHEMEDCDTEMEVDSSQLRRQLCGGSQAAIERMIHFGRELQAMSEQLRRDCGKNTANKKMLKDAFSLLAYSDPWNSPVGNQLDPIQREPVCSALNSAILETHNLPKQPPLALAMGQATQCLGLMARSGIGSCAFATVEDYLH
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
64 (in isoform 2)Ubiquitination-7.8521890473
104 (in isoform 2)Ubiquitination-26.5021890473
119UbiquitinationPGPAGGAPTPALVAG
CCCCCCCCCCHHCCC		42.04-
168PhosphorylationQETPLPRSWSPKDKF
CCCCCCCCCCCCCCC		29.9328464451
170PhosphorylationTPLPRSWSPKDKFSY
CCCCCCCCCCCCCCE		24.2624719451
172UbiquitinationLPRSWSPKDKFSYIG
CCCCCCCCCCCCEEE		68.95-
174UbiquitinationRSWSPKDKFSYIGLS
CCCCCCCCCCEEEEC		42.19-
174AcetylationRSWSPKDKFSYIGLS
CCCCCCCCCCEEEEC		42.1925953088
176UbiquitinationWSPKDKFSYIGLSQN
CCCCCCCCEEEECCC		22.91-
177PhosphorylationSPKDKFSYIGLSQNN
CCCCCCCEEEECCCC		11.3528464451
181PhosphorylationKFSYIGLSQNNLRVH
CCCEEEECCCCEEEE		26.16-
183UbiquitinationSYIGLSQNNLRVHYK
CEEEECCCCEEEEEC		46.24-
189PhosphorylationQNNLRVHYKGHGKTP
CCCEEEEECCCCCCH		18.79-
197UbiquitinationKGHGKTPKDAASVRA
CCCCCCHHHCCCHHC		66.29-
216UbiquitinationPAACGIYYFEVKIVS
CCCCEEEEEEEEEEE		7.43-
304 (in isoform 2)Ubiquitination-10.25-
308 (in isoform 2)Ubiquitination-7.44-
348UbiquitinationYMREWRTKIQAQIDR
HHHHHHHHHHHHHCC		25.01-
405AcetylationLEELASIKNRQRIQK
HHHHHHHCCHHHHHH		43.5119608861
405 (in isoform 1)Ubiquitination-43.5121890473
405UbiquitinationLEELASIKNRQRIQK
HHHHHHHCCHHHHHH		43.5121906983
412UbiquitinationKNRQRIQKLVLAGRM
CCHHHHHHHHHCCCH		37.89-
412AcetylationKNRQRIQKLVLAGRM
CCHHHHHHHHHCCCH		37.8925953088
416UbiquitinationRIQKLVLAGRMGEAI
HHHHHHHCCCHHHHH		8.96-
420UbiquitinationLVLAGRMGEAIETTQ
HHHCCCHHHHHHHHH		21.59-
443PhosphorylationRNPNLLFTLKVRQFI
HCCCEEEEEEHHHHH		26.16-
445UbiquitinationPNLLFTLKVRQFIEM
CCEEEEEEHHHHHHH		32.1121890473
445 (in isoform 1)Ubiquitination-32.1121890473
445UbiquitinationPNLLFTLKVRQFIEM
CCEEEEEEHHHHHHH		32.1121890473
467PhosphorylationVRCLGGRSPKSQDSY
EEECCCCCCCCCCCC		39.7025159151
470PhosphorylationLGGRSPKSQDSYPVS
CCCCCCCCCCCCCCC		42.4723663014
473PhosphorylationRSPKSQDSYPVSPRP
CCCCCCCCCCCCCCC		24.5730266825
474PhosphorylationSPKSQDSYPVSPRPF
CCCCCCCCCCCCCCC		18.8823927012
477PhosphorylationSQDSYPVSPRPFSSP
CCCCCCCCCCCCCCC		15.6419664994
482PhosphorylationPVSPRPFSSPSMSPS
CCCCCCCCCCCCCCC		43.9823401153
483PhosphorylationVSPRPFSSPSMSPSH
CCCCCCCCCCCCCCC		22.7523401153
485PhosphorylationPRPFSSPSMSPSHGM
CCCCCCCCCCCCCCC		33.5623401153
487PhosphorylationPFSSPSMSPSHGMNI
CCCCCCCCCCCCCCH		27.8229255136
489PhosphorylationSSPSMSPSHGMNIHN
CCCCCCCCCCCCHHC		25.9329255136
499PhosphorylationMNIHNLASGKGSTAH
CCHHCCCCCCCCCCC		44.1723927012
503PhosphorylationNLASGKGSTAHFSGF
CCCCCCCCCCCCCCC		26.38-
508PhosphorylationKGSTAHFSGFESCSN
CCCCCCCCCCCCCCC		32.4828555341
531UbiquitinationQSYCHSNKHQSSNLN
HHHHCCCCCCCCCCC		46.14-
534PhosphorylationCHSNKHQSSNLNVPE
HCCCCCCCCCCCCCH		22.4027080861
535PhosphorylationHSNKHQSSNLNVPEL
CCCCCCCCCCCCCHH		38.4727080861
544PhosphorylationLNVPELNSINMSRSQ
CCCCHHHHHCCCHHH		28.1528555341
548PhosphorylationELNSINMSRSQQVNN
HHHHHCCCHHHHHCC		25.0528555341
550PhosphorylationNSINMSRSQQVNNFT
HHHCCCHHHHHCCCC		20.05-
568PhosphorylationVDMETDHYSNGVGET
CCCCCCCCCCCCCCC		13.47-
596PhosphorylationHEMEDCDTEMEVDSS
CCCCCCCCEEECCHH		43.49-
603PhosphorylationTEMEVDSSQLRRQLC
CEEECCHHHHHHHHC		28.8617525332
613PhosphorylationRRQLCGGSQAAIERM
HHHHCCCCHHHHHHH		11.26-
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
181SPhosphorylationKinaseATMQ13315
PSP
550SPhosphorylationKinaseATMQ13315
PSP
603SPhosphorylationKinaseATMQ13315
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RANB9_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 RANB9_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
UBP11_HUMANUSP11physical
12084015
ANDR_HUMANARphysical
12361945
S10A7_HUMANS100A7physical
12421467
GCR_HUMANNR3C1physical
12361945
DYR1B_HUMANDYRK1Bphysical
14500717
RAN_HUMANRANphysical
9817760
GID8_HUMANGID8physical
12559565
MPP8_HUMANMPHOSPH8physical
12559565
MKLN1_HUMANMKLN1physical
12559565
P73_HUMANTP73physical
15558019
TRAF6_HUMANTRAF6physical
21805090
L2GL1_HUMANLLGL1physical
20829363
MKLN1_HUMANMKLN1physical
17467196
MAEA_HUMANMAEAphysical
17467196
RMD5A_HUMANRMND5Aphysical
17467196
GID8_HUMANGID8physical
17467196
RANB9_HUMANRANBP9physical
17467196
PP1G_HUMANPPP1CCphysical
21382349
TGFR1_HUMANTGFBR1physical
24103590
TRAF6_HUMANTRAF6physical
24103590
TSR1_HUMANTSR1physical
22863883
UBC9_HUMANUBE2Iphysical
18455188
HDAC6_HUMANHDAC6physical
24795145
LRP1_HUMANLRP1physical
19251705
A4_HUMANAPPphysical
19251705
BACE1_HUMANBACE1physical
19251705
HEM3_HUMANHMBSphysical
12917623
RANB9_HUMANRANBP9physical
19729516
ADAP1_HUMANADAP1physical
18298663
RAN_HUMANRANphysical
11470507
THB_HUMANTHRBphysical
16595702
THA_HUMANTHRAphysical
16595702
ANDR_HUMANARphysical
16595702
ESR1_HUMANESR1physical
16595702
NTRK2_HUMANNTRK2physical
20403074
ENTP1_HUMANENTPD1physical
16478441
CD11B_HUMANCDK11Bphysical
14511641
FMR1_HUMANFMR1physical
15381419
CSN5_HUMANCOPS5physical
23926111
OPRM_HUMANOPRM1physical
19788913
RAF1_HUMANRAF1physical
23118896
EXOC2_HUMANEXOC2physical
21516116
CCND1_HUMANCCND1physical
21516116
RBP10_HUMANRANBP10physical
27173435
WDR26_HUMANWDR26physical
27173435
YPEL5_HUMANYPEL5physical
27173435
ARMC8_HUMANARMC8physical
27173435
ZMY19_HUMANZMYND19physical
27173435
RAB8A_HUMANRAB8Aphysical
27173435
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 RANB9_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-405, AND MASS SPECTROMETRY.
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-603, AND MASSSPECTROMETRY.

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