GRAP1_HUMAN - dbPTM
GRAP1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID GRAP1_HUMAN
UniProt AC Q4V328
Protein Name GRIP1-associated protein 1
Gene Name GRIPAP1
Organism Homo sapiens (Human).
Sequence Length 841
Subcellular Localization Early endosome membrane
Peripheral membrane protein . Recycling endosome membrane
Peripheral membrane protein . Cell projection, axon . Cell projection, dendrite . Cell junction, synapse . Localizes to recycling endosomal tubules that are emanati
Protein Description Regulates the endosomal recycling back to the neuronal plasma membrane, possibly by connecting early and late recycling endosomal domains and promoting segregation of recycling endosomes from early endosomal membranes. Involved in the localization of recycling endosomes to dendritic spines, thereby playing a role in the maintenance of dendritic spine morphology. Required for the activity-induced AMPA receptor recycling to dendrite membranes and for long-term potentiation and synaptic plasticity (By similarity).; GRASP-1 C-terminal chain: Functions as a scaffold protein to facilitate MAP3K1/MEKK1-mediated activation of the JNK1 kinase by phosphorylation, possibly by bringing MAP3K1/MEKK1 and JNK1 in close proximity..
Protein Sequence MAQALSEEEFQRMQAQLLELRTNNYQLSDELRKNGVELTSLRQKVAYLDKEFSKAQKALSKSKKAQEVEVLLSENEMLQAKLHSQEEDFRLQNSTLMAEFSKLCSQMEQLEQENQQLKEGAAGAGVAQAGPLVDGELLRLQAENTALQKNVAALQERYGKEAGKFSAVSEGQGDPPGGPAPTVLAPMPLAEVELKWEMEKEEKRLLWEQLQGLESSKQAETSRLQEELAKLSEKLKKKQESFCRLQTEKETLFNDSRNKIEELQQRKEADHKAQLARTQKLQQELEAANQSLAELRDQRQGERLEHAAALRALQDQVSIQSADAQEQVEGLLAENNALRTSLAALEQIQTAKTQELNMLREQTTGLAAELQQQQAEYEDLMGQKDDLNSQLQESLRANSRLLEQLQEIGQEKEQLTQELQEARKSAEKRKAMLDELAMETLQEKSQHKEELGAVRLRHEKEVLGVRARYERELRELHEDKKRQEEELRGQIREEKARTRELETLQQTVEELQAQVHSMDGAKGWFERRLKEAEESLQQQQQEQEEALKQCREQHAAELKGKEEELQDVRDQLEQAQEERDCHLKTISSLKQEVKDTVDGQRILEKKGSAALKDLKRQLHLERKRADKLQERLQDILTNSKSRSGLEELVLSEMNSPSRTQTGDSSSISSFSYREILREKESSAVPARSLSSSPQAQPPRPAELSDEEVAELFQRLAETQQEKWMLEEKVKHLEVSSASMAEDLCRKSAIIETYVMDSRIDVSVAAGHTDRSGLGSVLRDLVKPGDENLREMNKKLQNMLEEQLTKNMHLHKDMEVLSQEIVRLSKECVGPPDPDLEPGETS
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------MAQALSEEE
------CCCCCCHHH		11.8922223895
13SulfoxidationSEEEFQRMQAQLLEL
CHHHHHHHHHHHHHH		2.4221406390
33UbiquitinationQLSDELRKNGVELTS
CCCHHHHHCCCCHHH		71.3429967540
50AcetylationQKVAYLDKEFSKAQK
HHHHHHHHHHHHHHH		59.0525953088
73PhosphorylationQEVEVLLSENEMLQA
HHHHHHHCHHHHHHH		33.93-
73UbiquitinationQEVEVLLSENEMLQA
HHHHHHHCHHHHHHH		33.9321890473
81UbiquitinationENEMLQAKLHSQEED
HHHHHHHHHHCCHHH		33.5032015554
139 (in isoform 3)Ubiquitination-37.0621890473
145PhosphorylationLRLQAENTALQKNVA
HHHHHHHHHHHHHHH		21.9120068231
149UbiquitinationAENTALQKNVAALQE
HHHHHHHHHHHHHHH		54.9929967540
149 (in isoform 1)Ubiquitination-54.9921890473
149 (in isoform 3)Ubiquitination-54.9921890473
149 (in isoform 4)Ubiquitination-54.9921890473
169PhosphorylationAGKFSAVSEGQGDPP
CCCCCCCCCCCCCCC		35.4120068231
173UbiquitinationSAVSEGQGDPPGGPA
CCCCCCCCCCCCCCC		61.3221890473
182PhosphorylationPPGGPAPTVLAPMPL
CCCCCCCCEEECCCH		30.2020068231
183UbiquitinationPGGPAPTVLAPMPLA
CCCCCCCEEECCCHH		4.1121890473
194 (in isoform 2)Phosphorylation-10.63-
196UbiquitinationLAEVELKWEMEKEEK
HHHCHHHHCCHHHHH		23.8524816145
196 (in isoform 2)Ubiquitination-23.8521890473
198 (in isoform 2)Phosphorylation-9.66-
206 (in isoform 2)Ubiquitination-5.7021890473
217UbiquitinationLQGLESSKQAETSRL
HHHHHHHHHHHHHHH		63.9132015554
222PhosphorylationSSKQAETSRLQEELA
HHHHHHHHHHHHHHH		23.6216674116
230UbiquitinationRLQEELAKLSEKLKK
HHHHHHHHHHHHHHH		66.2332015554
232PhosphorylationQEELAKLSEKLKKKQ
HHHHHHHHHHHHHHH		31.7928348404
241PhosphorylationKLKKKQESFCRLQTE
HHHHHHHHHHHHHHH		27.4425159151
247PhosphorylationESFCRLQTEKETLFN
HHHHHHHHHHHHHHC		54.3320068231
249UbiquitinationFCRLQTEKETLFNDS
HHHHHHHHHHHHCCH		60.4329967540
249 (in isoform 1)Ubiquitination-60.4321890473
249 (in isoform 4)Ubiquitination-60.4321890473
251PhosphorylationRLQTEKETLFNDSRN
HHHHHHHHHHCCHHH		47.9520068231
256PhosphorylationKETLFNDSRNKIEEL
HHHHHCCHHHHHHHH		38.5721815630
259UbiquitinationLFNDSRNKIEELQQR
HHCCHHHHHHHHHHH		50.8429967540
259 (in isoform 1)Ubiquitination-50.8421890473
259 (in isoform 4)Ubiquitination-50.8421890473
272UbiquitinationQRKEADHKAQLARTQ
HHHHHHHHHHHHHHH		38.0724816145
280UbiquitinationAQLARTQKLQQELEA
HHHHHHHHHHHHHHH		47.8829967540
291PhosphorylationELEAANQSLAELRDQ
HHHHHHHHHHHHHHH		29.3828555341
296MethylationNQSLAELRDQRQGER
HHHHHHHHHHHHHHH		29.53-
318PhosphorylationRALQDQVSIQSADAQ
HHHHHHHCCCCCCHH		14.8528857561
321PhosphorylationQDQVSIQSADAQEQV
HHHHCCCCCCHHHHH		26.8428348404
358SulfoxidationAKTQELNMLREQTTG
HHHHHHHHHHHHHHH		6.1221406390
363PhosphorylationLNMLREQTTGLAAEL
HHHHHHHHHHHHHHH		20.3424043423
364PhosphorylationNMLREQTTGLAAELQ
HHHHHHHHHHHHHHH		29.8724043423
377PhosphorylationLQQQQAEYEDLMGQK
HHHHHHHHHHHHCCH		20.1224043423
412UbiquitinationLQEIGQEKEQLTQEL
HHHHHHHHHHHHHHH		42.7632015554
432SulfoxidationSAEKRKAMLDELAME
HHHHHHHHHHHHHHH		5.6321406390
440PhosphorylationLDELAMETLQEKSQH
HHHHHHHHHHHHHHC		22.21-
444UbiquitinationAMETLQEKSQHKEEL
HHHHHHHHHHCHHHH		42.3232015554
454UbiquitinationHKEELGAVRLRHEKE
CHHHHCHHHHHHHHH		5.8624816145
460UbiquitinationAVRLRHEKEVLGVRA
HHHHHHHHHHHHHHH		47.1729967540
464UbiquitinationRHEKEVLGVRARYER
HHHHHHHHHHHHHHH		16.4324816145
525UbiquitinationMDGAKGWFERRLKEA
CCCCHHHHHHHHHHH		7.7424816145
530UbiquitinationGWFERRLKEAEESLQ
HHHHHHHHHHHHHHH		53.7324816145
530 (in isoform 3)Ubiquitination-53.7321890473
538UbiquitinationEAEESLQQQQQEQEE
HHHHHHHHHHHHHHH		48.6324816145
540UbiquitinationEESLQQQQQEQEEAL
HHHHHHHHHHHHHHH		44.4324816145
548UbiquitinationQEQEEALKQCREQHA
HHHHHHHHHHHHHHH		55.1732015554
551UbiquitinationEEALKQCREQHAAEL
HHHHHHHHHHHHHHH		44.0824816145
558 (in isoform 2)Phosphorylation-8.32-
561UbiquitinationHAAELKGKEEELQDV
HHHHHCCCHHHHHHH		61.4424816145
561 (in isoform 2)Ubiquitination-61.4421890473
564UbiquitinationELKGKEEELQDVRDQ
HHCCCHHHHHHHHHH		53.4724816145
574UbiquitinationDVRDQLEQAQEERDC
HHHHHHHHHHHHHHH		57.8724816145
576 (in isoform 2)Phosphorylation-53.42-
577UbiquitinationDQLEQAQEERDCHLK
HHHHHHHHHHHHHHH		59.0024816145
584AcetylationEERDCHLKTISSLKQ
HHHHHHHHHHHHHHH		21.8325953088
584UbiquitinationEERDCHLKTISSLKQ
HHHHHHHHHHHHHHH		21.8332015554
585 (in isoform 2)Phosphorylation-32.24-
586 (in isoform 2)Phosphorylation-2.23-
587PhosphorylationDCHLKTISSLKQEVK
HHHHHHHHHHHHHHH		34.5523403867
587 (in isoform 2)Phosphorylation-34.55-
588PhosphorylationCHLKTISSLKQEVKD
HHHHHHHHHHHHHHH		35.4224719451
589 (in isoform 2)Phosphorylation-5.46-
590 (in isoform 2)Phosphorylation-46.49-
593 (in isoform 2)Phosphorylation-6.69-
596PhosphorylationLKQEVKDTVDGQRIL
HHHHHHHCCCHHHHH		18.12-
601UbiquitinationKDTVDGQRILEKKGS
HHCCCHHHHHHHHCC		40.7724816145
603UbiquitinationTVDGQRILEKKGSAA
CCCHHHHHHHHCCHH		9.5824816145
606AcetylationGQRILEKKGSAALKD
HHHHHHHHCCHHHHH		49.0425953088
609 (in isoform 4)Ubiquitination-26.0221890473
611UbiquitinationEKKGSAALKDLKRQL
HHHCCHHHHHHHHHH		4.4224816145
612AcetylationKKGSAALKDLKRQLH
HHCCHHHHHHHHHHH		57.1825953088
613UbiquitinationKGSAALKDLKRQLHL
HCCHHHHHHHHHHHH		59.2724816145
614UbiquitinationGSAALKDLKRQLHLE
CCHHHHHHHHHHHHH		4.7524816145
624UbiquitinationQLHLERKRADKLQER
HHHHHHHHHHHHHHH		54.9924816145
627UbiquitinationLERKRADKLQERLQD
HHHHHHHHHHHHHHH		51.6024816145
637PhosphorylationERLQDILTNSKSRSG
HHHHHHHHCCCCCCC		37.4720068231
637UbiquitinationERLQDILTNSKSRSG
HHHHHHHHCCCCCCC		37.4724816145
639PhosphorylationLQDILTNSKSRSGLE
HHHHHHCCCCCCCHH		27.1124719451
640UbiquitinationQDILTNSKSRSGLEE
HHHHHCCCCCCCHHH		52.5421906983
640 (in isoform 1)Ubiquitination-52.5421890473
641PhosphorylationDILTNSKSRSGLEEL
HHHHCCCCCCCHHHH		31.3430576142
643PhosphorylationLTNSKSRSGLEELVL
HHCCCCCCCHHHHHH		55.6221712546
650UbiquitinationSGLEELVLSEMNSPS
CCHHHHHHHCCCCCC		5.8424816145
651PhosphorylationGLEELVLSEMNSPSR
CHHHHHHHCCCCCCC		27.5922167270
653UbiquitinationEELVLSEMNSPSRTQ
HHHHHHCCCCCCCCC		5.5924816145
655PhosphorylationLVLSEMNSPSRTQTG
HHHHCCCCCCCCCCC		23.9622167270
657PhosphorylationLSEMNSPSRTQTGDS
HHCCCCCCCCCCCCC		48.0222167270
659O-linked_GlycosylationEMNSPSRTQTGDSSS
CCCCCCCCCCCCCCC		34.5230379171
659PhosphorylationEMNSPSRTQTGDSSS
CCCCCCCCCCCCCCC		34.5223403867
661PhosphorylationNSPSRTQTGDSSSIS
CCCCCCCCCCCCCCC		42.2027251789
663UbiquitinationPSRTQTGDSSSISSF
CCCCCCCCCCCCCCC		49.0524816145
664PhosphorylationSRTQTGDSSSISSFS
CCCCCCCCCCCCCCC		27.5922167270
665PhosphorylationRTQTGDSSSISSFSY
CCCCCCCCCCCCCCH		36.1122167270
666PhosphorylationTQTGDSSSISSFSYR
CCCCCCCCCCCCCHH		30.3723401153
668PhosphorylationTGDSSSISSFSYREI
CCCCCCCCCCCHHHH		27.5522167270
669PhosphorylationGDSSSISSFSYREIL
CCCCCCCCCCHHHHH		19.2822167270
671PhosphorylationSSSISSFSYREILRE
CCCCCCCCHHHHHHH		25.8128122231
672PhosphorylationSSISSFSYREILREK
CCCCCCCHHHHHHHH		15.3929978859
679UbiquitinationYREILREKESSAVPA
HHHHHHHHHHCCCCC		57.3624816145
680UbiquitinationREILREKESSAVPAR
HHHHHHHHHCCCCCC		45.2124816145
681PhosphorylationEILREKESSAVPARS
HHHHHHHHCCCCCCC		34.3626657352
682PhosphorylationILREKESSAVPARSL
HHHHHHHCCCCCCCC		34.0826074081
688PhosphorylationSSAVPARSLSSSPQA
HCCCCCCCCCCCCCC		34.4128176443
689UbiquitinationSAVPARSLSSSPQAQ
CCCCCCCCCCCCCCC		4.8524816145
690PhosphorylationAVPARSLSSSPQAQP
CCCCCCCCCCCCCCC		29.9829255136
691PhosphorylationVPARSLSSSPQAQPP
CCCCCCCCCCCCCCC		51.8629255136
692PhosphorylationPARSLSSSPQAQPPR
CCCCCCCCCCCCCCC		20.0429255136
704PhosphorylationPPRPAELSDEEVAEL
CCCCCCCCHHHHHHH		34.1930266825
706UbiquitinationRPAELSDEEVAELFQ
CCCCCCHHHHHHHHH		51.5024816145
716UbiquitinationAELFQRLAETQQEKW
HHHHHHHHHHHHHHH		21.7124816145
722UbiquitinationLAETQQEKWMLEEKV
HHHHHHHHHHHHHHH		33.3032015554
728UbiquitinationEKWMLEEKVKHLEVS
HHHHHHHHHHHHCCC		47.4032015554
730UbiquitinationWMLEEKVKHLEVSSA
HHHHHHHHHHCCCCH		54.2429967540
735PhosphorylationKVKHLEVSSASMAED
HHHHHCCCCHHHHHH		15.7128387310
736PhosphorylationVKHLEVSSASMAEDL
HHHHCCCCHHHHHHH		29.5528450419
738PhosphorylationHLEVSSASMAEDLCR
HHCCCCHHHHHHHHH		22.0728387310
746UbiquitinationMAEDLCRKSAIIETY
HHHHHHHCCHHHHHH		43.1529967540
747PhosphorylationAEDLCRKSAIIETYV
HHHHHHCCHHHHHHH		12.8327499020
753PhosphorylationKSAIIETYVMDSRID
CCHHHHHHHCCCCCC		4.8727642862
756UbiquitinationIIETYVMDSRIDVSV
HHHHHHCCCCCCEEH		25.3924816145
762PhosphorylationMDSRIDVSVAAGHTD
CCCCCCEEHHCCCCC		11.4228555341
766UbiquitinationIDVSVAAGHTDRSGL
CCEEHHCCCCCCCCH		17.9424816145
771PhosphorylationAAGHTDRSGLGSVLR
HCCCCCCCCHHHHHH		40.9728555341
775PhosphorylationTDRSGLGSVLRDLVK
CCCCCHHHHHHHHCC		24.0323312004
782UbiquitinationSVLRDLVKPGDENLR
HHHHHHCCCCCHHHH		51.0524816145
792UbiquitinationDENLREMNKKLQNML
CHHHHHHHHHHHHHH		33.2924816145
794UbiquitinationNLREMNKKLQNMLEE
HHHHHHHHHHHHHHH		50.7530230243
798SulfoxidationMNKKLQNMLEEQLTK
HHHHHHHHHHHHHHH		3.0030846556
805UbiquitinationMLEEQLTKNMHLHKD
HHHHHHHHHCHHHHC		61.9529967540
811AcetylationTKNMHLHKDMEVLSQ
HHHCHHHHCHHHHHH		66.197491951
811UbiquitinationTKNMHLHKDMEVLSQ
HHHCHHHHCHHHHHH		66.1932015554
813SulfoxidationNMHLHKDMEVLSQEI
HCHHHHCHHHHHHHH		4.5921406390
817PhosphorylationHKDMEVLSQEIVRLS
HHCHHHHHHHHHHHH		30.8324173317
825UbiquitinationQEIVRLSKECVGPPD
HHHHHHHHHHCCCCC		60.7829967540
840PhosphorylationPDLEPGETS------
CCCCCCCCC------		45.7327732954
841PhosphorylationDLEPGETS-------
CCCCCCCC-------		33.6427732954
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 GRAP1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of GRAP1_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 GRAP1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CCNT1_HUMANCCNT1physical
11704662
RAB4A_HUMANRAB4Aphysical
21988832
HERC1_HUMANHERC1physical
22863883
MYL6_HUMANMYL6physical
22863883
PKN3_HUMANPKN3physical
27173435
NCK5L_HUMANNCKAP5Lphysical
27173435
TFPT_HUMANTFPTphysical
27173435
YETS4_HUMANYEATS4physical
27173435
GOGA5_HUMANGOLGA5physical
27173435
CLOCK_HUMANCLOCKphysical
27173435
PSMD9_HUMANPSMD9physical
27173435
VPS50_HUMANCCDC132physical
27173435
CAVN1_HUMANPTRFphysical
27173435
HAUS6_HUMANHAUS6physical
27173435
RPR1A_HUMANRPRD1Aphysical
27173435
BMAL1_HUMANARNTLphysical
27173435
RABX5_HUMANRABGEF1physical
27173435
NUF2_HUMANNUF2physical
27173435
EIPR1_HUMANTSSC1physical
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 GRAP1_HUMAN

loading...

Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-666; SER-690 ANDSER-692, AND MASS SPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-655, AND MASSSPECTROMETRY.
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis.";
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III;
J. Proteome Res. 7:1346-1351(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-655, AND MASSSPECTROMETRY.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory