HGS_HUMAN - dbPTM
HGS_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID HGS_HUMAN
UniProt AC O14964
Protein Name Hepatocyte growth factor-regulated tyrosine kinase substrate
Gene Name HGS
Organism Homo sapiens (Human).
Sequence Length 777
Subcellular Localization Cytoplasm . Early endosome membrane
Peripheral membrane protein
Cytoplasmic side . Endosome, multivesicular body membrane
Peripheral membrane protein . Colocalizes with UBQLN1 in ubiquitin-rich cytoplasmic aggregates that are not endocytic comp
Protein Description Involved in intracellular signal transduction mediated by cytokines and growth factors. When associated with STAM, it suppresses DNA signaling upon stimulation by IL-2 and GM-CSF. Could be a direct effector of PI3-kinase in vesicular pathway via early endosomes and may regulate trafficking to early and late endosomes by recruiting clathrin. May concentrate ubiquitinated receptors within clathrin-coated regions. Involved in down-regulation of receptor tyrosine kinase via multivesicular body (MVBs) when complexed with STAM (ESCRT-0 complex). The ESCRT-0 complex binds ubiquitin and acts as sorting machinery that recognizes ubiquitinated receptors and transfers them to further sequential lysosomal sorting/trafficking processes. May contribute to the efficient recruitment of SMADs to the activin receptor complex. Involved in receptor recycling via its association with the CART complex, a multiprotein complex required for efficient transferrin receptor recycling but not for EGFR degradation..
Protein Sequence MGRGSGTFERLLDKATSQLLLETDWESILQICDLIRQGDTQAKYAVNSIKKKVNDKNPHVALYALEVMESVVKNCGQTVHDEVANKQTMEELKDLLKRQVEVNVRNKILYLIQAWAHAFRNEPKYKVVQDTYQIMKVEGHVFPEFKESDAMFAAERAPDWVDAEECHRCRVQFGVMTRKHHCRACGQIFCGKCSSKYSTIPKFGIEKEVRVCEPCYEQLNRKAEGKATSTTELPPEYLTSPLSQQSQLPPKRDETALQEEEELQLALALSQSEAEEKERLRQKSTYTSYPKAEPMPSASSAPPASSLYSSPVNSSAPLAEDIDPELARYLNRNYWEKKQEEARKSPTPSAPVPLTEPAAQPGEGHAAPTNVVENPLPETDSQPIPPSGGPFSEPQFHNGESEESHEQFLKALQNAVTTFVNRMKSNHMRGRSITNDSAVLSLFQSINGMHPQLLELLNQLDERRLYYEGLQDKLAQIRDARGALSALREEHREKLRRAAEEAERQRQIQLAQKLEIMRQKKQEYLEVQRQLAIQRLQEQEKERQMRLEQQKQTVQMRAQMPAFPLPYAQLQAMPAAGGVLYQPSGPASFPSTFSPAGSVEGSPMHGVYMSQPAPAAGPYPSMPSTAADPSMVSAYMYPAGATGAQAAPQAQAGPTASPAYSSYQPTPTAGYQNVASQAPQSLPAISQPPQSSTMGYMGSQSVSMGYQPYNMQNLMTTLPSQDASLPPQQPYIAGQQPMYQQMAPSGGPPQQQPPVAQQPQAQGPPAQGSEAQLISFD
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
17PhosphorylationRLLDKATSQLLLETD
HHHHHHHHHHHHHCC		24.5622210691
27PhosphorylationLLETDWESILQICDL
HHHCCHHHHHHHHHH		25.0922210691
40PhosphorylationDLIRQGDTQAKYAVN
HHHHCCCHHHHHHHH		36.9322210691
43UbiquitinationRQGDTQAKYAVNSIK
HCCCHHHHHHHHHHH		24.75-
50AcetylationKYAVNSIKKKVNDKN
HHHHHHHHHHHCCCC		46.4925953088
56UbiquitinationIKKKVNDKNPHVALY
HHHHHCCCCHHHHHH		68.1521906983
56 (in isoform 1)Ubiquitination-68.1521890473
56 (in isoform 2)Ubiquitination-68.1521890473
78PhosphorylationVVKNCGQTVHDEVAN
HHHHCCCHHHHHHHC		12.7020068231
86UbiquitinationVHDEVANKQTMEELK
HHHHHHCHHHHHHHH		37.0921890473
86 (in isoform 1)Ubiquitination-37.0921890473
86 (in isoform 2)Ubiquitination-37.0921890473
93UbiquitinationKQTMEELKDLLKRQV
HHHHHHHHHHHHHHC		50.0021890473
93 (in isoform 1)Ubiquitination-50.0021890473
93 (in isoform 2)Ubiquitination-50.0021890473
97UbiquitinationEELKDLLKRQVEVNV
HHHHHHHHHHCHHHH		48.3520972266
125PhosphorylationAFRNEPKYKVVQDTY
HHHCCCCCCEEECHH		21.5222817900
126UbiquitinationFRNEPKYKVVQDTYQ
HHCCCCCCEEECHHH		41.8921890473
126 (in isoform 1)Ubiquitination-41.8921890473
126 (in isoform 2)Ubiquitination-41.8921890473
131PhosphorylationKYKVVQDTYQIMKVE
CCCEEECHHHHHEEC		10.5528152594
132PhosphorylationYKVVQDTYQIMKVEG
CCEEECHHHHHEECC		12.3425159151
136UbiquitinationQDTYQIMKVEGHVFP
ECHHHHHEECCCCCC		38.4721890473
136 (in isoform 1)Ubiquitination-38.4721890473
136 (in isoform 2)Ubiquitination-38.4721890473
146UbiquitinationGHVFPEFKESDAMFA
CCCCCCCCHHHHCHH		55.4321906983
146 (in isoform 1)Ubiquitination-55.4321890473
146 (in isoform 2)Ubiquitination-55.4321890473
151SulfoxidationEFKESDAMFAAERAP
CCCHHHHCHHHHCCC		2.5621406390
176SulfoxidationCRVQFGVMTRKHHCR
CCEECCCCCCCCCCC		2.8421406390
177PhosphorylationRVQFGVMTRKHHCRA
CEECCCCCCCCCCCC		33.8728857561
192AcetylationCGQIFCGKCSSKYST
CCCEEECCCCCCCCC		31.9325953088
192UbiquitinationCGQIFCGKCSSKYST
CCCEEECCCCCCCCC		31.9321906983
192 (in isoform 1)Ubiquitination-31.9321890473
192 (in isoform 2)Ubiquitination-31.9321890473
196UbiquitinationFCGKCSSKYSTIPKF
EECCCCCCCCCCCCC		27.2521906983
196 (in isoform 1)Ubiquitination-27.2521890473
196 (in isoform 2)Ubiquitination-27.2521890473
197PhosphorylationCGKCSSKYSTIPKFG
ECCCCCCCCCCCCCC		17.0020068231
198PhosphorylationGKCSSKYSTIPKFGI
CCCCCCCCCCCCCCC		24.4820068231
199PhosphorylationKCSSKYSTIPKFGIE
CCCCCCCCCCCCCCC		37.9020068231
202UbiquitinationSKYSTIPKFGIEKEV
CCCCCCCCCCCCCEE		52.9921890473
202 (in isoform 1)Ubiquitination-52.9921890473
202 (in isoform 2)Ubiquitination-52.9921890473
207AcetylationIPKFGIEKEVRVCEP
CCCCCCCCEEEECHH		60.6419608861
207MalonylationIPKFGIEKEVRVCEP
CCCCCCCCEEEECHH		60.6426320211
207UbiquitinationIPKFGIEKEVRVCEP
CCCCCCCCEEEECHH		60.6421890473
207 (in isoform 1)Ubiquitination-60.6421890473
207 (in isoform 2)Ubiquitination-60.6421890473
216PhosphorylationVRVCEPCYEQLNRKA
EEECHHHHHHHHHHH		19.8827273156
222UbiquitinationCYEQLNRKAEGKATS
HHHHHHHHHCCCCCC		50.1121906983
222 (in isoform 1)Ubiquitination-50.1121890473
222 (in isoform 2)Ubiquitination-50.1121890473
226UbiquitinationLNRKAEGKATSTTEL
HHHHHCCCCCCCCCC		39.742266
226 (in isoform 1)Ubiquitination-39.7421890473
226 (in isoform 2)Ubiquitination-39.7421890473
228PhosphorylationRKAEGKATSTTELPP
HHHCCCCCCCCCCCH		30.0526074081
229PhosphorylationKAEGKATSTTELPPE
HHCCCCCCCCCCCHH		37.8926074081
230PhosphorylationAEGKATSTTELPPEY
HCCCCCCCCCCCHHH		21.6726074081
231PhosphorylationEGKATSTTELPPEYL
CCCCCCCCCCCHHHH		34.9826074081
237PhosphorylationTTELPPEYLTSPLSQ
CCCCCHHHHCCCHHH		22.5127259358
239PhosphorylationELPPEYLTSPLSQQS
CCCHHHHCCCHHHCC		27.6522199227
240PhosphorylationLPPEYLTSPLSQQSQ
CCHHHHCCCHHHCCC		22.6525159151
243PhosphorylationEYLTSPLSQQSQLPP
HHHCCCHHHCCCCCC		29.5622199227
246PhosphorylationTSPLSQQSQLPPKRD
CCCHHHCCCCCCCCC		26.5026074081
251UbiquitinationQQSQLPPKRDETALQ
HCCCCCCCCCCCHHH		71.2221890473
251 (in isoform 1)Ubiquitination-71.2221890473
251 (in isoform 2)Ubiquitination-71.2221890473
277UbiquitinationSQSEAEEKERLRQKS
CCHHHHHHHHHHHHH		39.3721906983
277 (in isoform 1)Ubiquitination-39.3721890473
277 (in isoform 2)Ubiquitination-39.3721890473
283UbiquitinationEKERLRQKSTYTSYP
HHHHHHHHHCCCCCC		38.03-
284PhosphorylationKERLRQKSTYTSYPK
HHHHHHHHCCCCCCC		20.5028796482
285PhosphorylationERLRQKSTYTSYPKA
HHHHHHHCCCCCCCC		37.5428796482
286PhosphorylationRLRQKSTYTSYPKAE
HHHHHHCCCCCCCCC		10.7727273156
287PhosphorylationLRQKSTYTSYPKAEP
HHHHHCCCCCCCCCC		23.1328796482
288PhosphorylationRQKSTYTSYPKAEPM
HHHHCCCCCCCCCCC		29.0825884760
289PhosphorylationQKSTYTSYPKAEPMP
HHHCCCCCCCCCCCC		10.8425159151
291UbiquitinationSTYTSYPKAEPMPSA
HCCCCCCCCCCCCCC		58.0921906983
291 (in isoform 1)Ubiquitination-58.0921890473
291 (in isoform 2)Ubiquitination-58.0921890473
295SulfoxidationSYPKAEPMPSASSAP
CCCCCCCCCCCCCCC		2.8530846556
297O-linked_GlycosylationPKAEPMPSASSAPPA
CCCCCCCCCCCCCCC		34.2328510447
297PhosphorylationPKAEPMPSASSAPPA
CCCCCCCCCCCCCCC		34.2321945579
299O-linked_GlycosylationAEPMPSASSAPPASS
CCCCCCCCCCCCCHH		31.2228510447
299PhosphorylationAEPMPSASSAPPASS
CCCCCCCCCCCCCHH		31.2221945579
300O-linked_GlycosylationEPMPSASSAPPASSL
CCCCCCCCCCCCHHH		44.5028510447
300PhosphorylationEPMPSASSAPPASSL
CCCCCCCCCCCCHHH		44.5021945579
305PhosphorylationASSAPPASSLYSSPV
CCCCCCCHHHCCCCC		27.0121945579
306PhosphorylationSSAPPASSLYSSPVN
CCCCCCHHHCCCCCC		33.1721945579
308PhosphorylationAPPASSLYSSPVNSS
CCCCHHHCCCCCCCC		14.7321945579
309PhosphorylationPPASSLYSSPVNSSA
CCCHHHCCCCCCCCC		33.2021945579
310O-linked_GlycosylationPASSLYSSPVNSSAP
CCHHHCCCCCCCCCC		21.2228510447
310PhosphorylationPASSLYSSPVNSSAP
CCHHHCCCCCCCCCC		21.2221945579
314PhosphorylationLYSSPVNSSAPLAED
HCCCCCCCCCCCHHC		28.2821945579
315O-linked_GlycosylationYSSPVNSSAPLAEDI
CCCCCCCCCCCHHCC		28.8028510447
315PhosphorylationYSSPVNSSAPLAEDI
CCCCCCCCCCCHHCC		28.8021945579
329PhosphorylationIDPELARYLNRNYWE
CCHHHHHHHHHHHHH		11.6127273156
334PhosphorylationARYLNRNYWEKKQEE
HHHHHHHHHHHHHHH		16.2327273156
337UbiquitinationLNRNYWEKKQEEARK
HHHHHHHHHHHHHHC		45.6821906983
337 (in isoform 1)Ubiquitination-45.6821890473
337 (in isoform 2)Ubiquitination-45.6821890473
345PhosphorylationKQEEARKSPTPSAPV
HHHHHHCCCCCCCCC		28.5826657352
347PhosphorylationEEARKSPTPSAPVPL
HHHHCCCCCCCCCCC		36.6526657352
349PhosphorylationARKSPTPSAPVPLTE
HHCCCCCCCCCCCCC		47.9126074081
355PhosphorylationPSAPVPLTEPAAQPG
CCCCCCCCCCCCCCC		33.5826074081
369PhosphorylationGEGHAAPTNVVENPL
CCCCCCCCCCCCCCC		35.6026074081
379PhosphorylationVENPLPETDSQPIPP
CCCCCCCCCCCCCCC		38.7226074081
387PhosphorylationDSQPIPPSGGPFSEP
CCCCCCCCCCCCCCC		51.5322468782
466PhosphorylationQLDERRLYYEGLQDK
HHHHHHHHHHHHHHH		9.5427642862
467PhosphorylationLDERRLYYEGLQDKL
HHHHHHHHHHHHHHH		14.2325147952
4732-HydroxyisobutyrylationYYEGLQDKLAQIRDA
HHHHHHHHHHHHHHH		32.53-
473UbiquitinationYYEGLQDKLAQIRDA
HHHHHHHHHHHHHHH		32.5321890473
473 (in isoform 1)Ubiquitination-32.5321890473
473 (in isoform 2)Ubiquitination-32.5321890473
485PhosphorylationRDARGALSALREEHR
HHHHHHHHHHHHHHH		25.4020860994
494AcetylationLREEHREKLRRAAEE
HHHHHHHHHHHHHHH		47.4571051
513UbiquitinationRQIQLAQKLEIMRQK
HHHHHHHHHHHHHHH		42.3421890473
513 (in isoform 1)Ubiquitination-42.3421890473
520UbiquitinationKLEIMRQKKQEYLEV
HHHHHHHHHHHHHHH		46.16-
521UbiquitinationLEIMRQKKQEYLEVQ
HHHHHHHHHHHHHHH		39.7721906983
521 (in isoform 1)Ubiquitination-39.7721890473
524PhosphorylationMRQKKQEYLEVQRQL
HHHHHHHHHHHHHHH		12.9828796482
541UbiquitinationQRLQEQEKERQMRLE
HHHHHHHHHHHHHHH		58.8721906983
541 (in isoform 1)Ubiquitination-58.8721890473
551SuccinylationQMRLEQQKQTVQMRA
HHHHHHHHHHHHHHH		47.86-
551SuccinylationQMRLEQQKQTVQMRA
HHHHHHHHHHHHHHH		47.862190698
551UbiquitinationQMRLEQQKQTVQMRA
HHHHHHHHHHHHHHH		47.86-
551 (in isoform 1)Ubiquitination-47.8621890473
553PhosphorylationRLEQQKQTVQMRAQM
HHHHHHHHHHHHHHC		21.5329083192
567PhosphorylationMPAFPLPYAQLQAMP
CCCCCCCHHHHHCCC		18.0520068231
581PhosphorylationPAAGGVLYQPSGPAS
CCCCCEEECCCCCCC		18.9020068231
584PhosphorylationGGVLYQPSGPASFPS
CCEEECCCCCCCCCC		41.7120068231
588PhosphorylationYQPSGPASFPSTFSP
ECCCCCCCCCCCCCC		40.6020068231
591PhosphorylationSGPASFPSTFSPAGS
CCCCCCCCCCCCCCC		39.8220068231
592PhosphorylationGPASFPSTFSPAGSV
CCCCCCCCCCCCCCC		28.5020068231
594PhosphorylationASFPSTFSPAGSVEG
CCCCCCCCCCCCCCC		17.5820068231
598PhosphorylationSTFSPAGSVEGSPMH
CCCCCCCCCCCCCCC		21.0720068231
602PhosphorylationPAGSVEGSPMHGVYM
CCCCCCCCCCCCEEE		12.9220068231
608PhosphorylationGSPMHGVYMSQPAPA
CCCCCCEEECCCCCC		8.8120068231
610PhosphorylationPMHGVYMSQPAPAAG
CCCCEEECCCCCCCC		18.4820068231
619PhosphorylationPAPAAGPYPSMPSTA
CCCCCCCCCCCCCCC		13.6620068231
621PhosphorylationPAAGPYPSMPSTAAD
CCCCCCCCCCCCCCC		37.1720068231
624PhosphorylationGPYPSMPSTAADPSM
CCCCCCCCCCCCHHH		23.2620068231
625PhosphorylationPYPSMPSTAADPSMV
CCCCCCCCCCCHHHH		21.7220068231
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
329YPhosphorylationKinaseEGFRP00533
PhosphoELM
-KUbiquitinationE3 ubiquitin ligaseNEDD4P46934
PMID:12230472
-KUbiquitinationE3 ubiquitin ligaseCBLP22681
PMID:20029031
-KUbiquitinationE3 ubiquitin ligaseSH3RF1Q7Z6J0
PMID:16084064
-KUbiquitinationE3 ubiquitin ligaseITCHQ96J02
PMID:22199232
-KUbiquitinationE3 ubiquitin ligaseNEDD4LQ96PU5
PMID:20675381
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of HGS_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 HGS_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
EXOC7_HUMANEXOC7physical
16189514
GKAP1_HUMANGKAP1physical
16189514
USBP1_HUMANUSHBP1physical
16189514
EHMT2_HUMANEHMT2physical
16189514
EXOC8_HUMANEXOC8physical
16189514
MI4GD_HUMANMIF4GDphysical
16189514
LDOC1_HUMANLDOC1physical
16189514
CCD33_HUMANCCDC33physical
16189514
BEGIN_HUMANBEGAINphysical
16189514
LURA1_HUMANLURAP1physical
16189514
DAZP2_HUMANDAZAP2physical
16189514
STAM2_HUMANSTAM2physical
16189514
MED7_HUMANMED7physical
16189514
UBQL1_HUMANUBQLN1physical
16189514
TS101_HUMANTSG101physical
12802020
MERL_HUMANNF2physical
11285248
EPS15_HUMANEPS15physical
10809762
STAM1_HUMANSTAMphysical
9407053
HAP1_HUMANHAP1physical
12021262
STAM1_HUMANSTAMphysical
12551915
STAM2_HUMANSTAM2physical
12551915
EPS15_HUMANEPS15physical
12551915
SNX1_HUMANSNX1physical
11110793
MERL_HUMANNF2physical
10861283
SCAM3_HUMANSCAMP3physical
19158374
A4_HUMANAPPphysical
19019082
APLP2_HUMANAPLP2physical
19019082
AT2A2_HUMANATP2A2physical
19019082
AR6P1_HUMANARL6IP1physical
19019082
BASI_HUMANBSGphysical
19019082
TIDC1_HUMANTIMMDC1physical
19019082
BRNP3_HUMANBRINP3physical
19019082
VMP1_HUMANVMP1physical
19019082
SUN2_HUMANSUN2physical
19019082
SAHH2_HUMANAHCYL1physical
19019082
CSKP_HUMANCASKphysical
19019082
ZO2_HUMANTJP2physical
19019082
HSP7C_HUMANHSPA8physical
19019082
M3K10_HUMANMAP3K10physical
19019082
STXB1_HUMANSTXBP1physical
19019082
SCRN1_HUMANSCRN1physical
19019082
DPYL1_HUMANCRMP1physical
19019082
DCTN2_HUMANDCTN2physical
19019082
GFAP_HUMANGFAPphysical
19019082
MARK4_HUMANMARK4physical
19019082
PP16A_HUMANPPP1R16Aphysical
19019082
RHBT3_HUMANRHOBTB3physical
19019082
TBB2A_HUMANTUBB2Aphysical
19019082
ERR3_HUMANESRRGphysical
19019082
ILKAP_HUMANILKAPphysical
19019082
PP1R7_HUMANPPP1R7physical
19019082
RSU1_HUMANRSU1physical
19019082
UBA1_HUMANUBA1physical
19019082
ACLY_HUMANACLYphysical
19019082
CBS_HUMANCBSphysical
19019082
DECR_HUMANDECR1physical
19019082
METK2_HUMANMAT2Aphysical
19019082
C1TM_HUMANMTHFD1Lphysical
19019082
OSBL5_HUMANOSBPL5physical
19019082
PLD3_HUMANPLD3physical
19019082
PFKAM_HUMANPFKMphysical
19019082
HNRDL_HUMANHNRNPDLphysical
19019082
RS3A_HUMANRPS3Aphysical
19019082
SF3B3_HUMANSF3B3physical
19019082
PTCD3_HUMANPTCD3physical
19019082
ZN302_HUMANZNF302physical
19019082
MEST_HUMANMESTphysical
19019082
TMCC2_HUMANTMCC2physical
19019082
AT1A1_HUMANATP1A1physical
19019082
TRAP1_HUMANTRAP1physical
19019082
GGA2_HUMANGGA2physical
19019082
TBB5_HUMANTUBBphysical
19019082
CLH1_HUMANCLTCphysical
11532964
IL2RB_HUMANIL2RBphysical
18445679
UBC_HUMANUBCphysical
16771824
VPS4A_HUMANVPS4Aphysical
14602072
ITCH_HUMANITCHphysical
14602072
SH3K1_HUMANSH3KBP1physical
21635887
TS101_HUMANTSG101physical
17229889
SCNNA_HUMANSCNN1Aphysical
20675381
TM189_HUMANTMEM189physical
20420830
CEP55_HUMANCEP55physical
17853893
TM1L1_HUMANTOM1L1physical
15611048
TS101_HUMANTSG101physical
12900395
MERL_HUMANNF2physical
12444101
STAM2_HUMANSTAM2physical
15113837
UBB_BOVINUBBphysical
16462748
EPS15_HUMANEPS15physical
18362181
INSR_HUMANINSRphysical
17445799
VEGFA_HUMANVEGFAphysical
17445799
TLR4_HUMANTLR4physical
16467847
STAM2_HUMANSTAM2physical
13679051
STAM1_HUMANSTAMphysical
13679051
BST2_HUMANBST2physical
21304933
PELP1_HUMANPELP1physical
16352611
TRAK1_HUMANTRAK1physical
18675823
VPS35_HUMANVPS35physical
19874558
SNP25_HUMANSNAP25physical
12847087
VAMP2_HUMANVAMP2physical
12847087
STX12_HUMANSTX12physical
12847087
SPY2_HUMANSPRY2physical
17320394
TS101_HUMANTSG101physical
17320394
ACTN4_HUMANACTN4physical
15772161
EPS15_HUMANEPS15physical
15772161
TRIM3_HUMANTRIM3physical
15772161
MYO5A_HUMANMYO5Aphysical
15772161
A4_HUMANAPPphysical
21832049
STAM2_HUMANSTAM2physical
22939629
STAM1_HUMANSTAMphysical
22939629
MOG1_HUMANRANGRFphysical
22939629
UBC_HUMANUBCphysical
23314748
EGFR_HUMANEGFRphysical
23153581
SH3R1_XENLAsh3rf1physical
16084064
UBC_BOVINUBCphysical
20150893
SNX5_HUMANSNX5physical
23602387
MKNK1_HUMANMKNK1physical
21988832
REPI1_HUMANREPIN1physical
22863883
MEP50_HUMANWDR77physical
22863883
UBE4B_HUMANUBE4Bphysical
24344129
STAM1_HUMANSTAMphysical
24790097
LRIG1_HUMANLRIG1physical
24828152
MET_HUMANMETphysical
24828152
LITAF_HUMANLITAFphysical
25416956
DAZP2_HUMANDAZAP2physical
25416956
JKIP2_HUMANJAKMIP2physical
25416956
ABI2_HUMANABI2physical
25416956
SPF27_HUMANBCAS2physical
25416956
NDC80_HUMANNDC80physical
25416956
POGZ_HUMANPOGZphysical
25416956
EXOC7_HUMANEXOC7physical
25416956
CSTFT_HUMANCSTF2Tphysical
25416956
LDOC1_HUMANLDOC1physical
25416956
ARFP2_HUMANARFIP2physical
25416956
SNX7_HUMANSNX7physical
25416956
NUP54_HUMANNUP54physical
25416956
VP37C_HUMANVPS37Cphysical
25416956
CT2NL_HUMANCTTNBP2NLphysical
25416956
MI4GD_HUMANMIF4GDphysical
25416956
ING5_HUMANING5physical
25416956
INT4_HUMANINTS4physical
25416956
CC114_HUMANCCDC114physical
25416956
MISSL_HUMANMAPK1IP1Lphysical
25416956
MR1L1_HUMANMRFAP1L1physical
25416956
K1C40_HUMANKRT40physical
25416956
P4HA3_HUMANP4HA3physical
25416956
CE57L_HUMANCEP57L1physical
25416956
CC103_HUMANCCDC103physical
25416956
PEF1_HUMANPEF1physical
25416956
STAM2_HUMANSTAM2physical
16429130
HNRPK_HUMANHNRNPKphysical
26344197
SC23A_HUMANSEC23Aphysical
26344197
SNX12_HUMANSNX12physical
26344197
SNX3_HUMANSNX3physical
26344197
STAM1_HUMANSTAMphysical
26344197
STAM2_HUMANSTAM2physical
26344197
CLH1_HUMANCLTCphysical
21411634
VP33B_HUMANVPS33Bphysical
21411634
NOTC1_HUMANNOTCH1physical
24662486
EPS15_HUMANEPS15physical
27008177
ERBB3_HUMANERBB3physical
28867611
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 HGS_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-207, AND MASS SPECTROMETRY.
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-240, AND MASSSPECTROMETRY.
"An extensive survey of tyrosine phosphorylation revealing new sitesin human mammary epithelial cells.";
Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A.,Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D.,Wiley H.S., Qian W.-J.;
J. Proteome Res. 8:3852-3861(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-286; TYR-289 ANDTYR-308, AND MASS SPECTROMETRY.
"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer.";
Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.;
Cell 131:1190-1203(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-132 AND TYR-216, ANDMASS SPECTROMETRY.
"Immunoaffinity profiling of tyrosine phosphorylation in cancercells.";
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,Zha X.-M., Polakiewicz R.D., Comb M.J.;
Nat. Biotechnol. 23:94-101(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-216, AND MASSSPECTROMETRY.
"Phosphoproteome analysis of HeLa cells using stable isotope labelingwith amino acids in cell culture (SILAC).";
Amanchy R., Kalume D.E., Iwahori A., Zhong J., Pandey A.;
J. Proteome Res. 4:1661-1671(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-308, AND MASSSPECTROMETRY.

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