dbPTM

HS105_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	HS105_HUMAN
UniProt AC	Q92598
Protein Name	Heat shock protein 105 kDa
Gene Name	HSPH1
Organism	Homo sapiens (Human).
Sequence Length	858
Subcellular Localization	Cytoplasm .
Protein Description	Acts as a nucleotide-exchange factor (NEF) for chaperone proteins HSPA1A and HSPA1B, promoting the release of ADP from HSPA1A/B thereby triggering client/substrate protein release. [PubMed: 24318877 Prevents the aggregation of denatured proteins in cells under severe stress, on which the ATP levels decrease markedly. Inhibits HSPA8/HSC70 ATPase and chaperone activities (By similarity]
Protein Sequence	MSVVGLDVGSQSCYIAVARAGGIETIANEFSDRCTPSVISFGSKNRTIGVAAKNQQITHANNTVSNFKRFHGRAFNDPFIQKEKENLSYDLVPLKNGGVGIKVMYMGEEHLFSVEQITAMLLTKLKETAENSLKKPVTDCVISVPSFFTDAERRSVLDAAQIVGLNCLRLMNDMTAVALNYGIYKQDLPSLDEKPRIVVFVDMGHSAFQVSACAFNKGKLKVLGTAFDPFLGGKNFDEKLVEHFCAEFKTKYKLDAKSKIRALLRLYQECEKLKKLMSSNSTDLPLNIECFMNDKDVSGKMNRSQFEELCAELLQKIEVPLYSLLEQTHLKVEDVSAVEIVGGATRIPAVKERIAKFFGKDISTTLNADEAVARGCALQCAILSPAFKVREFSVTDAVPFPISLIWNHDSEDTEGVHEVFSRNHAAPFSKVLTFLRRGPFELEAFYSDPQGVPYPEAKIGRFVVQNVSAQKDGEKSRVKVKVRVNTHGIFTISTASMVEKVPTEENEMSSEADMECLNQRPPENPDTDKNVQQDNSEAGTQPQVQTDAQQTSQSPPSPELTSEENKIPDADKANEKKVDQPPEAKKPKIKVVNVELPIEANLVWQLGKDLLNMYIETEGKMIMQDKLEKERNDAKNAVEEYVYEFRDKLCGPYEKFICEQDHQNFLRLLTETEDWLYEEGEDQAKQAYVDKLEELMKIGTPVKVRFQEAEERPKMFEELGQRLQHYAKIAADFRNKDEKYNHIDESEMKKVEKSVNEVMEWMNNVMNAQAKKSLDQDPVVRAQEIKTKIKELNNTCEPVVTQPKPKIESPKLERTPNGPNIDKKEEDLEDKNNFGAEPPHQNGECYPNEKNSVNMDLD

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MSVVGLDVG ------CCEEEEECC	26.05	22223895
2	Phosphorylation	------MSVVGLDVG ------CCEEEEECC	26.05	24043423
10	Phosphorylation	VVGLDVGSQSCYIAV EEEEECCCCEEEEEH	20.83	22817900
12	Phosphorylation	GLDVGSQSCYIAVAR EEECCCCEEEEEHHH	15.58	22817900
14	Phosphorylation	DVGSQSCYIAVARAG ECCCCEEEEEHHHCC	9.36	22817900
25	Phosphorylation	ARAGGIETIANEFSD HHCCCHHHHHHHCCC	24.38	-
31	Phosphorylation	ETIANEFSDRCTPSV HHHHHHCCCCCCCCE	20.26	22817900
33	Methylation	IANEFSDRCTPSVIS HHHHCCCCCCCCEEE	25.63	115479691
34	S-palmitoylation	ANEFSDRCTPSVISF HHHCCCCCCCCEEEE	8.67	26865113
37	Phosphorylation	FSDRCTPSVISFGSK CCCCCCCCEEEECCC	17.58	28450419
40	Phosphorylation	RCTPSVISFGSKNRT CCCCCEEEECCCCCE	22.77	28450419
43	Phosphorylation	PSVISFGSKNRTIGV CCEEEECCCCCEEEE	25.42	28450419
44	Ubiquitination	SVISFGSKNRTIGVA CEEEECCCCCEEEEE	51.32	-
53	2-Hydroxyisobutyrylation	RTIGVAAKNQQITHA CEEEEEEECCEEECC	45.62	-
53	Ubiquitination	RTIGVAAKNQQITHA CEEEEEEECCEEECC	45.62	21890473
53 (in isoform 2)	Ubiquitination	-	45.62	22053931
53 (in isoform 3)	Ubiquitination	-	45.62	21906983
55 (in isoform 1)	Ubiquitination	-	35.03	21906983
68	2-Hydroxyisobutyrylation	NNTVSNFKRFHGRAF CCCCCHHHHHCCCCC	59.41	-
68	Acetylation	NNTVSNFKRFHGRAF CCCCCHHHHHCCCCC	59.41	25953088
68	Methylation	NNTVSNFKRFHGRAF CCCCCHHHHHCCCCC	59.41	129939
68	Ubiquitination	NNTVSNFKRFHGRAF CCCCCHHHHHCCCCC	59.41	21906983
68 (in isoform 2)	Ubiquitination	-	59.41	22053931
68 (in isoform 3)	Ubiquitination	-	59.41	21906983
70	Ubiquitination	TVSNFKRFHGRAFND CCCHHHHHCCCCCCC	8.05	-
70 (in isoform 1)	Ubiquitination	-	8.05	21906983
82	Acetylation	FNDPFIQKEKENLSY CCCHHHHHHHCCCCC	66.97	27452117
82	Ubiquitination	FNDPFIQKEKENLSY CCCHHHHHHHCCCCC	66.97	-
82 (in isoform 2)	Ubiquitination	-	66.97	-
84	Ubiquitination	DPFIQKEKENLSYDL CHHHHHHHCCCCCCE	59.96	-
84	2-Hydroxyisobutyrylation	DPFIQKEKENLSYDL CHHHHHHHCCCCCCE	59.96	-
84	Acetylation	DPFIQKEKENLSYDL CHHHHHHHCCCCCCE	59.96	25953088
84	Ubiquitination	DPFIQKEKENLSYDL CHHHHHHHCCCCCCE	59.96	-
86	Ubiquitination	FIQKEKENLSYDLVP HHHHHHCCCCCCEEE	45.41	-
89	Phosphorylation	KEKENLSYDLVPLKN HHHCCCCCCEEECCC	19.23	22817900
95	Acetylation	SYDLVPLKNGGVGIK CCCEEECCCCCEEEE	47.69	25953088
95	Ubiquitination	SYDLVPLKNGGVGIK CCCEEECCCCCEEEE	47.69	21906983
95 (in isoform 2)	Ubiquitination	-	47.69	22053931
95 (in isoform 3)	Ubiquitination	-	47.69	21906983
97 (in isoform 1)	Ubiquitination	-	30.49	21906983
102	Ubiquitination	KNGGVGIKVMYMGEE CCCCEEEEEEECCCC	18.28	-
104	Ubiquitination	GGVGIKVMYMGEEHL CCEEEEEEECCCCCC	1.29	-
105	Phosphorylation	GVGIKVMYMGEEHLF CEEEEEEECCCCCCC	12.64	20860994
126	Ubiquitination	AMLLTKLKETAENSL HHHHHHHHHHHHHHC	55.35	-
132	Phosphorylation	LKETAENSLKKPVTD HHHHHHHHCCCCCCC	32.83	-
138	Phosphorylation	NSLKKPVTDCVISVP HHCCCCCCCEEEECC	32.01	-
149	Phosphorylation	ISVPSFFTDAERRSV EECCCCCCHHHHHHH	32.08	27251275
167	Glutathionylation	AQIVGLNCLRLMNDM HHHHCHHHHHHHCHH	2.55	22555962
180 (in isoform 3)	Ubiquitination	-	24.21	21906983
185	Ubiquitination	ALNYGIYKQDLPSLD HHHCCHHHCCCCCCC	35.10	-
187	Ubiquitination	NYGIYKQDLPSLDEK HCCHHHCCCCCCCCC	57.29	-
193 (in isoform 3)	Ubiquitination	-	70.97	21906983
194	Acetylation	DLPSLDEKPRIVVFV CCCCCCCCCCEEEEE	38.98	23749302
194	Ubiquitination	DLPSLDEKPRIVVFV CCCCCCCCCCEEEEE	38.98	22053931
194 (in isoform 2)	Ubiquitination	-	38.98	22053931
196	Acetylation	PSLDEKPRIVVFVDM CCCCCCCCEEEEEEC	45.46	-
196	Ubiquitination	PSLDEKPRIVVFVDM CCCCCCCCEEEEEEC	45.46	-
221	Ubiquitination	AFNKGKLKVLGTAFD CCCCCCEEEEEEECC	38.61	21906983
221 (in isoform 2)	Ubiquitination	-	38.61	22053931
223	Ubiquitination	NKGKLKVLGTAFDPF CCCCEEEEEEECCHH	4.89	-
223 (in isoform 1)	Ubiquitination	-	4.89	21906983
225	Phosphorylation	GKLKVLGTAFDPFLG CCEEEEEEECCHHCC	21.71	21601212
234	2-Hydroxyisobutyrylation	FDPFLGGKNFDEKLV CCHHCCCCCCCHHHH	53.28	-
234	Acetylation	FDPFLGGKNFDEKLV CCHHCCCCCCCHHHH	53.28	132957
234	Ubiquitination	FDPFLGGKNFDEKLV CCHHCCCCCCCHHHH	53.28	21906983
234 (in isoform 2)	Ubiquitination	-	53.28	22053931
236	Ubiquitination	PFLGGKNFDEKLVEH HHCCCCCCCHHHHHH	17.07	-
236 (in isoform 1)	Ubiquitination	-	17.07	21906983
239	Ubiquitination	GGKNFDEKLVEHFCA CCCCCCHHHHHHHHH	60.73	-
249	Acetylation	EHFCAEFKTKYKLDA HHHHHHHCHHCCCCH	35.30	25953088
249	Ubiquitination	EHFCAEFKTKYKLDA HHHHHHHCHHCCCCH	35.30	-
257	Acetylation	TKYKLDAKSKIRALL HHCCCCHHHHHHHHH	52.53	25953088
265	Methylation	SKIRALLRLYQECEK HHHHHHHHHHHHHHH	32.00	-
272	Acetylation	RLYQECEKLKKLMSS HHHHHHHHHHHHHHC	76.81	23749302
272	Ubiquitination	RLYQECEKLKKLMSS HHHHHHHHHHHHHHC	76.81	19608861
274	Acetylation	YQECEKLKKLMSSNS HHHHHHHHHHHHCCC	55.73	7987869
274	Ubiquitination	YQECEKLKKLMSSNS HHHHHHHHHHHHCCC	55.73	-
275	Ubiquitination	QECEKLKKLMSSNST HHHHHHHHHHHCCCC	60.91	-
278	Phosphorylation	EKLKKLMSSNSTDLP HHHHHHHHCCCCCCC	36.48	30624053
279	Phosphorylation	KLKKLMSSNSTDLPL HHHHHHHCCCCCCCC	22.34	30624053
281	Phosphorylation	KKLMSSNSTDLPLNI HHHHHCCCCCCCCEE	25.83	30624053
290	Glutathionylation	DLPLNIECFMNDKDV CCCCEEEEECCCCCC	3.29	22555962
295	Acetylation	IECFMNDKDVSGKMN EEEECCCCCCCCCCC	55.83	25953088
295	Ubiquitination	IECFMNDKDVSGKMN EEEECCCCCCCCCCC	55.83	-
298	O-linked_Glycosylation	FMNDKDVSGKMNRSQ ECCCCCCCCCCCHHH	42.71	23301498
300	Ubiquitination	NDKDVSGKMNRSQFE CCCCCCCCCCHHHHH	26.04	-
304	O-linked_Glycosylation	VSGKMNRSQFEELCA CCCCCCHHHHHHHHH	33.93	23301498
304	Phosphorylation	VSGKMNRSQFEELCA CCCCCCHHHHHHHHH	33.93	21712546
310	Glutathionylation	RSQFEELCAELLQKI HHHHHHHHHHHHHHC	2.90	22555962
322	Phosphorylation	QKIEVPLYSLLEQTH HHCCCCHHHHHHHCC	7.39	-
345	Phosphorylation	VEIVGGATRIPAVKE EEEECCCCCCHHHHH	32.19	20860994
347 (in isoform 3)	Ubiquitination	-	1.92	21906983
351	2-Hydroxyisobutyrylation	ATRIPAVKERIAKFF CCCCHHHHHHHHHHH	43.30	-
351	Ubiquitination	ATRIPAVKERIAKFF CCCCHHHHHHHHHHH	43.30	-
356	2-Hydroxyisobutyrylation	AVKERIAKFFGKDIS HHHHHHHHHHCCCHH	38.56	-
356	Acetylation	AVKERIAKFFGKDIS HHHHHHHHHHCCCHH	38.56	25953088
356	Ubiquitination	AVKERIAKFFGKDIS HHHHHHHHHHCCCHH	38.56	-
360	Acetylation	RIAKFFGKDISTTLN HHHHHHCCCHHHCCC	46.89	26051181
360	Ubiquitination	RIAKFFGKDISTTLN HHHHHHCCCHHHCCC	46.89	-
365	Phosphorylation	FGKDISTTLNADEAV HCCCHHHCCCHHHHH	15.95	-
376	Glutathionylation	DEAVARGCALQCAIL HHHHHHHHHHHHHHH	2.59	22555962
376	S-palmitoylation	DEAVARGCALQCAIL HHHHHHHHHHHHHHH	2.59	29575903
380	S-palmitoylation	ARGCALQCAILSPAF HHHHHHHHHHHCCCE	2.37	29575903
384	Phosphorylation	ALQCAILSPAFKVRE HHHHHHHCCCEEEEE	14.20	25159151
388	Methylation	AILSPAFKVREFSVT HHHCCCEEEEEEECC	42.35	7869883
388	Ubiquitination	AILSPAFKVREFSVT HHHCCCEEEEEEECC	42.35	22053931
388 (in isoform 2)	Ubiquitination	-	42.35	22053931
389 (in isoform 3)	Ubiquitination	-	5.99	21906983
390	Ubiquitination	LSPAFKVREFSVTDA HCCCEEEEEEECCCC	39.57	-
390 (in isoform 1)	Ubiquitination	-	39.57	21906983
417 (in isoform 3)	Ubiquitination	-	36.04	21906983
429	Phosphorylation	RNHAAPFSKVLTFLR CCCCCCHHHHHHHHH	22.31	25849741
430	Acetylation	NHAAPFSKVLTFLRR CCCCCHHHHHHHHHH	41.46	19608861
430	Ubiquitination	NHAAPFSKVLTFLRR CCCCCHHHHHHHHHH	41.46	19608861
430 (in isoform 2)	Ubiquitination	-	41.46	22053931
430 (in isoform 3)	Ubiquitination	-	41.46	21906983
432	Acetylation	AAPFSKVLTFLRRGP CCCHHHHHHHHHHCC	3.01	19608861
432	Ubiquitination	AAPFSKVLTFLRRGP CCCHHHHHHHHHHCC	3.01	19608861
432 (in isoform 1)	Ubiquitination	-	3.01	21906983
433	Phosphorylation	APFSKVLTFLRRGPF CCHHHHHHHHHHCCE	24.50	23312004
446	Phosphorylation	PFELEAFYSDPQGVP CEEEEEEEECCCCCC	21.15	-
458	Ubiquitination	GVPYPEAKIGRFVVQ CCCCCHHHHCCEEEE	43.99	22053931
458 (in isoform 2)	Ubiquitination	-	43.99	22053931
460 (in isoform 1)	Ubiquitination	-	19.10	21906983
468	Phosphorylation	RFVVQNVSAQKDGEK CEEEEECCCCCCCCC	32.31	27050516
471	2-Hydroxyisobutyrylation	VQNVSAQKDGEKSRV EEECCCCCCCCCCCE	68.37	-
471	Acetylation	VQNVSAQKDGEKSRV EEECCCCCCCCCCCE	68.37	23236377
471	Malonylation	VQNVSAQKDGEKSRV EEECCCCCCCCCCCE	68.37	26320211
471	Ubiquitination	VQNVSAQKDGEKSRV EEECCCCCCCCCCCE	68.37	-
471 (in isoform 2)	Ubiquitination	-	68.37	22053931
473 (in isoform 1)	Ubiquitination	-	51.79	21906983
475	Ubiquitination	SAQKDGEKSRVKVKV CCCCCCCCCCEEEEE	49.44	-
486	Phosphorylation	KVKVRVNTHGIFTIS EEEEEECCCCEEEEE	20.72	27273156
491	Phosphorylation	VNTHGIFTISTASMV ECCCCEEEEEEHHHE	16.46	27080861
493	Phosphorylation	THGIFTISTASMVEK CCCEEEEEEHHHEEE	18.18	23312004
494	Phosphorylation	HGIFTISTASMVEKV CCEEEEEEHHHEEEC	20.92	25693802
496	Phosphorylation	IFTISTASMVEKVPT EEEEEEHHHEEECCC	24.37	27080861
503	Phosphorylation	SMVEKVPTEENEMSS HHEEECCCCCCCCCC	59.94	28450419
509	Phosphorylation	PTEENEMSSEADMEC CCCCCCCCCHHHHHH	20.88	28450419
510	Phosphorylation	TEENEMSSEADMECL CCCCCCCCHHHHHHH	35.18	30576142
527	Phosphorylation	RPPENPDTDKNVQQD CCCCCCCCCCCCCCC	50.56	26074081
536	Phosphorylation	KNVQQDNSEAGTQPQ CCCCCCCCCCCCCCC	36.79	20068231
540	Phosphorylation	QDNSEAGTQPQVQTD CCCCCCCCCCCCCCC	44.09	29496963
546	Phosphorylation	GTQPQVQTDAQQTSQ CCCCCCCCCHHHHCC	34.15	30278072
551	Phosphorylation	VQTDAQQTSQSPPSP CCCCHHHHCCCCCCC	19.36	25159151
552	Phosphorylation	QTDAQQTSQSPPSPE CCCHHHHCCCCCCCC	25.07	25159151
554	Phosphorylation	DAQQTSQSPPSPELT CHHHHCCCCCCCCCC	38.25	30278072
557	Phosphorylation	QTSQSPPSPELTSEE HHCCCCCCCCCCCCC	34.10	25159151
561	Phosphorylation	SPPSPELTSEENKIP CCCCCCCCCCCCCCC	32.22	20201521
562	Phosphorylation	PPSPELTSEENKIPD CCCCCCCCCCCCCCC	56.38	30278072
582 (in isoform 2)	Ubiquitination	-	48.85	22053931
585 (in isoform 3)	Ubiquitination	-	68.87	21906983
588	Ubiquitination	PPEAKKPKIKVVNVE CCCCCCCCEEEEEEE	65.13	-
590	Ubiquitination	EAKKPKIKVVNVELP CCCCCCEEEEEEECC	46.38	-
611 (in isoform 2)	Ubiquitination	-	5.06	22053931
613	Sulfoxidation	LGKDLLNMYIETEGK HCHHHHHHHHHHCCC	3.44	28183972
614	Phosphorylation	GKDLLNMYIETEGKM CHHHHHHHHHHCCCH	8.43	-
626	Ubiquitination	GKMIMQDKLEKERND CCHHHHHHHHHHHHH	41.47	-
628 (in isoform 1)	Ubiquitination	-	59.62	21906983
635	Ubiquitination	EKERNDAKNAVEEYV HHHHHHHHHHHHHHH	48.59	-
641	Phosphorylation	AKNAVEEYVYEFRDK HHHHHHHHHHHHHHH	8.53	28152594
643	Phosphorylation	NAVEEYVYEFRDKLC HHHHHHHHHHHHHHC	14.40	28152594
648	Acetylation	YVYEFRDKLCGPYEK HHHHHHHHHCCCHHH	41.23	25953088
648	Ubiquitination	YVYEFRDKLCGPYEK HHHHHHHHHCCCHHH	41.23	-
653	Phosphorylation	RDKLCGPYEKFICEQ HHHHCCCHHHCEECH	19.62	28152594
655	2-Hydroxyisobutyrylation	KLCGPYEKFICEQDH HHCCCHHHCEECHHH	33.90	-
655	Acetylation	KLCGPYEKFICEQDH HHCCCHHHCEECHHH	33.90	25953088
655	Ubiquitination	KLCGPYEKFICEQDH HHCCCHHHCEECHHH	33.90	22053931
657	Ubiquitination	CGPYEKFICEQDHQN CCCHHHCEECHHHHH	3.61	-
659 (in isoform 2)	Ubiquitination	-	54.98	-
670	Phosphorylation	QNFLRLLTETEDWLY HHHHHHHHHCHHHHH	45.51	-
672	Phosphorylation	FLRLLTETEDWLYEE HHHHHHHCHHHHHHC	33.73	-
677	Phosphorylation	TETEDWLYEEGEDQA HHCHHHHHHCCHHHH	14.00	27259358
688	Phosphorylation	EDQAKQAYVDKLEEL HHHHHHHHHHHHHHH	13.49	-
691	2-Hydroxyisobutyrylation	AKQAYVDKLEELMKI HHHHHHHHHHHHHHH	47.99	-
691	Acetylation	AKQAYVDKLEELMKI HHHHHHHHHHHHHHH	47.99	23236377
691	Ubiquitination	AKQAYVDKLEELMKI HHHHHHHHHHHHHHH	47.99	21890473
697	2-Hydroxyisobutyrylation	DKLEELMKIGTPVKV HHHHHHHHHCCCEEE	51.08	-
697	Ubiquitination	DKLEELMKIGTPVKV HHHHHHHHHCCCEEE	51.08	-
699	Ubiquitination	LEELMKIGTPVKVRF HHHHHHHCCCEEEEC	20.60	-
700	Phosphorylation	EELMKIGTPVKVRFQ HHHHHHCCCEEEECH	28.51	27134283
703	2-Hydroxyisobutyrylation	MKIGTPVKVRFQEAE HHHCCCEEEECHHHH	28.97	-
703	Acetylation	MKIGTPVKVRFQEAE HHHCCCEEEECHHHH	28.97	25953088
703	Ubiquitination	MKIGTPVKVRFQEAE HHHCCCEEEECHHHH	28.97	-
714	Ubiquitination	QEAEERPKMFEELGQ HHHHHCHHHHHHHHH	63.54	-
728	Acetylation	QRLQHYAKIAADFRN HHHHHHHHHHHHHCC	26.22	25953088
739	2-Hydroxyisobutyrylation	DFRNKDEKYNHIDES HHCCCCHHCCCCCHH	62.58	-
740	Phosphorylation	FRNKDEKYNHIDESE HCCCCHHCCCCCHHH	15.21	28509920
749	Acetylation	HIDESEMKKVEKSVN CCCHHHHHHHHHHHH	50.01	25953088
749	Ubiquitination	HIDESEMKKVEKSVN CCCHHHHHHHHHHHH	50.01	-
750	Acetylation	IDESEMKKVEKSVNE CCHHHHHHHHHHHHH	55.08	25953088
753	Ubiquitination	SEMKKVEKSVNEVME HHHHHHHHHHHHHHH	63.79	-
771	Acetylation	NVMNAQAKKSLDQDP HHHHHHHHHHCCCCH	30.71	25953088
772	Ubiquitination	VMNAQAKKSLDQDPV HHHHHHHHHCCCCHH	60.30	-
790	Acetylation	QEIKTKIKELNNTCE HHHHHHHHHHCCCCC	58.67	26051181
790	Ubiquitination	QEIKTKIKELNNTCE HHHHHHHHHHCCCCC	58.67	2189047
795	Phosphorylation	KIKELNNTCEPVVTQ HHHHHCCCCCCCCCC	19.71	26074081
796	Glutathionylation	IKELNNTCEPVVTQP HHHHCCCCCCCCCCC	6.38	22555962
801	Phosphorylation	NTCEPVVTQPKPKIE CCCCCCCCCCCCCCC	39.11	26074081
804	Ubiquitination	EPVVTQPKPKIESPK CCCCCCCCCCCCCCC	49.47	-
806	Ubiquitination	VVTQPKPKIESPKLE CCCCCCCCCCCCCCC	66.29	-
809	Phosphorylation	QPKPKIESPKLERTP CCCCCCCCCCCCCCC	30.70	29255136
811	Acetylation	KPKIESPKLERTPNG CCCCCCCCCCCCCCC	72.72	83037497
811	Ubiquitination	KPKIESPKLERTPNG CCCCCCCCCCCCCCC	72.72	-
815	Phosphorylation	ESPKLERTPNGPNID CCCCCCCCCCCCCCC	16.25	30266825
823	Acetylation	PNGPNIDKKEEDLED CCCCCCCCCHHHCCC	59.28	27452117
823	Ubiquitination	PNGPNIDKKEEDLED CCCCCCCCCHHHCCC	59.28	-
824	Ubiquitination	NGPNIDKKEEDLEDK CCCCCCCCHHHCCCC	63.69	-
846	Phosphorylation	PHQNGECYPNEKNSV CCCCCCCCCCCCCCC	12.56	28555341
850	Acetylation	GECYPNEKNSVNMDL CCCCCCCCCCCCCCC	62.25	26051181
852	Phosphorylation	CYPNEKNSVNMDLD- CCCCCCCCCCCCCC-	26.41	25159151

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 HS105_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
509	S	Phosphorylation		-
Phosphorylation on Ser-509 may be important for regulation of the HSPA8/HSC70 chaperone activity.

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 HS105_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
COF1_HUMAN	CFL1	physical	14733918
DLRB1_HUMAN	DYNLRB1	physical	14733918
ADDA_MOUSE	Add1	physical	14733918
UBA1_MOUSE	Uba1	physical	14733918
PA1B3_MOUSE	Pafah1b3	physical	14733918
PGK1_MOUSE	Pgk1	physical	14733918
UBA1_HUMAN	UBA1	physical	14733918
PGK1_HUMAN	PGK1	physical	14733918
PA1B3_HUMAN	PAFAH1B3	physical	14733918
ADDA_HUMAN	ADD1	physical	14733918
CHD3_HUMAN	CHD3	physical	16169070
HIRP3_HUMAN	HIRIP3	physical	22863883
ANM3_HUMAN	PRMT3	physical	22863883
RANB3_HUMAN	RANBP3	physical	22863883
SF01_HUMAN	SF1	physical	22863883
XPO7_HUMAN	XPO7	physical	22863883
ASSY_HUMAN	ASS1	physical	26344197
TCPB_HUMAN	CCT2	physical	26344197
DNJA1_HUMAN	DNAJA1	physical	26344197
DNJA2_HUMAN	DNAJA2	physical	26344197
DNJA4_HUMAN	DNAJA4	physical	26344197
DNJB1_HUMAN	DNAJB1	physical	26344197
DNJB4_HUMAN	DNAJB4	physical	26344197
DNJC3_HUMAN	DNAJC3	physical	26344197
HSP72_HUMAN	HSPA2	physical	26344197
HSP74_HUMAN	HSPA4	physical	26344197
STIP1_HUMAN	STIP1	physical	26344197
TAGL2_HUMAN	TAGLN2	physical	26344197
TAGL3_HUMAN	TAGLN3	physical	26344197
SNUT2_HUMAN	USP39	physical	26344197
UBP7_HUMAN	USP7	physical	26344197

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 HS105_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"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-430, AND MASS SPECTROMETRY.	19608861 [Abstract]
Phosphorylation
Reference	PubMed
"Large-scale proteomics analysis of the human kinome."; Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.; Mol. Cell. Proteomics 8:1751-1764(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-809, AND MASSSPECTROMETRY.	19369195 [Abstract]
"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-557 AND SER-562, ANDMASS SPECTROMETRY.	19413330 [Abstract]
"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 THR-700; SER-809 ANDTHR-815, AND MASS SPECTROMETRY.	18669648 [Abstract]
"Phosphorylation analysis of primary human T lymphocytes usingsequential IMAC and titanium oxide enrichment."; Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.; J. Proteome Res. 7:5167-5176(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-809, AND MASSSPECTROMETRY.	19367720 [Abstract]
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column."; Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.; Anal. Sci. 24:161-166(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-31 AND SER-809, AND MASSSPECTROMETRY.	18187866 [Abstract]
"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry."; Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.; Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-557 AND SER-809, ANDMASS SPECTROMETRY.	17287340 [Abstract]
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."; Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.; J. Proteome Res. 6:4150-4162(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-809, AND MASSSPECTROMETRY.	17924679 [Abstract]
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization."; Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.; Nat. Biotechnol. 24:1285-1292(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-384 AND THR-815, ANDMASS SPECTROMETRY.	16964243 [Abstract]
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks."; Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.; Cell 127:635-648(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-809, AND MASSSPECTROMETRY.	17081983 [Abstract]
"Global phosphoproteome of HT-29 human colon adenocarcinoma cells."; Kim J.-E., Tannenbaum S.R., White F.M.; J. Proteome Res. 4:1339-1346(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-809, AND MASSSPECTROMETRY.	16083285 [Abstract]

show