dbPTM

UBA1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	UBA1_HUMAN
UniProt AC	P22314
Protein Name	Ubiquitin-like modifier-activating enzyme 1
Gene Name	UBA1
Organism	Homo sapiens (Human).
Sequence Length	1058
Subcellular Localization	Cytoplasm . Mitochondrion . Nucleus . Isoform 1: Nucleus . Isoform 2: Cytoplasm .
Protein Description	Catalyzes the first step in ubiquitin conjugation to mark cellular proteins for degradation through the ubiquitin-proteasome system. [PubMed: 1606621]
Protein Sequence	MSSSPLSKKRRVSGPDPKPGSNCSPAQSVLSEVPSVPTNGMAKNGSEADIDEGLYSRQLYVLGHEAMKRLQTSSVLVSGLRGLGVEIAKNIILGGVKAVTLHDQGTAQWADLSSQFYLREEDIGKNRAEVSQPRLAELNSYVPVTAYTGPLVEDFLSGFQVVVLTNTPLEDQLRVGEFCHNRGIKLVVADTRGLFGQLFCDFGEEMILTDSNGEQPLSAMVSMVTKDNPGVVTCLDEARHGFESGDFVSFSEVQGMVELNGNQPMEIKVLGPYTFSICDTSNFSDYIRGGIVSQVKVPKKISFKSLVASLAEPDFVVTDFAKFSRPAQLHIGFQALHQFCAQHGRPPRPRNEEDAAELVALAQAVNARALPAVQQNNLDEDLIRKLAYVAAGDLAPINAFIGGLAAQEVMKACSGKFMPIMQWLYFDALECLPEDKEVLTEDKCLQRQNRYDGQVAVFGSDLQEKLGKQKYFLVGAGAIGCELLKNFAMIGLGCGEGGEIIVTDMDTIEKSNLNRQFLFRPWDVTKLKSDTAAAAVRQMNPHIRVTSHQNRVGPDTERIYDDDFFQNLDGVANALDNVDARMYMDRRCVYYRKPLLESGTLGTKGNVQVVIPFLTESYSSSQDPPEKSIPICTLKNFPNAIEHTLQWARDEFEGLFKQPAENVNQYLTDPKFVERTLRLAGTQPLEVLEAVQRSLVLQRPQTWADCVTWACHHWHTQYSNNIRQLLHNFPPDQLTSSGAPFWSGPKRCPHPLTFDVNNPLHLDYVMAAANLFAQTYGLTGSQDRAAVATFLQSVQVPEFTPKSGVKIHVSDQELQSANASVDDSRLEELKATLPSPDKLPGFKMYPIDFEKDDDSNFHMDFIVAASNLRAENYDIPSADRHKSKLIAGKIIPAIATTTAAVVGLVCLELYKVVQGHRQLDSYKNGFLNLALPFFGFSEPLAAPRHQYYNQEWTLWDRFEVQGLQPNGEEMTLKQFLDYFKTEHKLEITMLSQGVSMLYSFFMPAAKLKERLDQPMTEIVSRVSKRKLGRHVRALVLELCCNDESGEDVEVPYVRYTIR

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MSSSPLSKK ------CCCCCCCCC	51.32	22814378
2	Phosphorylation	------MSSSPLSKK ------CCCCCCCCC	51.32	20068231
2 (in isoform 2)	Acetylation	-	51.32	22814378
3	Phosphorylation	-----MSSSPLSKKR -----CCCCCCCCCC	48.08	25159151
4	Phosphorylation	----MSSSPLSKKRR ----CCCCCCCCCCC	38.87	23401153
6 (in isoform 2)	Phosphorylation	-	14.67	29743597
7	Phosphorylation	-MSSSPLSKKRRVSG -CCCCCCCCCCCCCC	39.24	20873877
9	Ubiquitination	SSSPLSKKRRVSGPD CCCCCCCCCCCCCCC	41.90	-
13	Phosphorylation	LSKKRRVSGPDPKPG CCCCCCCCCCCCCCC	42.68	22167270
21	Phosphorylation	GPDPKPGSNCSPAQS CCCCCCCCCCCHHHH	43.10	22167270
24	Phosphorylation	PKPGSNCSPAQSVLS CCCCCCCCHHHHHHH	27.76	22167270
28	Phosphorylation	SNCSPAQSVLSEVPS CCCCHHHHHHHCCCC	27.42	22167270
31	Phosphorylation	SPAQSVLSEVPSVPT CHHHHHHHCCCCCCC	34.10	30278072
35	Phosphorylation	SVLSEVPSVPTNGMA HHHHCCCCCCCCCCC	46.00	23927012
38	Phosphorylation	SEVPSVPTNGMAKNG HCCCCCCCCCCCCCC	42.10	23927012
46	Phosphorylation	NGMAKNGSEADIDEG CCCCCCCCCCCCCCC	38.72	29255136
55	Phosphorylation	ADIDEGLYSRQLYVL CCCCCCHHHHHHHHH	16.80	21945579
56	Phosphorylation	DIDEGLYSRQLYVLG CCCCCHHHHHHHHHC	20.70	21945579
60	Phosphorylation	GLYSRQLYVLGHEAM CHHHHHHHHHCHHHH	5.81	28796482
67	Sulfoxidation	YVLGHEAMKRLQTSS HHHCHHHHHHHHHHH	2.06	30846556
68	2-Hydroxyisobutyrylation	VLGHEAMKRLQTSSV HHCHHHHHHHHHHHH	57.94	-
68	Acetylation	VLGHEAMKRLQTSSV HHCHHHHHHHHHHHH	57.94	25953088
68	Succinylation	VLGHEAMKRLQTSSV HHCHHHHHHHHHHHH	57.94	23954790
68	Ubiquitination	VLGHEAMKRLQTSSV HHCHHHHHHHHHHHH	57.94	21890473
72	Phosphorylation	EAMKRLQTSSVLVSG HHHHHHHHHHHHHHC	27.79	26270265
73	Phosphorylation	AMKRLQTSSVLVSGL HHHHHHHHHHHHHCC	12.89	26270265
74	O-linked_Glycosylation	MKRLQTSSVLVSGLR HHHHHHHHHHHHCCH	23.90	23301498
74	Phosphorylation	MKRLQTSSVLVSGLR HHHHHHHHHHHHCCH	23.90	21712546
78	O-linked_Glycosylation	QTSSVLVSGLRGLGV HHHHHHHHCCHHHCH	28.13	23301498
78	Phosphorylation	QTSSVLVSGLRGLGV HHHHHHHHCCHHHCH	28.13	26546556
81	Methylation	SVLVSGLRGLGVEIA HHHHHCCHHHCHHHH	41.64	115919325
89	Acetylation	GLGVEIAKNIILGGV HHCHHHHHHHEECCE	55.10	134137
89	Ubiquitination	GLGVEIAKNIILGGV HHCHHHHHHHEECCE	55.10	21906983
97	Ubiquitination	NIILGGVKAVTLHDQ HHEECCEEEEEECCC	40.18	-
119	Methylation	LSSQFYLREEDIGKN HHHCEEEEHHHHCCC	33.60	115919297
140	Phosphorylation	PRLAELNSYVPVTAY CCHHHHHCCCCEEEE	39.88	21406692
141	Phosphorylation	RLAELNSYVPVTAYT CHHHHHCCCCEEEEC	14.01	21406692
185	Acetylation	FCHNRGIKLVVADTR HHHHCCCEEEEECCC	37.74	25953088
185	Ubiquitination	FCHNRGIKLVVADTR HHHHCCCEEEEECCC	37.74	21906983
191	Phosphorylation	IKLVVADTRGLFGQL CEEEEECCCCHHCHH	19.52	21406692
234	S-nitrosocysteine	DNPGVVTCLDEARHG CCCCCEEEEHHHCCC	2.81	-
234	Glutathionylation	DNPGVVTCLDEARHG CCCCCEEEEHHHCCC	2.81	22555962
234	S-nitrosylation	DNPGVVTCLDEARHG CCCCCEEEEHHHCCC	2.81	22178444
273	Phosphorylation	EIKVLGPYTFSICDT EEEEECCEEEEEECC	20.72	23663014
274	Phosphorylation	IKVLGPYTFSICDTS EEEECCEEEEEECCC	17.65	23663014
276	Phosphorylation	VLGPYTFSICDTSNF EECCEEEEEECCCCH	17.95	23663014
280	Phosphorylation	YTFSICDTSNFSDYI EEEEEECCCCHHHHC	22.59	23663014
281	Phosphorylation	TFSICDTSNFSDYIR EEEEECCCCHHHHCC	23.72	23663014
284	Phosphorylation	ICDTSNFSDYIRGGI EECCCCHHHHCCCCC	33.48	20201521
286	Phosphorylation	DTSNFSDYIRGGIVS CCCCHHHHCCCCCCC	7.42	23663014
288	Methylation	SNFSDYIRGGIVSQV CCHHHHCCCCCCCCC	30.93	115919301
293	Phosphorylation	YIRGGIVSQVKVPKK HCCCCCCCCCCCCCC	27.60	23663014
296	2-Hydroxyisobutyrylation	GGIVSQVKVPKKISF CCCCCCCCCCCCCCH	45.22	-
296	Acetylation	GGIVSQVKVPKKISF CCCCCCCCCCCCCCH	45.22	25953088
296	Ubiquitination	GGIVSQVKVPKKISF CCCCCCCCCCCCCCH	45.22	-
300	Ubiquitination	SQVKVPKKISFKSLV CCCCCCCCCCHHHHH	37.20	-
302	Phosphorylation	VKVPKKISFKSLVAS CCCCCCCCHHHHHHH	35.19	24719451
304	Methylation	VPKKISFKSLVASLA CCCCCCHHHHHHHHC	35.77	30799361
304	Ubiquitination	VPKKISFKSLVASLA CCCCCCHHHHHHHHC	35.77	21906983
305	Phosphorylation	PKKISFKSLVASLAE CCCCCHHHHHHHHCC	26.51	20068231
309	Phosphorylation	SFKSLVASLAEPDFV CHHHHHHHHCCCCEE	22.19	20068231
318	Phosphorylation	AEPDFVVTDFAKFSR CCCCEEEECHHHCCC	21.79	20068231
322	Ubiquitination	FVVTDFAKFSRPAQL EEEECHHHCCCCCHH	43.81	21906983
368	Methylation	LAQAVNARALPAVQQ HHHHHHHCCCHHHHC	31.30	115919305
384	Methylation	NLDEDLIRKLAYVAA CCCHHHHHHHHHHHH	34.92	115919309
385	Ubiquitination	LDEDLIRKLAYVAAG CCHHHHHHHHHHHHC	30.40	-
388	Phosphorylation	DLIRKLAYVAAGDLA HHHHHHHHHHHCCCH	10.89	-
411	Ubiquitination	LAAQEVMKACSGKFM HHHHHHHHHCCCCCC	51.95	-
416	Ubiquitination	VMKACSGKFMPIMQW HHHHCCCCCCHHHHH	23.38	-
443	Acetylation	KEVLTEDKCLQRQNR CCCCCCCHHHHHCCC	30.52	27452117
443	Ubiquitination	KEVLTEDKCLQRQNR CCCCCCCHHHHHCCC	30.52	21906983
451	Phosphorylation	CLQRQNRYDGQVAVF HHHHCCCCCCEEEEE	31.79	28152594
460	Phosphorylation	GQVAVFGSDLQEKLG CEEEEECHHHHHHHC	24.55	21712546
465	2-Hydroxyisobutyrylation	FGSDLQEKLGKQKYF ECHHHHHHHCCCCEE	49.97	-
465	Acetylation	FGSDLQEKLGKQKYF ECHHHHHHHCCCCEE	49.97	23954790
465	Ubiquitination	FGSDLQEKLGKQKYF ECHHHHHHHCCCCEE	49.97	21906983
468	Ubiquitination	DLQEKLGKQKYFLVG HHHHHHCCCCEEEEC	54.79	-
470	Acetylation	QEKLGKQKYFLVGAG HHHHCCCCEEEECCH	41.26	134141
470	Ubiquitination	QEKLGKQKYFLVGAG HHHHCCCCEEEECCH	41.26	21906983
481	Glutathionylation	VGAGAIGCELLKNFA ECCHHHHHHHHHHCE	2.45	22555962
510	Ubiquitination	TDMDTIEKSNLNRQF ECCCCCCCCCCCCCC	40.57	-
511	Phosphorylation	DMDTIEKSNLNRQFL CCCCCCCCCCCCCCC	33.49	23882029
526	2-Hydroxyisobutyrylation	FRPWDVTKLKSDTAA CCCCCHHHCCHHHHH	54.49	-
526	Acetylation	FRPWDVTKLKSDTAA CCCCCHHHCCHHHHH	54.49	25953088
526	Ubiquitination	FRPWDVTKLKSDTAA CCCCCHHHCCHHHHH	54.49	21906983
528	2-Hydroxyisobutyrylation	PWDVTKLKSDTAAAA CCCHHHCCHHHHHHH	48.09	-
528	Succinylation	PWDVTKLKSDTAAAA CCCHHHCCHHHHHHH	48.09	-
528	Succinylation	PWDVTKLKSDTAAAA CCCHHHCCHHHHHHH	48.09	23954790
528	Sumoylation	PWDVTKLKSDTAAAA CCCHHHCCHHHHHHH	48.09	-
528	Ubiquitination	PWDVTKLKSDTAAAA CCCHHHCCHHHHHHH	48.09	-
529	Phosphorylation	WDVTKLKSDTAAAAV CCHHHCCHHHHHHHH	51.10	20068231
531	Phosphorylation	VTKLKSDTAAAAVRQ HHHCCHHHHHHHHHH	25.86	20068231
551	Methylation	RVTSHQNRVGPDTER EEEECCCCCCCCCCC	28.35	115919313
558	Methylation	RVGPDTERIYDDDFF CCCCCCCCCCCCCHH	34.55	115919317
560	Phosphorylation	GPDTERIYDDDFFQN CCCCCCCCCCCHHHC	21.38	21253578
590	Phosphorylation	YMDRRCVYYRKPLLE HHCCCCCEEECCCHH	10.94	17360941
591	Phosphorylation	MDRRCVYYRKPLLES HCCCCCEEECCCHHC	7.55	30576142
593	Acetylation	RRCVYYRKPLLESGT CCCCEEECCCHHCCC	24.72	19666805
593	Ubiquitination	RRCVYYRKPLLESGT CCCCEEECCCHHCCC	24.72	21906983
600	Phosphorylation	KPLLESGTLGTKGNV CCCHHCCCCCCCCCE	31.15	28674419
603	Phosphorylation	LESGTLGTKGNVQVV HHCCCCCCCCCEEEE	38.60	-
604	Acetylation	ESGTLGTKGNVQVVI HCCCCCCCCCEEEEE	46.84	19666811
604	Sumoylation	ESGTLGTKGNVQVVI HCCCCCCCCCEEEEE	46.84	-
604	Ubiquitination	ESGTLGTKGNVQVVI HCCCCCCCCCEEEEE	46.84	21906983
615	Phosphorylation	QVVIPFLTESYSSSQ EEEEEEECCCCCCCC	24.22	30576142
617	Phosphorylation	VIPFLTESYSSSQDP EEEEECCCCCCCCCC	25.69	27251275
618	Phosphorylation	IPFLTESYSSSQDPP EEEECCCCCCCCCCC	13.31	27251275
619	O-linked_Glycosylation	PFLTESYSSSQDPPE EEECCCCCCCCCCCC	32.56	23301498
619	Phosphorylation	PFLTESYSSSQDPPE EEECCCCCCCCCCCC	32.56	27251275
620	Phosphorylation	FLTESYSSSQDPPEK EECCCCCCCCCCCCC	24.64	27690223
621	Phosphorylation	LTESYSSSQDPPEKS ECCCCCCCCCCCCCC	32.44	27251275
627	Acetylation	SSQDPPEKSIPICTL CCCCCCCCCCCEEEE	60.50	26051181
627	Ubiquitination	SSQDPPEKSIPICTL CCCCCCCCCCCEEEE	60.50	21906983
628	Phosphorylation	SQDPPEKSIPICTLK CCCCCCCCCCEEEEC	31.75	25159151
632	S-nitrosocysteine	PEKSIPICTLKNFPN CCCCCCEEEECCCCC	2.82	-
632	S-nitrosylation	PEKSIPICTLKNFPN CCCCCCEEEECCCCC	2.82	19483679
632	S-palmitoylation	PEKSIPICTLKNFPN CCCCCCEEEECCCCC	2.82	21044946
635	Acetylation	SIPICTLKNFPNAIE CCCEEEECCCCCHHH	38.09	25953088
635	Sumoylation	SIPICTLKNFPNAIE CCCEEEECCCCCHHH	38.09	-
635	Ubiquitination	SIPICTLKNFPNAIE CCCEEEECCCCCHHH	38.09	21906983
657	Acetylation	DEFEGLFKQPAENVN HHHHHHHCCCCCHHH	61.49	26051181
657	Ubiquitination	DEFEGLFKQPAENVN HHHHHHHCCCCCHHH	61.49	21906983
666	Phosphorylation	PAENVNQYLTDPKFV CCCHHHHHHCCHHHH	13.33	28152594
668	Phosphorylation	ENVNQYLTDPKFVER CHHHHHHCCHHHHHH	45.37	24719451
671	Acetylation	NQYLTDPKFVERTLR HHHHCCHHHHHHHHH	65.92	19608861
671	Malonylation	NQYLTDPKFVERTLR HHHHCCHHHHHHHHH	65.92	26320211
671	Ubiquitination	NQYLTDPKFVERTLR HHHHCCHHHHHHHHH	65.92	21890473
678	Methylation	KFVERTLRLAGTQPL HHHHHHHHHCCCCCH	23.14	115919321
682	Phosphorylation	RTLRLAGTQPLEVLE HHHHHCCCCCHHHHH	22.77	17525332
735	Phosphorylation	NFPPDQLTSSGAPFW HCCHHHCCCCCCCCC	18.40	28122231
736	Phosphorylation	FPPDQLTSSGAPFWS CCHHHCCCCCCCCCC	35.05	28122231
737	Phosphorylation	PPDQLTSSGAPFWSG CHHHCCCCCCCCCCC	33.47	28122231
743	Phosphorylation	SSGAPFWSGPKRCPH CCCCCCCCCCCCCCC	45.67	28122231
746	Acetylation	APFWSGPKRCPHPLT CCCCCCCCCCCCCCE	70.88	26051181
746	Ubiquitination	APFWSGPKRCPHPLT CCCCCCCCCCCCCCE	70.88	21906983
781	Phosphorylation	QTYGLTGSQDRAAVA HHHCCCCCHHHHHHH	24.54	-
789	Phosphorylation	QDRAAVATFLQSVQV HHHHHHHHHHHHCCC	20.48	21712546
793	Phosphorylation	AVATFLQSVQVPEFT HHHHHHHHCCCCCCC	19.36	30087585
800	Phosphorylation	SVQVPEFTPKSGVKI HCCCCCCCCCCCCEE	28.30	21712546
802	Ubiquitination	QVPEFTPKSGVKIHV CCCCCCCCCCCEEEE	57.70	21906983
803	Phosphorylation	VPEFTPKSGVKIHVS CCCCCCCCCCEEEEC	50.45	28464451
806	Ubiquitination	FTPKSGVKIHVSDQE CCCCCCCEEEECHHH	30.53	-
810	Phosphorylation	SGVKIHVSDQELQSA CCCEEEECHHHHHHC	21.29	30266825
816	Phosphorylation	VSDQELQSANASVDD ECHHHHHHCCCCCCH	35.79	29255136
820	Phosphorylation	ELQSANASVDDSRLE HHHHCCCCCCHHHHH	26.36	25159151
824	Phosphorylation	ANASVDDSRLEELKA CCCCCCHHHHHHHHH	34.01	23898821
830	Ubiquitination	DSRLEELKATLPSPD HHHHHHHHHHCCCCC	42.47	-
832	Phosphorylation	RLEELKATLPSPDKL HHHHHHHHCCCCCCC	37.30	30266825
835	Phosphorylation	ELKATLPSPDKLPGF HHHHHCCCCCCCCCC	49.17	29255136
838	2-Hydroxyisobutyrylation	ATLPSPDKLPGFKMY HHCCCCCCCCCCEEE	61.02	-
838	Acetylation	ATLPSPDKLPGFKMY HHCCCCCCCCCCEEE	61.02	23749302
838	Ubiquitination	ATLPSPDKLPGFKMY HHCCCCCCCCCCEEE	61.02	21906983
843	Ubiquitination	PDKLPGFKMYPIDFE CCCCCCCEEEECCCC	43.36	21890473
855	Phosphorylation	DFEKDDDSNFHMDFI CCCCCCCCCCCHHEE	48.68	28348404
866	Phosphorylation	MDFIVAASNLRAENY HHEEEEECCCCCCCC	27.02	-
873	Phosphorylation	SNLRAENYDIPSADR CCCCCCCCCCCCCHH	13.52	28152594
877	Phosphorylation	AENYDIPSADRHKSK CCCCCCCCCHHHHHH	43.04	26437602
880	Methylation	YDIPSADRHKSKLIA CCCCCCHHHHHHHHH	38.56	115919329
882	Ubiquitination	IPSADRHKSKLIAGK CCCCHHHHHHHHHCC	50.62	-
884	2-Hydroxyisobutyrylation	SADRHKSKLIAGKII CCHHHHHHHHHCCHH	49.03	-
884	Acetylation	SADRHKSKLIAGKII CCHHHHHHHHHCCHH	49.03	25953088
884	Ubiquitination	SADRHKSKLIAGKII CCHHHHHHHHHCCHH	49.03	-
889	Ubiquitination	KSKLIAGKIIPAIAT HHHHHHCCHHHHHHH	28.57	-
898	Phosphorylation	IPAIATTTAAVVGLV HHHHHHHHHHHHHHH	14.31	21601212
906	S-palmitoylation	AAVVGLVCLELYKVV HHHHHHHHHHHHHHH	2.69	29575903
923	Ubiquitination	HRQLDSYKNGFLNLA HHCHHHHCCCCCCEE	55.32	-
957	Methylation	QEWTLWDRFEVQGLQ CCCEEHHCEEECCCC	20.31	115919333
970	Sulfoxidation	LQPNGEEMTLKQFLD CCCCCCEECHHHHHH	4.65	30846556
978	Phosphorylation	TLKQFLDYFKTEHKL CHHHHHHHHHHCCHH	14.77	-
980	Acetylation	KQFLDYFKTEHKLEI HHHHHHHHHCCHHHH	46.93	19608861
980	Ubiquitination	KQFLDYFKTEHKLEI HHHHHHHHHCCHHHH	46.93	19608861
991	Phosphorylation	KLEITMLSQGVSMLY HHHHEEHHHHHHHHH	17.67	22210691
1006	Ubiquitination	SFFMPAAKLKERLDQ HHHHCHHHHHHHCCC	63.30	-
1008	Ubiquitination	FMPAAKLKERLDQPM HHCHHHHHHHCCCHH	39.83	-
1015	Sulfoxidation	KERLDQPMTEIVSRV HHHCCCHHHHHHHHH	4.34	21406390
1016	Phosphorylation	ERLDQPMTEIVSRVS HHCCCHHHHHHHHHH	29.28	21406692
1020	Phosphorylation	QPMTEIVSRVSKRKL CHHHHHHHHHHHHHH	32.40	21406692
1024	Acetylation	EIVSRVSKRKLGRHV HHHHHHHHHHHHHHH	51.17	7481281
1044	Phosphorylation	ELCCNDESGEDVEVP HHHCCCCCCCCCCCC	50.80	26657352
1056	Phosphorylation	EVPYVRYTIR----- CCCEEEEEEC-----	10.34	24719451

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
4	S	Phosphorylation	Kinase	CDK1	P06493	PhosphoELM
4	S	Phosphorylation	Kinase	CDK1	P11440	PSP
13	S	Phosphorylation	Kinase	CK2-FAMILY	-	GPS
13	S	Phosphorylation	Kinase	CK2_GROUP	-	PhosphoELM
835	S	Phosphorylation	Kinase	CDK1	P06493	PhosphoELM

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of UBA1_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 UBA1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
DDB1_HUMAN	DDB1	physical	22145905
UBD_HUMAN	UBD	physical	22434192
UBE2B_HUMAN	UBE2B	physical	22069333
UB2R1_HUMAN	CDC34	physical	22069333
UB2D1_HUMAN	UBE2D1	physical	22069333
UB2D2_HUMAN	UBE2D2	physical	22069333
UB2D3_HUMAN	UBE2D3	physical	22069333
UB2L3_HUMAN	UBE2L3	physical	22069333
UB2E1_HUMAN	UBE2E1	physical	22069333
UB2E3_HUMAN	UBE2E3	physical	22069333
UBE2S_HUMAN	UBE2S	physical	22069333
UB2E2_HUMAN	UBE2E2	physical	22069333
UB2L3_HUMAN	UBE2L3	physical	22350887
UBE2A_HUMAN	UBE2A	physical	22427669
UBC_HUMAN	UBC	physical	23003343
WDR73_HUMAN	WDR73	physical	22939629
USH1C_HUMAN	USH1C	physical	22939629
UBE2K_HUMAN	UBE2K	physical	2265617
PUR9_HUMAN	ATIC	physical	22863883
PYRG1_HUMAN	CTPS1	physical	22863883
EZRI_HUMAN	EZR	physical	22863883
IPO5_HUMAN	IPO5	physical	22863883
MSHR_HUMAN	MC1R	physical	22863883
PABP1_HUMAN	PABPC1	physical	22863883
PDC6I_HUMAN	PDCD6IP	physical	22863883
RIC8A_HUMAN	RIC8A	physical	22863883
XPP1_HUMAN	XPNPEP1	physical	22863883
UBI4P_YEAST	UBI4	physical	2842867
UBC_HUMAN	UBC	physical	24816100
UB2R2_HUMAN	UBE2R2	physical	17597759
UBE2K_HUMAN	UBE2K	physical	17597759
UBE2H_HUMAN	UBE2H	physical	17597759
UBE2W_HUMAN	UBE2W	physical	17597759
UBE2C_HUMAN	UBE2C	physical	17597759
UBE2B_HUMAN	UBE2B	physical	17597759
UBE2A_HUMAN	UBE2A	physical	17597759
UBE2S_HUMAN	UBE2S	physical	17597759
UB2D1_HUMAN	UBE2D1	physical	17597759
UB2D2_HUMAN	UBE2D2	physical	17597759
UB2D3_HUMAN	UBE2D3	physical	17597759
UBE2T_HUMAN	UBE2T	physical	17597759
UB2R1_HUMAN	CDC34	physical	17597759
UB2J1_HUMAN	UBE2J1	physical	17597759
UB2E3_HUMAN	UBE2E3	physical	17597759
UB2E2_HUMAN	UBE2E2	physical	17597759
UB2E1_HUMAN	UBE2E1	physical	17597759
UB2G1_HUMAN	UBE2G1	physical	17597759
UB2L3_HUMAN	UBE2L3	physical	17597759
UB2G2_HUMAN	UBE2G2	physical	17597759
UB2R1_HUMAN	CDC34	physical	24912152
FUS_HUMAN	FUS	physical	25192599
UB2D2_HUMAN	UBE2D2	physical	25275296
UB2E1_HUMAN	UBE2E1	physical	8576257
UB2L3_HUMAN	UBE2L3	physical	8576257
UBA1_HUMAN	UBA1	physical	22350887
UBE2K_HUMAN	UBE2K	physical	9857030
UB2D2_HUMAN	UBE2D2	physical	19250909
UB2L3_HUMAN	UBE2L3	physical	19250909
UBE2C_HUMAN	UBE2C	physical	19250909
UBC2_YEAST	RAD6	physical	19250909
UBE2K_HUMAN	UBE2K	physical	8125920
UB2L6_HUMAN	UBE2L6	physical	9153201
UB2L3_HUMAN	UBE2L3	physical	11807090
UB2D1_HUMAN	UBE2D1	physical	11807090
UB2D2_HUMAN	UBE2D2	physical	11807090
UBE2C_HUMAN	UBE2C	physical	11807090
UBE2N_HUMAN	UBE2N	physical	14517261
UB2E1_HUMAN	UBE2E1	physical	16428300
UB2D3_HUMAN	UBE2D3	physical	25207809
UBE2A_HUMAN	UBE2A	physical	25527291
UBE2B_HUMAN	UBE2B	physical	25527291
UB2D1_HUMAN	UBE2D1	physical	25527291
UB2D4_HUMAN	UBE2D4	physical	25527291
UB2E1_HUMAN	UBE2E1	physical	25527291
UB2G2_HUMAN	UBE2G2	physical	25527291
UB2L3_HUMAN	UBE2L3	physical	25527291
UB2Q2_HUMAN	UBE2Q2	physical	25527291
UB2R1_HUMAN	CDC34	physical	25527291
UBE2S_HUMAN	UBE2S	physical	25527291
UBE2W_HUMAN	UBE2W	physical	25527291
UBE2N_HUMAN	UBE2N	physical	25527291
AP1G1_HUMAN	AP1G1	physical	26344197
AP1S1_HUMAN	AP1S1	physical	26344197
RHG01_HUMAN	ARHGAP1	physical	26344197
ARMC6_HUMAN	ARMC6	physical	26344197
DPP3_HUMAN	DPP3	physical	26344197
MCA3_HUMAN	EEF1E1	physical	26344197
GFPT1_HUMAN	GFPT1	physical	26344197
SYIC_HUMAN	IARS	physical	26344197
SYLC_HUMAN	LARS	physical	26344197
TYW4_HUMAN	LCMT2	physical	26344197
MK03_HUMAN	MAPK3	physical	26344197
NMD3_HUMAN	NMD3	physical	26344197
NPL4_HUMAN	NPLOC4	physical	26344197
NUP93_HUMAN	NUP93	physical	26344197
PCH2_HUMAN	TRIP13	physical	26344197
UCHL3_HUMAN	UCHL3	physical	26344197
NDUV3_HUMAN	NDUFV3	physical	26496610
NVL_HUMAN	NVL	physical	26496610
CTF8_HUMAN	CHTF8	physical	26496610
SAPC2_HUMAN	SAPCD2	physical	26496610
CHK1_HUMAN	CHEK1	physical	26296656
UBE2B_HUMAN	UBE2B	physical	21041297
UB2D2_HUMAN	UBE2D2	physical	21041297
UB2D2_HUMAN	UBE2D2	physical	28134249
UBE2N_HUMAN	UBE2N	physical	27173435

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
301830	Spinal muscular atrophy X-linked 2 (SMAX2)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of UBA1_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-671 AND LYS-980, AND MASSSPECTROMETRY.	19608861 [Abstract]
Phosphorylation
Reference	PubMed
"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-46 AND SER-810, AND MASSSPECTROMETRY.	19690332 [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-4 AND SER-835, AND MASSSPECTROMETRY.	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 SER-13; SER-24; SER-46;THR-800 AND SER-835, AND MASS SPECTROMETRY.	18669648 [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-46, AND MASSSPECTROMETRY.	16964243 [Abstract]
"Large-scale characterization of HeLa cell nuclear phosphoproteins."; Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-46, AND MASSSPECTROMETRY.	15302935 [Abstract]
"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-55, AND MASSSPECTROMETRY.	15592455 [Abstract]