dbPTM

HYOU1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	HYOU1_HUMAN
UniProt AC	Q9Y4L1
Protein Name	Hypoxia up-regulated protein 1
Gene Name	HYOU1
Organism	Homo sapiens (Human).
Sequence Length	999
Subcellular Localization	Endoplasmic reticulum lumen.
Protein Description	Has a pivotal role in cytoprotective cellular mechanisms triggered by oxygen deprivation. May play a role as a molecular chaperone and participate in protein folding..
Protein Sequence	MADKVRRQRPRRRVCWALVAVLLADLLALSDTLAVMSVDLGSESMKVAIVKPGVPMEIVLNKESRRKTPVIVTLKENERFFGDSAASMAIKNPKATLRYFQHLLGKQADNPHVALYQARFPEHELTFDPQRQTVHFQISSQLQFSPEEVLGMVLNYSRSLAEDFAEQPIKDAVITVPVFFNQAERRAVLQAARMAGLKVLQLINDNTATALSYGVFRRKDINTTAQNIMFYDMGSGSTVCTIVTYQMVKTKEAGMQPQLQIRGVGFDRTLGGLEMELRLRERLAGLFNEQRKGQRAKDVRENPRAMAKLLREANRLKTVLSANADHMAQIEGLMDDVDFKAKVTRVEFEELCADLFERVPGPVQQALQSAEMSLDEIEQVILVGGATRVPRVQEVLLKAVGKEELGKNINADEAAAMGAVYQAAALSKAFKVKPFVVRDAVVYPILVEFTREVEEEPGIHSLKHNKRVLFSRMGPYPQRKVITFNRYSHDFNFHINYGDLGFLGPEDLRVFGSQNLTTVKLKGVGDSFKKYPDYESKGIKAHFNLDESGVLSLDRVESVFETLVEDSAEEESTLTKLGNTISSLFGGGTTPDAKENGTDTVQEEEESPAEGSKDEPGEQVELKEEAEAPVEDGSQPPPPEPKGDATPEGEKATEKENGDKSEAQKPSEKAEAGPEGVAPAPEGEKKQKPARKRRMVEEIGVELVVLDLPDLPEDKLAQSVQKLQDLTLRDLEKQEREKAANSLEAFIFETQDKLYQPEYQEVSTEEQREEISGKLSAASTWLEDEGVGATTVMLKEKLAELRKLCQGLFFRVEERKKWPERLSALDNLLNHSSMFLKGARLIPEMDQIFTEVEMTTLEKVINETWAWKNATLAEQAKLPATEKPVLLSKDIEAKMMALDREVQYLLNKAKFTKPRPRPKDKNGTRAEPPLNASASDQGEKVIPPAGQTEDAEPISEPEKVETGSEPGDTEPLELGGPGAEPEQKEQSTGQKRPLKNDEL

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
19	Ubiquitination	RRVCWALVAVLLADL HHHHHHHHHHHHHHH	2.40	-
51	Ubiquitination	SMKVAIVKPGVPMEI EEEEEEECCCCCCEE	29.91	-
56	Sulfoxidation	IVKPGVPMEIVLNKE EECCCCCCEEEECCC	5.22	28465586
62	Ubiquitination	PMEIVLNKESRRKTP CCEEEECCCCCCCCC	53.56	-
75	2-Hydroxyisobutyrylation	TPVIVTLKENERFFG CCEEEEECCCCEECC	49.48	-
75	Acetylation	TPVIVTLKENERFFG CCEEEEECCCCEECC	49.48	26822725
75	Malonylation	TPVIVTLKENERFFG CCEEEEECCCCEECC	49.48	26320211
75	Ubiquitination	TPVIVTLKENERFFG CCEEEEECCCCEECC	49.48	-
79	Methylation	VTLKENERFFGDSAA EEECCCCEECCCHHH	43.72	115480067
88	Sulfoxidation	FGDSAASMAIKNPKA CCCHHHHHHHCCHHH	3.71	21406390
91	Ubiquitination	SAASMAIKNPKATLR HHHHHHHCCHHHHHH	58.63	21890473
91	Ubiquitination	SAASMAIKNPKATLR HHHHHHHCCHHHHHH	58.63	21890473
94	2-Hydroxyisobutyrylation	SMAIKNPKATLRYFQ HHHHCCHHHHHHHHH	64.49	-
94	Ubiquitination	SMAIKNPKATLRYFQ HHHHCCHHHHHHHHH	64.49	-
99	Phosphorylation	NPKATLRYFQHLLGK CHHHHHHHHHHHHCC	15.65	28152594
106	Ubiquitination	YFQHLLGKQADNPHV HHHHHHCCCCCCCCE	42.13	-
116	Phosphorylation	DNPHVALYQARFPEH CCCCEEEEEECCCCC	7.15	28152594
155	N-linked_Glycosylation	EVLGMVLNYSRSLAE HHHHHHHHHCHHHHH	22.71	12754519
155	N-linked_Glycosylation	EVLGMVLNYSRSLAE HHHHHHHHHCHHHHH	22.71	12754519
170	Ubiquitination	DFAEQPIKDAVITVP HHHHCCCCCEEEEHH	46.44	-
198	Acetylation	AARMAGLKVLQLIND HHHHCCCCEEHHHCC	39.73	155333
198	Ubiquitination	AARMAGLKVLQLIND HHHHCCCCEEHHHCC	39.73	-
207	Phosphorylation	LQLINDNTATALSYG EHHHCCCCHHHHHHC	28.40	25072903
209	Phosphorylation	LINDNTATALSYGVF HHCCCCHHHHHHCEE	26.54	25072903
212	Phosphorylation	DNTATALSYGVFRRK CCCHHHHHHCEECCC	19.85	25072903
213	Phosphorylation	NTATALSYGVFRRKD CCHHHHHHCEECCCC	20.40	25072903
221	Ubiquitination	GVFRRKDINTTAQNI CEECCCCCCCCCCEE	5.75	-
222	N-linked_Glycosylation	VFRRKDINTTAQNIM EECCCCCCCCCCEEE	41.32	UniProtKB CARBOHYD
255	Sulfoxidation	VKTKEAGMQPQLQIR EECCCCCCCCCEEEE	7.28	21406390
262	Methylation	MQPQLQIRGVGFDRT CCCCEEEEECCCCCC	22.30	115480059
269	Phosphorylation	RGVGFDRTLGGLEME EECCCCCCCCHHHHH	31.44	-
275	Sulfoxidation	RTLGGLEMELRLRER CCCCHHHHHHHHHHH	7.65	21406390
278	Methylation	GGLEMELRLRERLAG CHHHHHHHHHHHHHH	20.56	115480083
308	Acetylation	ENPRAMAKLLREANR HCHHHHHHHHHHHHH	34.66	25953088
308	Ubiquitination	ENPRAMAKLLREANR HCHHHHHHHHHHHHH	34.66	-
311	Ubiquitination	RAMAKLLREANRLKT HHHHHHHHHHHHHHH	51.96	21890473
315	Ubiquitination	KLLREANRLKTVLSA HHHHHHHHHHHHHHC	44.61	-
369	Phosphorylation	PVQQALQSAEMSLDE HHHHHHHHCCCCHHH	27.35	20860994
372	Sulfoxidation	QALQSAEMSLDEIEQ HHHHHCCCCHHHCCE	4.88	30846556
373	Phosphorylation	ALQSAEMSLDEIEQV HHHHCCCCHHHCCEE	24.95	21406692
376	Ubiquitination	SAEMSLDEIEQVILV HCCCCHHHCCEEEEE	54.44	-
387	Phosphorylation	VILVGGATRVPRVQE EEEECCCCCCHHHHH	35.16	20860994
398	Ubiquitination	RVQEVLLKAVGKEEL HHHHHHHHHHCHHHH	36.54	21890473
398	Acetylation	RVQEVLLKAVGKEEL HHHHHHHHHHCHHHH	36.54	27452117
398	Ubiquitination	RVQEVLLKAVGKEEL HHHHHHHHHHCHHHH	36.54	21890473
402	2-Hydroxyisobutyrylation	VLLKAVGKEELGKNI HHHHHHCHHHHCCCC	41.22	-
402	Acetylation	VLLKAVGKEELGKNI HHHHHHCHHHHCCCC	41.22	26822725
402	Ubiquitination	VLLKAVGKEELGKNI HHHHHHCHHHHCCCC	41.22	-
421	Phosphorylation	AAAMGAVYQAAALSK HHHHHHHHHHHHHHH	7.60	-
431	Acetylation	AALSKAFKVKPFVVR HHHHHHHCCCCEEEC	54.96	25953088
433	Ubiquitination	LSKAFKVKPFVVRDA HHHHHCCCCEEECCC	33.07	-
433	Ubiquitination	LSKAFKVKPFVVRDA HHHHHCCCCEEECCC	33.07	-
443	Phosphorylation	VVRDAVVYPILVEFT EECCCCHHHHHEEEE	4.30	-
461	Phosphorylation	EEEPGIHSLKHNKRV HCCCCCCCCCCCCEE	36.87	28450419
463	Acetylation	EPGIHSLKHNKRVLF CCCCCCCCCCCEEEE	48.42	25825284
463	Ubiquitination	EPGIHSLKHNKRVLF CCCCCCCCCCCEEEE	48.42	-
515	N-linked_Glycosylation	LRVFGSQNLTTVKLK HEEECCCCCEEEEEE	40.84	16263699
515	N-linked_Glycosylation	LRVFGSQNLTTVKLK HEEECCCCCEEEEEE	40.84	16263699
520	Ubiquitination	SQNLTTVKLKGVGDS CCCCEEEEEEECCHH	42.25	-
522	Ubiquitination	NLTTVKLKGVGDSFK CCEEEEEEECCHHHH	45.92	-
527	Phosphorylation	KLKGVGDSFKKYPDY EEEECCHHHHHCCCC	32.79	-
529	2-Hydroxyisobutyrylation	KGVGDSFKKYPDYES EECCHHHHHCCCCCC	56.18	-
529	Ubiquitination	KGVGDSFKKYPDYES EECCHHHHHCCCCCC	56.18	-
530	Acetylation	GVGDSFKKYPDYESK ECCHHHHHCCCCCCC	61.07	27178108
531	Phosphorylation	VGDSFKKYPDYESKG CCHHHHHCCCCCCCC	11.26	28152594
537	2-Hydroxyisobutyrylation	KYPDYESKGIKAHFN HCCCCCCCCCHHCCC	53.36	-
537	Ubiquitination	KYPDYESKGIKAHFN HCCCCCCCCCHHCCC	53.36	-
562	Phosphorylation	RVESVFETLVEDSAE HHHHHHHHHHCCCHH	25.33	25693802
567	Phosphorylation	FETLVEDSAEEESTL HHHHHCCCHHHHHHH	24.87	29255136
572	Phosphorylation	EDSAEEESTLTKLGN CCCHHHHHHHHHHHH	31.81	29691806
573	Phosphorylation	DSAEEESTLTKLGNT CCHHHHHHHHHHHHH	41.55	29691806
575	Phosphorylation	AEEESTLTKLGNTIS HHHHHHHHHHHHHHH	25.06	25693802
580	O-linked_Glycosylation	TLTKLGNTISSLFGG HHHHHHHHHHHHHCC	22.04	55825385
580	Phosphorylation	TLTKLGNTISSLFGG HHHHHHHHHHHHHCC	22.04	30622161
582	Phosphorylation	TKLGNTISSLFGGGT HHHHHHHHHHHCCCC	20.96	25850435
583	Phosphorylation	KLGNTISSLFGGGTT HHHHHHHHHHCCCCC	24.70	25850435
589	O-linked_Glycosylation	SSLFGGGTTPDAKEN HHHHCCCCCCCHHHC	38.13	55834607
589	Phosphorylation	SSLFGGGTTPDAKEN HHHHCCCCCCCHHHC	38.13	25627689
590	O-linked_Glycosylation	SLFGGGTTPDAKENG HHHCCCCCCCHHHCC	23.57	55834613
590	Phosphorylation	SLFGGGTTPDAKENG HHHCCCCCCCHHHCC	23.57	25159151
596	N-linked_Glycosylation	TTPDAKENGTDTVQE CCCCHHHCCCCCCHH	58.94	12754519
596	N-linked_Glycosylation	TTPDAKENGTDTVQE CCCCHHHCCCCCCHH	58.94	12754519
600	Phosphorylation	AKENGTDTVQEEEES HHHCCCCCCHHHHCC	24.75	-
634	O-linked_Glycosylation	EAPVEDGSQPPPPEP CCCCCCCCCCCCCCC	52.41	OGP
634	Phosphorylation	EAPVEDGSQPPPPEP CCCCCCCCCCCCCCC	52.41	25159151
722	2-Hydroxyisobutyrylation	KLAQSVQKLQDLTLR HHHHHHHHHHHCCHH	46.06	-
727	Phosphorylation	VQKLQDLTLRDLEKQ HHHHHHCCHHHHHHH	28.21	20068231
738	Ubiquitination	LEKQEREKAANSLEA HHHHHHHHHHHHHHH	60.05	-
742	Phosphorylation	EREKAANSLEAFIFE HHHHHHHHHHHHHHH	23.90	27050516
750	Phosphorylation	LEAFIFETQDKLYQP HHHHHHHCCCHHCCC	31.17	25278378
753	Ubiquitination	FIFETQDKLYQPEYQ HHHHCCCHHCCCCHH	39.00	-
755	Phosphorylation	FETQDKLYQPEYQEV HHCCCHHCCCCHHCC	27.97	25278378
759	Phosphorylation	DKLYQPEYQEVSTEE CHHCCCCHHCCCCHH	19.36	25278378
763	Phosphorylation	QPEYQEVSTEEQREE CCCHHCCCCHHHHHH	29.37	25278378
764	Phosphorylation	PEYQEVSTEEQREEI CCHHCCCCHHHHHHH	49.03	25278378
797	2-Hydroxyisobutyrylation	TTVMLKEKLAELRKL HHHHHHHHHHHHHHH	51.95	-
830	N-linked_Glycosylation	SALDNLLNHSSMFLK HHHHHHHHHCHHHHH	35.84	19522481
830	N-linked_Glycosylation	SALDNLLNHSSMFLK HHHHHHHHHCHHHHH	35.84	12754519
832	O-linked_Glycosylation	LDNLLNHSSMFLKGA HHHHHHHCHHHHHHC	23.56	30059200
845	Sulfoxidation	GARLIPEMDQIFTEV HCCCCHHHHHHHHHH	3.74	30846556
850	Phosphorylation	PEMDQIFTEVEMTTL HHHHHHHHHHCHHHH	40.53	-
854	Sulfoxidation	QIFTEVEMTTLEKVI HHHHHHCHHHHHHHH	4.13	30846556
862	N-linked_Glycosylation	TTLEKVINETWAWKN HHHHHHHHHCCHHHC	43.57	12754519
862	N-linked_Glycosylation	TTLEKVINETWAWKN HHHHHHHHHCCHHHC	43.57	12754519
869	N-linked_Glycosylation	NETWAWKNATLAEQA HHCCHHHCCCHHHHC	27.70	UniProtKB CARBOHYD
869	N-linked_Glycosylation	NETWAWKNATLAEQA HHCCHHHCCCHHHHC	27.70	16335952
883	2-Hydroxyisobutyrylation	AKLPATEKPVLLSKD CCCCCCCCCEEECCH	35.75	-
883	Acetylation	AKLPATEKPVLLSKD CCCCCCCCCEEECCH	35.75	25953088
883	Malonylation	AKLPATEKPVLLSKD CCCCCCCCCEEECCH	35.75	26320211
889	2-Hydroxyisobutyrylation	EKPVLLSKDIEAKMM CCCEEECCHHHHHHH	63.80	-
894	2-Hydroxyisobutyrylation	LSKDIEAKMMALDRE ECCHHHHHHHHHHHH	19.20	-
894	Acetylation	LSKDIEAKMMALDRE ECCHHHHHHHHHHHH	19.20	26822725
900	Methylation	AKMMALDREVQYLLN HHHHHHHHHHHHHHH	47.00	115480075
904	Phosphorylation	ALDREVQYLLNKAKF HHHHHHHHHHHHHCC	20.52	28152594
908	2-Hydroxyisobutyrylation	EVQYLLNKAKFTKPR HHHHHHHHHCCCCCC	53.58	-
922	N-linked_Glycosylation	RPRPKDKNGTRAEPP CCCCCCCCCCCCCCC	68.17	UniProtKB CARBOHYD
931	N-linked_Glycosylation	TRAEPPLNASASDQG CCCCCCCCCCCCCCC	37.31	17623646
931	N-linked_Glycosylation	TRAEPPLNASASDQG CCCCCCCCCCCCCCC	37.31	12754519
933	O-linked_Glycosylation	AEPPLNASASDQGEK CCCCCCCCCCCCCCC	27.51	30059200
948	Phosphorylation	VIPPAGQTEDAEPIS CCCCCCCCCCCCCCC	34.61	26091039
955	Phosphorylation	TEDAEPISEPEKVET CCCCCCCCCCCCCCC	58.79	29507054
962	Phosphorylation	SEPEKVETGSEPGDT CCCCCCCCCCCCCCC	49.33	25627689
964	O-linked_Glycosylation	PEKVETGSEPGDTEP CCCCCCCCCCCCCCC	48.30	OGP
964	Phosphorylation	PEKVETGSEPGDTEP CCCCCCCCCCCCCCC	48.30	25627689

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 HYOU1_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of HYOU1_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 HYOU1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
RPAC1_HUMAN	POLR1C	physical	22939629
NUP37_HUMAN	NUP37	physical	22939629
ARMX3_HUMAN	ARMCX3	physical	22863883
BCAR1_HUMAN	BCAR1	physical	22863883
BIN1_HUMAN	BIN1	physical	22863883
KI13A_HUMAN	KIF13A	physical	22863883
MCM2_HUMAN	MCM2	physical	22863883
MSH6_HUMAN	MSH6	physical	22863883
XRCC5_HUMAN	XRCC5	physical	22863883
XRCC6_HUMAN	XRCC6	physical	22863883
DJB11_HUMAN	DNAJB11	physical	26344197
DNJC7_HUMAN	DNAJC7	physical	26344197
ERF1_HUMAN	ETF1	physical	26344197
HXK1_HUMAN	HK1	physical	26344197
HXK2_HUMAN	HK2	physical	26344197
NU205_HUMAN	NUP205	physical	26344197
SE1L1_HUMAN	SEL1L	physical	27030672

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 HYOU1_HUMAN

Related Literatures of Post-Translational Modification

N-linked Glycosylation
Reference	PubMed
"Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins."; Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,Schiess R., Aebersold R., Watts J.D.; Nat. Biotechnol. 27:378-386(2009). Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-515, AND MASSSPECTROMETRY.	19349973 [Abstract]
"Glycoproteomics analysis of human liver tissue by combination ofmultiple enzyme digestion and hydrazide chemistry."; Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.; J. Proteome Res. 8:651-661(2009). Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-515; ASN-596; ASN-830;ASN-862 AND ASN-931, AND MASS SPECTROMETRY.	19159218 [Abstract]
"Elucidation of N-glycosylation sites on human platelet proteins: aglycoproteomic approach."; Lewandrowski U., Moebius J., Walter U., Sickmann A.; Mol. Cell. Proteomics 5:226-233(2006). Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-515, AND MASSSPECTROMETRY.	16263699 [Abstract]
"Human plasma N-glycoproteome analysis by immunoaffinity subtraction,hydrazide chemistry, and mass spectrometry."; Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E.,Moore R.J., Smith R.D.; J. Proteome Res. 4:2070-2080(2005). Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-515; ASN-830; ASN-869 ANDASN-931, AND MASS SPECTROMETRY.	16335952 [Abstract]
"Identification and quantification of N-linked glycoproteins usinghydrazide chemistry, stable isotope labeling and mass spectrometry."; Zhang H., Li X.-J., Martin D.B., Aebersold R.; Nat. Biotechnol. 21:660-666(2003). Cited for: GLYCOSYLATION AT ASN-155; ASN-515; ASN-596; ASN-830; ASN-862 ANDASN-931.	12754519 [Abstract]