dbPTM

HBB_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	HBB_HUMAN
UniProt AC	P68871
Protein Name	Hemoglobin subunit beta
Gene Name	HBB
Organism	Homo sapiens (Human).
Sequence Length	147
Subcellular Localization
Protein Description	Involved in oxygen transport from the lung to the various peripheral tissues.; LVV-hemorphin-7 potentiates the activity of bradykinin, causing a decrease in blood pressure.; Spinorphin: functions as an endogenous inhibitor of enkephalin-degrading enzymes such as DPP3, and as a selective antagonist of the P2RX3 receptor which is involved in pain signaling, these properties implicate it as a regulator of pain and inflammation..
Protein Sequence	MVHLTPEEKSAVTALWGKVNVDEVGGEALGRLLVVYPWTQRFFESFGDLSTPDAVMGNPKVKAHGKKVLGAFSDGLAHLDNLKGTFATLSELHCDKLHVDPENFRLLGNVLVCVLAHHFGKEFTPPVQAAYQKVVAGVANALAHKYH

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	N-pyruvate 2-iminyl-valine	------MVHLTPEEK ------CCCCCHHHH	5.21	-
2	Acetylation	------MVHLTPEEK ------CCCCCHHHH	5.21	-
2	Other	------MVHLTPEEK ------CCCCCHHHH	5.21	-
2	N-linked_Glycosylation	------MVHLTPEEK ------CCCCCHHHH	5.21	635569
5	Phosphorylation	---MVHLTPEEKSAV ---CCCCCHHHHHHH	17.49	23025827
9	N-linked_Glycosylation	VHLTPEEKSAVTALW CCCCHHHHHHHHHHH	41.89	7358733
9	Glycation	VHLTPEEKSAVTALW CCCCHHHHHHHHHHH	41.89	-
9	Acetylation	VHLTPEEKSAVTALW CCCCHHHHHHHHHHH	41.89	7666987
10	Phosphorylation	HLTPEEKSAVTALWG CCCHHHHHHHHHHHC	31.11	25072903
13	Phosphorylation	PEEKSAVTALWGKVN HHHHHHHHHHHCCCC	18.75	24702127
18	Acetylation	AVTALWGKVNVDEVG HHHHHHCCCCHHHCC	21.03	20167786
18	N-linked_Glycosylation	AVTALWGKVNVDEVG HHHHHHCCCCHHHCC	21.03	7358733
18	Glycation	AVTALWGKVNVDEVG HHHHHHCCCCHHHCC	21.03	-
36	Phosphorylation	LGRLLVVYPWTQRFF HHHHEEHHHHHHHHH	5.88	21082442
36	Nitration	LGRLLVVYPWTQRFF HHHHEEHHHHHHHHH	5.88	-
39	Phosphorylation	LLVVYPWTQRFFESF HEEHHHHHHHHHHHH	12.83	28857561
45	O-linked_Glycosylation	WTQRFFESFGDLSTP HHHHHHHHHCCCCCC	29.40	OGP
45	Phosphorylation	WTQRFFESFGDLSTP HHHHHHHHHCCCCCC	29.40	24972180
50	O-linked_Glycosylation	FESFGDLSTPDAVMG HHHHCCCCCCCHHCC	42.51	20166139
50	Phosphorylation	FESFGDLSTPDAVMG HHHHCCCCCCCHHCC	42.51	23025827
51	Phosphorylation	ESFGDLSTPDAVMGN HHHCCCCCCCHHCCC	32.27	23025827
56	Sulfoxidation	LSTPDAVMGNPKVKA CCCCCHHCCCHHHCC	4.62	21192028
60	Acetylation	DAVMGNPKVKAHGKK CHHCCCHHHCCCCCE	61.44	4531009
62	Acetylation	VMGNPKVKAHGKKVL HCCCHHHCCCCCEEE	40.57	7675277
66	Acetylation	PKVKAHGKKVLGAFS HHHCCCCCEEEHHHH	29.82	30583883
67	N-linked_Glycosylation	KVKAHGKKVLGAFSD HHCCCCCEEEHHHHH	47.48	7358733
67	Glycation	KVKAHGKKVLGAFSD HHCCCCCEEEHHHHH	47.48	-
73	Phosphorylation	KKVLGAFSDGLAHLD CEEEHHHHHHHHHHH	30.18	23025827
73	O-linked_Glycosylation	KKVLGAFSDGLAHLD CEEEHHHHHHHHHHH	30.18	20166139
83	Acetylation	LAHLDNLKGTFATLS HHHHHHCCCHHHHHH	63.26	4531009
85	Phosphorylation	HLDNLKGTFATLSEL HHHHCCCHHHHHHHH	14.44	23312004
85	O-linked_Glycosylation	HLDNLKGTFATLSEL HHHHCCCHHHHHHHH	14.44	12556445
88	Phosphorylation	NLKGTFATLSELHCD HCCCHHHHHHHHCCC	26.99	26657352
90	Phosphorylation	KGTFATLSELHCDKL CCHHHHHHHHCCCCC	33.48	23025827
94	S-nitrosylation	ATLSELHCDKLHVDP HHHHHHCCCCCCCCH	8.46	9843411
94	Glutathionylation	ATLSELHCDKLHVDP HHHHHHCCCCCCCCH	8.46	16051210
94	S-nitrosocysteine	ATLSELHCDKLHVDP HHHHHHCCCCCCCCH	8.46	-
94	Methylation	ATLSELHCDKLHVDP HHHHHHCCCCCCCCH	8.46	-
96	Acetylation	LSELHCDKLHVDPEN HHHHCCCCCCCCHHH	45.98	25038526
113	S-nitrosylation	LLGNVLVCVLAHHFG HHHHHHHHHHHHHHC	1.49	25040305
121	Glycation	VLAHHFGKEFTPPVQ HHHHHHCCCCCHHHH	49.03	-
121	N-linked_Glycosylation	VLAHHFGKEFTPPVQ HHHHHHCCCCCHHHH	49.03	7358733
121	Acetylation	VLAHHFGKEFTPPVQ HHHHHHCCCCCHHHH	49.03	7669925
124	Phosphorylation	HHFGKEFTPPVQAAY HHHCCCCCHHHHHHH	27.98	23911959
131	Nitration	TPPVQAAYQKVVAGV CHHHHHHHHHHHHHH	16.34	-
131	Phosphorylation	TPPVQAAYQKVVAGV CHHHHHHHHHHHHHH	16.34	21253578
133	Acetylation	PVQAAYQKVVAGVAN HHHHHHHHHHHHHHH	26.46	7684877
145	N-linked_Glycosylation	VANALAHKYH----- HHHHHHHCCC-----	39.14	7358733
145	Glycation	VANALAHKYH----- HHHHHHHCCC-----	39.14	-
145	Acetylation	VANALAHKYH----- HHHHHHHCCC-----	39.14	4531009
146	Nitration	ANALAHKYH------ HHHHHHCCC------	11.68	-
146	Phosphorylation	ANALAHKYH------ HHHHHHCCC------	11.68	28857561

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 HBB_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
60	K	Acetylation	4531009
Acetylated on Lys-60, Lys-83 and Lys-145 upon aspirin exposure.
83	K	Acetylation	4531009
Acetylated on Lys-60, Lys-83 and Lys-145 upon aspirin exposure.
145	K	Acetylation	4531009
Acetylated on Lys-60, Lys-83 and Lys-145 upon aspirin exposure.

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
2	N-linked Glycosylation	7 (5)	E ⇒ V;K	rs334;rs33930165	Urinary albumin-to-creatinine ratio Hematocrit Mean corpuscular hemoglobin concentration Mean corpuscular volume Severe malaria	27650483 28453575 29381699
5	Phosphorylation	7 (2)	E ⇒ V;K	rs334;rs33930165	Urinary albumin-to-creatinine ratio Hematocrit Mean corpuscular hemoglobin concentration Mean corpuscular volume Severe malaria	27650483 28453575 29381699
9	Acetylation	7 (2)	E ⇒ V;K	rs334;rs33930165	Urinary albumin-to-creatinine ratio Hematocrit Mean corpuscular hemoglobin concentration Mean corpuscular volume Severe malaria	27650483 28453575 29381699
10	Phosphorylation	7 (3)	E ⇒ V;K	rs334;rs33930165	Urinary albumin-to-creatinine ratio Hematocrit Mean corpuscular hemoglobin concentration Mean corpuscular volume Severe malaria	27650483 28453575 29381699
13	Phosphorylation	7 (6)	E ⇒ V;K	rs334;rs33930165	Urinary albumin-to-creatinine ratio Hematocrit Mean corpuscular hemoglobin concentration Mean corpuscular volume Severe malaria	27650483 28453575 29381699

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
SELT_HUMAN	SELT	physical	16169070
HBA_HUMAN	HBA1	physical	6644819

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
140700	Heinz body anemias (HEIBAN)
613985	Beta-thalassemia (B-THAL)
603903	Sickle cell anemia (SKCA)
603902	Beta-thalassemia, dominant, inclusion body type (B-THALIB)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
DB00893	Iron Dextran

Regulatory Network of HBB_HUMAN

Related Literatures of Post-Translational Modification

N-linked Glycosylation
Reference	PubMed
"Sites of nonenzymatic glycosylation of human hemoglobin A."; Shapiro R., McManus M.J., Zalut C., Bunn H.F.; J. Biol. Chem. 255:3120-3127(1980). Cited for: GLYCATION AT LYS-9; LYS-18; LYS-67; LYS-121 AND LYS-145, AND LACK OFGLYCATION AT LYS-60; LYS-83 AND LYS-96.	7358733 [Abstract]
"The glycosylation of hemoglobin: relevance to diabetes mellitus."; Bunn H.F., Gabbay K.H., Gallop P.M.; Science 200:21-27(1978). Cited for: GLYCATION AT VAL-2.	635569 [Abstract]
Phosphorylation
Reference	PubMed
"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-131, AND MASSSPECTROMETRY.	18083107 [Abstract]
S-nitrosylation
Reference	PubMed
"Crystal structure of the S-nitroso form of liganded humanhemoglobin."; Chan N.L., Rogers P.H., Arnone A.; Biochemistry 37:16459-16464(1998). Cited for: S-NITROSYLATION AT CYS-94.	9843411 [Abstract]
"S-nitrosohaemoglobin: a dynamic activity of blood involved invascular control."; Jia L., Bonaventura C., Bonaventura J., Stamler J.S.; Nature 380:221-226(1996). Cited for: S-NITROSYLATION AT CYS-94.	8637569 [Abstract]

show

show

show