dbPTM

HG2A_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	HG2A_HUMAN
UniProt AC	P04233
Protein Name	HLA class II histocompatibility antigen gamma chain
Gene Name	CD74
Organism	Homo sapiens (Human).
Sequence Length	296
Subcellular Localization	Cell membrane Single-pass type II membrane protein . Endoplasmic reticulum membrane. Golgi apparatus, trans-Golgi network. Endosome. Lysosome. Transits through a number of intracellular compartments in the endocytic pathway. It can either undergo p
Protein Description	Plays a critical role in MHC class II antigen processing by stabilizing peptide-free class II alpha/beta heterodimers in a complex soon after their synthesis and directing transport of the complex from the endoplasmic reticulum to the endosomal/lysosomal system where the antigen processing and binding of antigenic peptides to MHC class II takes place. Serves as cell surface receptor for the cytokine MIF..
Protein Sequence	MHRRRSRSCREDQKPVMDDQRDLISNNEQLPMLGRRPGAPESKCSRGALYTGFSILVTLLLAGQATTAYFLYQQQGRLDKLTVTSQNLQLENLRMKLPKPPKPVSKMRMATPLLMQALPMGALPQGPMQNATKYGNMTEDHVMHLLQNADPLKVYPPLKGSFPENLRHLKNTMETIDWKVFESWMHHWLLFEMSRHSLEQKPTDAPPKVLTKCQEEVSHIPAVHPGSFRPKCDENGNYLPLQCYGSIGYCWCVFPNGTEVPNTRSRGHHNCSESLELEDPSSGLGVTKQDLGPVPM

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
6	Phosphorylation	--MHRRRSRSCREDQ --CCCCCCCCCCCCC	27.08	28857561
8	Phosphorylation	MHRRRSRSCREDQKP CCCCCCCCCCCCCCC	20.83	23401153
14	Ubiquitination	RSCREDQKPVMDDQR CCCCCCCCCCCCHHH	52.48	-
25	Phosphorylation	DDQRDLISNNEQLPM CHHHHHHHCCCCCCC	40.68	23401153
42	Phosphorylation	RRPGAPESKCSRGAL CCCCCCCCCCCCCHH	37.59	22817900
43	Ubiquitination	RPGAPESKCSRGALY CCCCCCCCCCCCHHH	34.27	21906983
43 (in isoform 1)	Ubiquitination	-	34.27	21890473
43 (in isoform 2)	Ubiquitination	-	34.27	21890473
45	Phosphorylation	GAPESKCSRGALYTG CCCCCCCCCCHHHHH	37.17	22817900
58	Phosphorylation	TGFSILVTLLLAGQA HHHHHHHHHHHHCHH	14.29	22210691
66	O-linked_Glycosylation	LLLAGQATTAYFLYQ HHHHCHHHHHHHHHH	12.22	29351928
69	Phosphorylation	AGQATTAYFLYQQQG HCHHHHHHHHHHCCC	7.63	26074081
72	Phosphorylation	ATTAYFLYQQQGRLD HHHHHHHHHCCCCCC	8.38	26074081
80 (in isoform 2)	Ubiquitination	-	51.12	21890473
80 (in isoform 1)	Ubiquitination	-	51.12	21890473
80	Ubiquitination	QQQGRLDKLTVTSQN HCCCCCCEEEEECCC	51.12	22817900
84	O-linked_Glycosylation	RLDKLTVTSQNLQLE CCCEEEEECCCCEEE	21.25	OGP
96	Methylation	QLENLRMKLPKPPKP EEEHHHHCCCCCCCC	56.02	-
99	Methylation	NLRMKLPKPPKPVSK HHHHCCCCCCCCCCH	81.84	-
111	Phosphorylation	VSKMRMATPLLMQAL CCHHHCHHHHHHHHC	12.72	24043423
130	N-linked_Glycosylation	LPQGPMQNATKYGNM CCCCCCCCCCHHCCC	43.24	7505883
132	Phosphorylation	QGPMQNATKYGNMTE CCCCCCCCHHCCCCH	32.14	24043423
136	N-linked_Glycosylation	QNATKYGNMTEDHVM CCCCHHCCCCHHHHH	30.98	7505883
159 (in isoform 2)	Ubiquitination	-	59.28	21890473
159	Ubiquitination	LKVYPPLKGSFPENL CCCCCCCCCCCCHHH	59.28	21890473
159 (in isoform 1)	Ubiquitination	-	59.28	21890473
170 (in isoform 1)	Ubiquitination	-	44.22	21890473
170 (in isoform 2)	Ubiquitination	-	44.22	21890473
170	Ubiquitination	PENLRHLKNTMETID CHHHHHHHHHHHHCC	44.22	22817900
197	O-linked_Glycosylation	LFEMSRHSLEQKPTD HHHHHHHHHHCCCCC	32.27	55827715
203 (in isoform 2)	Phosphorylation	-	52.40	26714015
203	O-linked_Glycosylation	HSLEQKPTDAPPKVL HHHHCCCCCCCCHHH	52.40	22171320
210 (in isoform 2)	Phosphorylation	-	4.77	26714015
223 (in isoform 2)	O-linked_Glycosylation	-	4.73	OGP
227	Phosphorylation	IPAVHPGSFRPKCDE CCCCCCCCCCCCCCC	23.64	27080861
256	N-linked_Glycosylation	YCWCVFPNGTEVPNT EEEEECCCCCCCCCC	59.56	10022822
272	Phosphorylation	SRGHHNCSESLELED CCCCCCCCCCCCCCC	35.22	26657352
274	Phosphorylation	GHHNCSESLELEDPS CCCCCCCCCCCCCCC	15.73	26657352
281	O-linked_Glycosylation	SLELEDPSSGLGVTK CCCCCCCCCCCCCCH	49.73	23234360
282	O-linked_Glycosylation	LELEDPSSGLGVTKQ CCCCCCCCCCCCCHH	43.34	7505883
287	Phosphorylation	PSSGLGVTKQDLGPV CCCCCCCCHHHCCCC	22.61	-

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
-	K	Ubiquitination	E3 ubiquitin ligase	MARCHF8	Q5T0T0	PMID:22199232

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of HG2A_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 HG2A_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
MIF_HUMAN	MIF	physical	12782713
HG2A_HUMAN	CD74	physical	2391366
A4_HUMAN	APP	physical	21832049
ECHA_HUMAN	HADHA	physical	21988832
COPG1_HUMAN	COPG1	physical	26186194
COPG2_HUMAN	COPG2	physical	26186194
DPB1_HUMAN	HLA-DPB1	physical	26186194
DQA1_HUMAN	HLA-DQA1	physical	25241761
NEF_HV1H2	nef	physical	18596106
COPG1_HUMAN	COPG1	physical	28514442
COPG2_HUMAN	COPG2	physical	28514442
CD44_HUMAN	CD44	physical	27872288

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
D08944	Milatuzumab (USAN)
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of HG2A_HUMAN

Related Literatures of Post-Translational Modification

N-linked Glycosylation
Reference	PubMed
"Crystal structure of MHC class II-associated p41 Ii fragment bound tocathepsin L reveals the structural basis for differentiation betweencathepsins L and S."; Guncar G., Pungercic G., Klemencic I., Turk V., Turk D.; EMBO J. 18:793-803(1999). Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 210-274, GLYCOSYLATION ATASN-256, AND DISULFIDE BONDS.	10022822 [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-136, AND MASSSPECTROMETRY.	19159218 [Abstract]
O-linked Glycosylation
Reference	PubMed
"Human urinary glycoproteomics; attachment site specific analysis ofN-and O-linked glycosylations by CID and ECD."; Halim A., Nilsson J., Ruetschi U., Hesse C., Larson G.; Mol. Cell. Proteomics 0:0-0(2011). Cited for: GLYCOSYLATION AT THR-203, STRUCTURE OF CARBOHYDRATES, AND MASSSPECTROMETRY.	22171320 [Abstract]