dbPTM

CD33_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	CD33_HUMAN
UniProt AC	P20138
Protein Name	Myeloid cell surface antigen CD33
Gene Name	CD33
Organism	Homo sapiens (Human).
Sequence Length	364
Subcellular Localization	Cell membrane Single-pass type I membrane protein.
Protein Description	Putative adhesion molecule of myelomonocytic-derived cells that mediates sialic-acid dependent binding to cells. Preferentially binds to alpha-2,6-linked sialic acid. The sialic acid recognition site may be masked by cis interactions with sialic acids on the same cell surface. In the immune response, may act as an inhibitory receptor upon ligand induced tyrosine phosphorylation by recruiting cytoplasmic phosphatase(s) via their SH2 domain(s) that block signal transduction through dephosphorylation of signaling molecules. Induces apoptosis in acute myeloid leukemia (in vitro)..
Protein Sequence	MPLLLLLPLLWAGALAMDPNFWLQVQESVTVQEGLCVLVPCTFFHPIPYYDKNSPVHGYWFREGAIISRDSPVATNKLDQEVQEETQGRFRLLGDPSRNNCSLSIVDARRRDNGSYFFRMERGSTKYSYKSPQLSVHVTDLTHRPKILIPGTLEPGHSKNLTCSVSWACEQGTPPIFSWLSAAPTSLGPRTTHSSVLIITPRPQDHGTNLTCQVKFAGAGVTTERTIQLNVTYVPQNPTTGIFPGDGSGKQETRAGVVHGAIGGAGVTALLALCLCLIFFIVKTHRRKAARTAVGRNDTHPTTGSASPKHQKKSKLHGPTETSSCSGAAPTVEMDEELHYASLNFHGMNPSKDTSTEYSEVRTQ

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
71	Phosphorylation	GAIISRDSPVATNKL CEEEECCCCCCCCCC	21.84	26657352
77	Ubiquitination	DSPVATNKLDQEVQE CCCCCCCCCCHHHHH	49.43	21906983
100	N-linked_Glycosylation	LGDPSRNNCSLSIVD CCCCCCCCCEEEEEE	18.68	8702538
100	N-linked_Glycosylation	LGDPSRNNCSLSIVD CCCCCCCCCEEEEEE	18.68	8702538
113	N-linked_Glycosylation	VDARRRDNGSYFFRM EECCCCCCCCEEEEE	39.23	UniProtKB CARBOHYD
160	N-linked_Glycosylation	LEPGHSKNLTCSVSW CCCCCCCCCEEEEEE	43.53	UniProtKB CARBOHYD
209	N-linked_Glycosylation	RPQDHGTNLTCQVKF CCCCCCCCEEEEEEE	37.63	UniProtKB CARBOHYD
226	Phosphorylation	AGVTTERTIQLNVTY CCCCEEEEEEEEEEE	13.57	-
230	N-linked_Glycosylation	TERTIQLNVTYVPQN EEEEEEEEEEECCCC	14.01	UniProtKB CARBOHYD
239	Phosphorylation	TYVPQNPTTGIFPGD EECCCCCCCCCCCCC	45.24	-
239	O-linked_Glycosylation	TYVPQNPTTGIFPGD EECCCCCCCCCCCCC	45.24	OGP
240	O-linked_Glycosylation	YVPQNPTTGIFPGDG ECCCCCCCCCCCCCC	29.54	OGP
248	Phosphorylation	GIFPGDGSGKQETRA CCCCCCCCCCCCCCC	47.78	-
250	Ubiquitination	FPGDGSGKQETRAGV CCCCCCCCCCCCCEE	46.81	21906983
299	Phosphorylation	TAVGRNDTHPTTGSA HHCCCCCCCCCCCCC	33.05	28450419
302	Phosphorylation	GRNDTHPTTGSASPK CCCCCCCCCCCCCHH	35.86	22115753
303	Phosphorylation	RNDTHPTTGSASPKH CCCCCCCCCCCCHHH	33.32	28450419
305	Phosphorylation	DTHPTTGSASPKHQK CCCCCCCCCCHHHCC	24.39	28450419
305 (in isoform 2)	Phosphorylation	-	24.39	28450419
307	Phosphorylation	HPTTGSASPKHQKKS CCCCCCCCHHHCCCC	35.86	23401153
307 (in isoform 2)	Phosphorylation	-	35.86	28450419
326	Phosphorylation	PTETSSCSGAAPTVE CCCCCCCCCCCCEEE	33.15	24247654
340	Dephosphorylation	EMDEELHYASLNFHG ECCCCCEEEEEEECC	15.54	10206955
340	Phosphorylation	EMDEELHYASLNFHG ECCCCCEEEEEEECC	15.54	10206955
358	Phosphorylation	SKDTSTEYSEVRTQ- CCCCCCCCCCCCCC-	15.37	25587033
359	Phosphorylation	KDTSTEYSEVRTQ-- CCCCCCCCCCCCC--	24.31	23532336
363	Phosphorylation	TEYSEVRTQ------ CCCCCCCCC------	43.75	28450419

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
340	Y	Phosphorylation	Kinase	LCK	P06239	Uniprot
340	Y	Phosphorylation	Kinase	SRC	P12931	GPS
340	Y	Phosphorylation	Kinase	SRC64	-	PhosphoELM
358	Y	Phosphorylation	Kinase	LCK	P06239	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
100	N	Glycosylation		8702538
Glycosylation at Asn-100 is critical for regulating ligand recognition.

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 CD33_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
PTN11_HUMAN	PTPN11	physical	10206955
PTN6_HUMAN	PTPN6	physical	10206955
HERC3_HUMAN	HERC3	physical	21988832
K1H1_HUMAN	KRT31	physical	25416956
K1C40_HUMAN	KRT40	physical	25416956
S39AB_HUMAN	SLC39A11	physical	26186194
PEX19_HUMAN	PEX19	physical	26186194
COMD3_HUMAN	COMMD3	physical	26186194
SAAL1_HUMAN	SAAL1	physical	26186194
PEX19_HUMAN	PEX19	physical	28514442
S39AB_HUMAN	SLC39A11	physical	28514442
COMD3_HUMAN	COMMD3	physical	28514442

Drug and Disease Associations

Kegg Disease
H00003	Acute myeloid leukemia (AML)
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
D03259	Gemtuzumab ozogamicin (genetical recombination) (JAN); Gemtuzumab ozogamicin (USAN); Gemtuzumab (INN
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of CD33_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"The myeloid-specific sialic acid-binding receptor, CD33, associateswith the protein-tyrosine phosphatases, SHP-1 and SHP-2."; Taylor V.C., Buckley C.D., Douglas M., Cody A.J., Simmons D.L.,Freeman S.D.; J. Biol. Chem. 274:11505-11512(1999). Cited for: PHOSPHORYLATION AT TYR-340 AND TYR-358, INTERACTION WITH PTPN6 ANDPTPN11, AND MUTAGENESIS OF TYR-340.	10206955 [Abstract]
"The sialoadhesin CD33 is a myeloid-specific inhibitory receptor."; Ulyanova T., Blasioli J., Woodford-Thomas T.A., Thomas M.L.; Eur. J. Immunol. 29:3440-3449(1999). Cited for: FUNCTION, PHOSPHORYLATION AT TYR-340 AND TYR-358, MUTAGENESIS OFTYR-358, AND INTERACTION WITH PTPN6.	10556798 [Abstract]

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