dbPTM

CEAM1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	CEAM1_HUMAN
UniProt AC	P13688
Protein Name	Carcinoembryonic antigen-related cell adhesion molecule 1 {ECO:0000303\|Ref.8}
Gene Name	CEACAM1 {ECO:0000312\|HGNC:HGNC:1814}
Organism	Homo sapiens (Human).
Sequence Length	526
Subcellular Localization	Isoform 1: Cell membrane Single-pass type I membrane protein . Lateral cell membrane . Apical cell membrane . Basal cell membrane . Cell junction . Cell junction, adherens junction . Canalicular domain of hepatocyte plasma membranes. Found as a mix
Protein Description	Isoform 1: Cell adhesion protein that mediates homophilic cell adhesion in a calcium-independent manner (By similarity). Plays a role as coinhibitory receptor in immune response, insulin action and functions also as an activator during angiogenesis. [PubMed: 18424730]
Protein Sequence	MGHLSAPLHRVRVPWQGLLLTASLLTFWNPPTTAQLTTESMPFNVAEGKEVLLLVHNLPQQLFGYSWYKGERVDGNRQIVGYAIGTQQATPGPANSGRETIYPNASLLIQNVTQNDTGFYTLQVIKSDLVNEEATGQFHVYPELPKPSISSNNSNPVEDKDAVAFTCEPETQDTTYLWWINNQSLPVSPRLQLSNGNRTLTLLSVTRNDTGPYECEIQNPVSANRSDPVTLNVTYGPDTPTISPSDTYYRPGANLSLSCYAASNPPAQYSWLINGTFQQSTQELFIPNITVNNSGSYTCHANNSVTGCNRTTVKTIIVTELSPVVAKPQIKASKTTVTGDKDSVNLTCSTNDTGISIRWFFKNQSLPSSERMKLSQGNTTLSINPVKREDAGTYWCEVFNPISKNQSDPIMLNVNYNALPQENGLSPGAIAGIVIGVVALVALIAVALACFLHFGKTGRASDQRDLTEHKPSVSNHTQDHSNDPPNKMNEVTYSTLNFEAQQPTQPTSASPSLTATEIIYSEVKKQ

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
35	Pyrrolidone_carboxylic_acid	WNPPTTAQLTTESMP CCCCCCCCCCCCCCC	36.93	-
35	Pyrrolidone_carboxylic_acid	WNPPTTAQLTTESMP CCCCCCCCCCCCCCC	36.93	2457922
35	Pyrrolidone_carboxylic_acid	WNPPTTAQLTTESMP CCCCCCCCCCCCCCC	36.93	2457922
90	O-linked_Glycosylation	AIGTQQATPGPANSG EEECCCCCCCCCCCC	25.17	OGP
104	N-linked_Glycosylation	GRETIYPNASLLIQN CCCEECCCCEEEEEE	25.78	16335952
106	O-linked_Glycosylation	ETIYPNASLLIQNVT CEECCCCEEEEEECC	30.28	29351928
111	N-linked_Glycosylation	NASLLIQNVTQNDTG CCEEEEEECCCCCCC	31.63	16335952
115	N-linked_Glycosylation	LIQNVTQNDTGFYTL EEEECCCCCCCEEEE	39.17	2341397
152	N-linked_Glycosylation	PKPSISSNNSNPVED CCCCCCCCCCCCCCC	49.51	2341397
182	N-linked_Glycosylation	TYLWWINNQSLPVSP EEEEEECCCCCCCCC	24.55	UniProtKB CARBOHYD
197	N-linked_Glycosylation	RLQLSNGNRTLTLLS CEECCCCCEEEEEEE	37.70	UniProtKB CARBOHYD
208	N-linked_Glycosylation	TLLSVTRNDTGPYEC EEEEEECCCCCCEEE	41.66	19159218
224	N-linked_Glycosylation	IQNPVSANRSDPVTL EECCCCCCCCCCEEE	36.16	19159218
232	N-linked_Glycosylation	RSDPVTLNVTYGPDT CCCCEEEEEEECCCC	18.08	UniProtKB CARBOHYD
254	N-linked_Glycosylation	TYYRPGANLSLSCYA CCCCCCCCEEEEEEE	35.76	UniProtKB CARBOHYD
274	N-linked_Glycosylation	AQYSWLINGTFQQST HHEEEEECCEECCCC	41.08	UniProtKB CARBOHYD
288	N-linked_Glycosylation	TQELFIPNITVNNSG CEEEECCCEEECCCC	37.43	UniProtKB CARBOHYD
292	N-linked_Glycosylation	FIPNITVNNSGSYTC ECCCEEECCCCCEEE	28.44	UniProtKB CARBOHYD
302	N-linked_Glycosylation	GSYTCHANNSVTGCN CCEEEECCCCCCCCC	20.04	UniProtKB CARBOHYD
309	N-linked_Glycosylation	NNSVTGCNRTTVKTI CCCCCCCCCCEEEEE	45.75	UniProtKB CARBOHYD
344 (in isoform 9)	Phosphorylation	-	11.04	-
345	N-linked_Glycosylation	TGDKDSVNLTCSTND ECCCCEEEEEEECCC	33.32	UniProtKB CARBOHYD
351	N-linked_Glycosylation	VNLTCSTNDTGISIR EEEEEECCCCCEEEE	28.66	UniProtKB CARBOHYD
361 (in isoform 11)	Phosphorylation	-	6.04	-
363	N-linked_Glycosylation	SIRWFFKNQSLPSSE EEEEEEECCCCCCHH	31.36	19159218
363 (in isoform 11)	Phosphorylation	-	31.36	-
378	N-linked_Glycosylation	RMKLSQGNTTLSINP CEEECCCCCEEEECC	23.42	19159218
392 (in isoform 9)	Phosphorylation	-	31.49	-
394 (in isoform 9)	Phosphorylation	-	13.72	-
405	N-linked_Glycosylation	VFNPISKNQSDPIML ECCCCCCCCCCCEEE	39.54	19159218
457	Phosphorylation	CFLHFGKTGRASDQR HHHHHHCCCCCCCCC	32.07	19146852
457 (in isoform 8)	Phosphorylation	-	32.07	-
459 (in isoform 8)	Phosphorylation	-	35.83	-
461	Phosphorylation	FGKTGRASDQRDLTE HHCCCCCCCCCCCCC	32.68	19146852
472	Phosphorylation	DLTEHKPSVSNHTQD CCCCCCCCCCCCCCC	42.87	26657352
474	Phosphorylation	TEHKPSVSNHTQDHS CCCCCCCCCCCCCCC	27.51	28857561
477	Phosphorylation	KPSVSNHTQDHSNDP CCCCCCCCCCCCCCC	39.69	26422651
481	Phosphorylation	SNHTQDHSNDPPNKM CCCCCCCCCCCCCCC	51.74	29507054
492	Phosphorylation	PNKMNEVTYSTLNFE CCCCCEEEEEEECEE	12.94	17192268
493	Phosphorylation	NKMNEVTYSTLNFEA CCCCEEEEEEECEEE	12.58	11278391
494	Phosphorylation	KMNEVTYSTLNFEAQ CCCEEEEEEECEEEC	19.63	17192268
508	Phosphorylation	QQPTQPTSASPSLTA CCCCCCCCCCCCCCH	33.17	11313949
510	Phosphorylation	PTQPTSASPSLTATE CCCCCCCCCCCCHHH	18.13	24275569
520	Phosphorylation	LTATEIIYSEVKKQ- CCHHHHHHHHHHCC-	12.39	8018919
521	Phosphorylation	TATEIIYSEVKKQ-- CHHHHHHHHHHCC--	26.04	-

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
457	T	Phosphorylation	Kinase	CAMK2D	Q13557	PSP
459	S	Phosphorylation	Kinase	CAMK2D	Q13557	PSP
493	Y	Phosphorylation	Kinase	EGFR	P00533	Uniprot
493	Y	Phosphorylation	Kinase	INSR	P06213	Uniprot
493	Y	Phosphorylation	Kinase	LCK	P06239	Uniprot
493	Y	Phosphorylation	Kinase	SRC	P12931	Uniprot
520	Y	Phosphorylation	Kinase	INSR	P06213	Uniprot
520	Y	Phosphorylation	Kinase	LCK	P06239	Uniprot
520	Y	Phosphorylation	Kinase	SRC	P12931	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
508	S	Phosphorylation	7478590
Phosphorylated at Ser-508; mediates activity.
508	S	Phosphorylation	7478590
Phosphorylated at Tyr-493 by EGFR and INSR upon stimulation; this phosphorylation is Ser-508-phosphorylation-dependent; mediates cellular internalization; increases interaction with downstream proteins like SHC1 and FASN (By similarity).

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 CEAM1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
ANXA2_HUMAN	ANXA2	physical	14522961
CEAM8_HUMAN	CEACAM8	physical	11994468
PTN11_HUMAN	PTPN11	physical	9867848
PAXI_HUMAN	PXN	physical	11035932
CEAM6_HUMAN	CEACAM6	physical	21982860
CEAM1_HUMAN	CEACAM1	physical	21982860
CART_HUMAN	CARTPT	physical	21982860
CEAM8_HUMAN	CEACAM8	physical	21982860
CEAM7_HUMAN	CEACAM7	physical	21982860
CEAM5_HUMAN	CEACAM5	physical	21982860

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
D02977	Arcitumomab (USAN/INN); Cea-Scan (TN)
D06028	Technetium Tc 99m arcitumomab (USP)
D06350	Yttrium Y 90 labetuzumab (USAN); CES-Cide (TN)
D06351	Yttrium Y 90 labetuzumab tetraxetan (USAN)
D08936	Labetuzumab (INN/USAN)
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of CEAM1_HUMAN

Related Literatures of Post-Translational Modification

N-linked Glycosylation
Reference	PubMed
"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-152; ASN-208; ASN-224;ASN-363; ASN-378 AND ASN-405, AND MASS SPECTROMETRY.	19159218 [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-104 AND ASN-111, AND MASSSPECTROMETRY.	16335952 [Abstract]

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