dbPTM

CR3L3_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	CR3L3_HUMAN
UniProt AC	Q68CJ9
Protein Name	Cyclic AMP-responsive element-binding protein 3-like protein 3
Gene Name	CREB3L3
Organism	Homo sapiens (Human).
Sequence Length	461
Subcellular Localization	Endoplasmic reticulum membrane Single-pass type II membrane protein . Processed cyclic AMP-responsive element-binding protein 3-like protein 3: Nucleus. Under ER stress the cleaved N-terminal cytoplasmic domain translocates into the nucleus.
Protein Description	Transcription factor that may act during endoplasmic reticulum stress by activating unfolded protein response target genes. Activated in response to cAMP stimulation. In vitro, binds to the cAMP response element (CRE) and box-B element. Activates transcription through box-B element. Activates transcription through CRE (By similarity). Seems to function synergistically with ATF6. In acute inflammatory response, may activate expression of acute phase response (APR) genes. May be involved in growth suppression..
Protein Sequence	MNTDLAAGKMASAACSMDPIDSFELLDLLFDRQDGILRHVELGEGWGHVKDQQVLPNPDSDDFLSSILGSGDSLPSSPLWSPEGSDSGISEDLPSDPQDTPPRSGPATSPAGCHPAQPGKGPCLSYHPGNSCSTTTPGPVIQVPEASVTIDLEMWSPGGRICAEKPADPVDLSPRCNLTVKDLLLSGSSGDLQQHHLGASYLLRPGAGHCQELVLTEDEKKLLAKEGITLPTQLPLTKYEERVLKKIRRKIRNKQSAQESRKKKKEYIDGLETRMSACTAQNQELQRKVLHLEKQNLSLLEQLKKLQAIVVQSTSKSAQTGTCVAVLLLSFALIILPSISPFGPNKTESPGDFAPVRVFSRTLHNDAASRVAADAVPGSEAPGPRPEADTTREESPGSPGADWGFQDTANLTNSTEELDNATLVLRNATEGLGQVALLDWVAPGPSTGSGRAGLEAAGDEL

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
109	Phosphorylation	PRSGPATSPAGCHPA CCCCCCCCCCCCCCC	18.17	24275569
173	Phosphorylation	PADPVDLSPRCNLTV CCCCCCCCCCCCCCH	13.06	22171320
200	Phosphorylation	QQHHLGASYLLRPGA HHHHCCCCEEECCCC	17.95	24719451
223	Ubiquitination	TEDEKKLLAKEGITL CHHHHHHHHHCCCCC	9.81	-
225	Ubiquitination	DEKKLLAKEGITLPT HHHHHHHHCCCCCCC	57.34	-
229	Phosphorylation	LLAKEGITLPTQLPL HHHHCCCCCCCCCCC	37.23	-
256	Phosphorylation	RKIRNKQSAQESRKK HHHHCHHHHHHHHHH	33.26	17924679
260	Phosphorylation	NKQSAQESRKKKKEY CHHHHHHHHHHHHHH	37.00	17924679
267	Phosphorylation	SRKKKKEYIDGLETR HHHHHHHHHHHHHHH	17.12	-
273	Phosphorylation	EYIDGLETRMSACTA HHHHHHHHHHHHHHH	36.39	-
276	Phosphorylation	DGLETRMSACTAQNQ HHHHHHHHHHHHHHH	19.53	-
294	Acetylation	RKVLHLEKQNLSLLE HHHHHHHHHCHHHHH	51.34	30587873
347	O-linked_Glycosylation	SPFGPNKTESPGDFA CCCCCCCCCCCCCCC	48.62	OGP
347	Phosphorylation	SPFGPNKTESPGDFA CCCCCCCCCCCCCCC	48.62	23879269
379	Phosphorylation	AADAVPGSEAPGPRP HHHCCCCCCCCCCCC	25.23	29759185
379	O-linked_Glycosylation	AADAVPGSEAPGPRP HHHCCCCCCCCCCCC	25.23	22171320
410	N-linked_Glycosylation	WGFQDTANLTNSTEE CCCCCCCCCCCCHHH	49.87	UniProtKB CARBOHYD
413	N-linked_Glycosylation	QDTANLTNSTEELDN CCCCCCCCCHHHHHH	50.53	20356926
420	N-linked_Glycosylation	NSTEELDNATLVLRN CCHHHHHHCEEEECC	47.66	20356926
427	N-linked_Glycosylation	NATLVLRNATEGLGQ HCEEEECCCCCCCCE	47.23	20356926
449	Phosphorylation	APGPSTGSGRAGLEA CCCCCCCCCCHHHHH	25.79	29759185

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 CR3L3_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
294	K	ubiquitylation		30389664
Ubiquitinated at Lys-294 by SYNV1/HRD1 via 'Lys-27'-linked ubiquitin.

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 CR3L3_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
ZHANG_HUMAN	CREBZF	physical	21994947
CR3L1_HUMAN	CREB3L1	physical	23661758
CR3L3_HUMAN	CREB3L3	physical	23661758
CREB3_HUMAN	CREB3	physical	23661758
IMA1_HUMAN	KPNA2	physical	21988832
RIOK3_HUMAN	RIOK3	physical	21988832
KHDR1_HUMAN	KHDRBS1	physical	21988832
PELI2_HUMAN	PELI2	physical	21988832
PRGC1_HUMAN	PPARGC1A	physical	21994947
FBW1A_HUMAN	BTRC	physical	26108621
FBW1A_HUMAN	BTRC	physical	27029215
CUL1_HUMAN	CUL1	physical	27029215
RBX1_HUMAN	RBX1	physical	27029215

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 CR3L3_HUMAN

Related Literatures of Post-Translational Modification

N-linked Glycosylation
Reference	PubMed
"N-linked glycosylation is required for optimal proteolytic activationof membrane-bound transcription factor CREB-H."; Chan C.P., Mak T.Y., Chin K.T., Ng I.O., Jin D.Y.; J. Cell Sci. 123:1438-1448(2010). Cited for: GLYCOSYLATION AT ASN-413; ASN-420 AND ASN-427.	20356926 [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 SER-379, STRUCTURE OF CARBOHYDRATES, AND MASSSPECTROMETRY.	22171320 [Abstract]
Phosphorylation
Reference	PubMed
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."; Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.; J. Proteome Res. 6:4150-4162(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-256 AND SER-260, ANDMASS SPECTROMETRY.	17924679 [Abstract]

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