CR3L1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: CR3L1_HUMAN
• UniProt AC: Q96BA8
• Protein Name: Cyclic AMP-responsive element-binding protein 3-like protein 1
• Gene Name: CREB3L1
• Organism: Homo sapiens (Human).
• Sequence Length: 519
• Subcellular Localization: Endoplasmic reticulum membrane ; Single-pass type II membrane protein. ER membrane resident protein. Upon ER stress, translocated to the Golgi apparatus where it is cleaved. The cytosolic N-terminal fragment (processed cyclic AMP-responsive element-b
• Protein Description: Transcription factor involved in unfolded protein response (UPR). Binds the DNA consensus sequence 5'-GTGXGCXGC-3'. [PubMed: 21767813 In the absence of endoplasmic reticulum (ER) stress, inserted into ER membranes, with N-terminal DNA-binding and transcription activation domains oriented toward the cytosolic face of the membrane. In response to ER stress, transported to the Golgi, where it is cleaved in a site-specific manner by resident proteases S1P/MBTPS1 and S2P/MBTPS2. The released N-terminal cytosolic domain is translocated to the nucleus to effect transcription of specific target genes. Plays a critical role in bone formation through the transcription of COL1A1, and possibly COL1A2, and the secretion of bone matrix proteins. Directly binds to the UPR element (UPRE)-like sequence in an osteoblast-specific COL1A1 promoter region and induces its transcription. Does not regulate COL1A1 in other tissues, such as skin (By similarity Required to protect astrocytes from ER stress-induced cell death. In astrocytes, binds to the cAMP response element (CRE) of the BiP/HSPA5 promoter and participate in its transcriptional activation (By similarity Required for TGFB1 to activate genes involved in the assembly of collagen extracellular matrix]
• Protein Sequence: MDAVLEPFPADRLFPGSSFLDLGDLNESDFLNNAHFPEHLDHFTENMEDFSNDLFSSFFDDPVLDEKSPLLDMELDSPTPGIQAEHSYSLSGDSAPQSPLVPIKMEDTTQDAEHGAWALGHKLCSIMVKQEQSPELPVDPLAAPSAMAAAAAMATTPLLGLSPLSRLPIPHQAPGEMTQLPVIKAEPLEVNQFLKVTPEDLVQMPPTPPSSHGSDSDGSQSPRSLPPSSPVRPMARSSTAISTSPLLTAPHKLQGTSGPLLLTEEEKRTLIAEGYPIPTKLPLTKAEEKALKRVRRKIKNKISAQESRRKKKEYVECLEKKVETFTSENNELWKKVETLENANRTLLQQLQKLQTLVTNKISRPYKMAATQTGTCLMVAALCFVLVLGSLVPCLPEFSSGSQTVKEDPLAADGVYTASQMPSRSLLFYDDGAGLWEDGRSTLLPMEPPDGWEINPGGPAEQRPRDHLQHDHLDSTHETTKYLSEAWPKDGGNGTSPDFSHSKEWFHDRDLGPNTTIKLS

Overview of Protein Modification Sites with Functional and Structural Information

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
79	Phosphorylation	DMELDSPTPGIQAEH CEECCCCCCCCCEEE	37.79	27251275
87	Phosphorylation	PGIQAEHSYSLSGDS CCCCEEEEEECCCCC	14.12	27251275
88	Phosphorylation	GIQAEHSYSLSGDSA CCCEEEEEECCCCCC	18.62	27251275
89	Phosphorylation	IQAEHSYSLSGDSAP CCEEEEEECCCCCCC	21.05	27251275
91	Phosphorylation	AEHSYSLSGDSAPQS EEEEEECCCCCCCCC	34.31	27251275
94	Phosphorylation	SYSLSGDSAPQSPLV EEECCCCCCCCCCCC	45.43	27251275
108	Phosphorylation	VPIKMEDTTQDAEHG CCEEEECCCCCHHHH	17.04	-
109	Phosphorylation	PIKMEDTTQDAEHGA CEEEECCCCCHHHHH	36.45	-
165	Phosphorylation	LLGLSPLSRLPIPHQ CCCCCCHHHCCCCCC	34.84	18669648
184	Sumoylation	MTQLPVIKAEPLEVN CCCCCEEECCCCCCC	47.10	28112733
197	Phosphorylation	VNQFLKVTPEDLVQM CCCCCCCCHHHHCCC	21.26	23312004
207	Phosphorylation	DLVQMPPTPPSSHGS HHCCCCCCCCCCCCC	41.79	23312004
210	Phosphorylation	QMPPTPPSSHGSDSD CCCCCCCCCCCCCCC	35.85	23312004
211	Phosphorylation	MPPTPPSSHGSDSDG CCCCCCCCCCCCCCC	37.33	23312004
214	Phosphorylation	TPPSSHGSDSDGSQS CCCCCCCCCCCCCCC	28.63	23312004
216	Phosphorylation	PSSHGSDSDGSQSPR CCCCCCCCCCCCCCC	45.64	23312004
219	Phosphorylation	HGSDSDGSQSPRSLP CCCCCCCCCCCCCCC	32.26	23312004
221	Phosphorylation	SDSDGSQSPRSLPPS CCCCCCCCCCCCCCC	24.79	23312004
224	Phosphorylation	DGSQSPRSLPPSSPV CCCCCCCCCCCCCCC	48.92	22210691
228	Phosphorylation	SPRSLPPSSPVRPMA CCCCCCCCCCCCCCC	45.38	29759185
229	Phosphorylation	PRSLPPSSPVRPMAR CCCCCCCCCCCCCCC	32.94	22210691
237	Phosphorylation	PVRPMARSSTAISTS CCCCCCCCCCCCCCC	23.62	26699800
238	Phosphorylation	VRPMARSSTAISTSP CCCCCCCCCCCCCCC	19.12	26699800
239	Phosphorylation	RPMARSSTAISTSPL CCCCCCCCCCCCCCC	29.29	26699800
242	Phosphorylation	ARSSTAISTSPLLTA CCCCCCCCCCCCCCC	21.99	22199227
243	Phosphorylation	RSSTAISTSPLLTAP CCCCCCCCCCCCCCC	28.40	26657352
244	Phosphorylation	SSTAISTSPLLTAPH CCCCCCCCCCCCCCC	13.53	22199227
248	Phosphorylation	ISTSPLLTAPHKLQG CCCCCCCCCCCCCCC	45.91	22199227
275	Phosphorylation	RTLIAEGYPIPTKLP HHHHCCCCCCCCCCC	6.90	30631047
284	Phosphorylation	IPTKLPLTKAEEKAL CCCCCCCCHHHHHHH	26.69	-
301	Sumoylation	VRRKIKNKISAQESR HHHHHHHHHCHHHHH	32.79	-
301	Ubiquitination	VRRKIKNKISAQESR HHHHHHHHHCHHHHH	32.79	-
301	Sumoylation	VRRKIKNKISAQESR HHHHHHHHHCHHHHH	32.79	-
370	Phosphorylation	RPYKMAATQTGTCLM CCCCCCCCHHHHHHH	19.68	-
492	N-linked_Glycosylation	AWPKDGGNGTSPDFS HCCCCCCCCCCCCCC	56.98	UniProtKB CARBOHYD
513	N-linked_Glycosylation	HDRDLGPNTTIKLS- CCCCCCCCCEEECC-	48.32	UniProtKB CARBOHYD

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	FBXW7	Q969H0	PMID:24658274

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of CR3L1_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of CR3L1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
CR3L1_HUMAN	CREB3L1	physical	23661758
CR3L3_HUMAN	CREB3L3	physical	23661758
CREB3_HUMAN	CREB3	physical	23661758
ZNT8_HUMAN	SLC30A8	physical	25416956
TM218_HUMAN	TMEM218	physical	25416956
FBXW7_HUMAN	FBXW7	physical	28514442
CR3L2_HUMAN	CREB3L2	physical	28514442
URFB1_HUMAN	UHRF1BP1	physical	28514442
TRRAP_HUMAN	TRRAP	physical	28514442
AP3B1_HUMAN	AP3B1	physical	28514442
UBP22_HUMAN	USP22	physical	28514442

Drug and Disease Associations

• Kegg Drug
• DrugBank
• There are no disease associations of PTM sites.