CR3L2_HUMAN - dbPTM
CR3L2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CR3L2_HUMAN
UniProt AC Q70SY1
Protein Name Cyclic AMP-responsive element-binding protein 3-like protein 2
Gene Name CREB3L2
Organism Homo sapiens (Human).
Sequence Length 520
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). 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 chondrogenesis by activating the transcription of SEC23A, which promotes the transport and secretion of cartilage matrix proteins, and possibly that of ER biogenesis-related genes (By similarity). In a neuroblastoma cell line, protects cells from ER stress-induced death. [PubMed: 17178827 In vitro activates transcription of target genes via direct binding to the CRE site]
Protein Sequence MEVLESGEQGVLQWDRKLSELSEPGDGEALMYHTHFSELLDEFSQNVLGQLLNDPFLSEKSVSMEVEPSPTSPAPLIQAEHSYSLCEEPRAQSPFTHITTSDSFNDDEVESEKWYLSTDFPSTSIKTEPVTDEPPPGLVPSVTLTITAISTPLEKEEPPLEMNTGVDSSCQTIIPKIKLEPHEVDQFLNFSPKEAPVDHLHLPPTPPSSHGSDSEGSLSPNPRLHPFSLPQTHSPSRAAPRAPSALSSSPLLTAPHKLQGSGPLVLTEEEKRTLIAEGYPIPTKLPLSKSEEKALKKIRRKIKNKISAQESRRKKKEYMDSLEKKVESCSTENLELRKKVEVLENTNRTLLQQLQKLQTLVMGKVSRTCKLAGTQTGTCLMVVVLCFAVAFGSFFQGYGPYPSATKMALPSQHSLQEPYTASVVRSRNLLIYEEHSPPEESSSPGSAGELGGWDRGSSLLRVSGLESRPDVDLPHFIISNETSLEKSVLLELQQHLVSAKLEGNETLKVVELDRRVNTTF
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 Orthologous
Protein Cluster
69PhosphorylationVSMEVEPSPTSPAPL
EECEEECCCCCCCCC		27.5728387310
71PhosphorylationMEVEPSPTSPAPLIQ
CEEECCCCCCCCCEE		52.2425159151
72PhosphorylationEVEPSPTSPAPLIQA
EEECCCCCCCCCEEE		23.5825159151
82PhosphorylationPLIQAEHSYSLCEEP
CCEEEEHHCCCCCCC		14.1227732954
83PhosphorylationLIQAEHSYSLCEEPR
CEEEEHHCCCCCCCC		13.9427732954
84PhosphorylationIQAEHSYSLCEEPRA
EEEEHHCCCCCCCCC		29.5627732954
93PhosphorylationCEEPRAQSPFTHITT
CCCCCCCCCCCEEEC		22.4627050516
96PhosphorylationPRAQSPFTHITTSDS
CCCCCCCCEEECCCC		18.7623186163
103PhosphorylationTHITTSDSFNDDEVE
CEEECCCCCCCCCHH		26.2229507054
145PhosphorylationLVPSVTLTITAISTP
CCCEEEEEEEEECCC		13.6022468782
147PhosphorylationPSVTLTITAISTPLE
CEEEEEEEEECCCCC		16.8322468782
151PhosphorylationLTITAISTPLEKEEP
EEEEEECCCCCCCCC		26.2722468782
176UbiquitinationSCQTIIPKIKLEPHE
CCCCCCCCCCCCHHH		41.90-
178SumoylationQTIIPKIKLEPHEVD
CCCCCCCCCCHHHHH		53.58-
178UbiquitinationQTIIPKIKLEPHEVD
CCCCCCCCCCHHHHH		53.58-
178SumoylationQTIIPKIKLEPHEVD
CCCCCCCCCCHHHHH		53.5828112733
191PhosphorylationVDQFLNFSPKEAPVD
HHHHHCCCCCCCCCC		33.7130266825
228PhosphorylationNPRLHPFSLPQTHSP
CCCCCCCCCCCCCCC		43.5223403867
232PhosphorylationHPFSLPQTHSPSRAA
CCCCCCCCCCCCCCC		23.5225159151
234PhosphorylationFSLPQTHSPSRAAPR
CCCCCCCCCCCCCCC		28.1423401153
236PhosphorylationLPQTHSPSRAAPRAP
CCCCCCCCCCCCCCC		37.2523403867
244PhosphorylationRAAPRAPSALSSSPL
CCCCCCCCCCCCCCC		40.6424732914
247PhosphorylationPRAPSALSSSPLLTA
CCCCCCCCCCCCCCC		28.6123401153
248PhosphorylationRAPSALSSSPLLTAP
CCCCCCCCCCCCCCC		36.5021712546
249PhosphorylationAPSALSSSPLLTAPH
CCCCCCCCCCCCCCC		19.0525159151
253PhosphorylationLSSSPLLTAPHKLQG
CCCCCCCCCCCCCCC		45.9124732914
257UbiquitinationPLLTAPHKLQGSGPL
CCCCCCCCCCCCCCE		41.25-
261PhosphorylationAPHKLQGSGPLVLTE
CCCCCCCCCCEEECH		25.03-
267PhosphorylationGSGPLVLTEEEKRTL
CCCCEEECHHHHCEE		33.59-
271UbiquitinationLVLTEEEKRTLIAEG
EEECHHHHCEEEECC		54.70-
273PhosphorylationLTEEEKRTLIAEGYP
ECHHHHCEEEECCCC		33.3226074081
279PhosphorylationRTLIAEGYPIPTKLP
CEEEECCCCCCCCCC		6.9026074081
283PhosphorylationAEGYPIPTKLPLSKS
ECCCCCCCCCCCCHH		46.0326074081
288PhosphorylationIPTKLPLSKSEEKAL
CCCCCCCCHHHHHHH		32.0026074081
289UbiquitinationPTKLPLSKSEEKALK
CCCCCCCHHHHHHHH		70.35-
290PhosphorylationTKLPLSKSEEKALKK
CCCCCCHHHHHHHHH		47.8425159151
305SumoylationIRRKIKNKISAQESR
HHHHHHHHHCHHHHH		32.79-
305UbiquitinationIRRKIKNKISAQESR
HHHHHHHHHCHHHHH		32.79-
305SumoylationIRRKIKNKISAQESR
HHHHHHHHHCHHHHH		32.79-
321PhosphorylationKKKEYMDSLEKKVES
HHHHHHHHHHHHHHH		23.1525954137
325SumoylationYMDSLEKKVESCSTE
HHHHHHHHHHHCCHH		41.69-
325UbiquitinationYMDSLEKKVESCSTE
HHHHHHHHHHHCCHH		41.69-
325SumoylationYMDSLEKKVESCSTE
HHHHHHHHHHHCCHH		41.69-
328PhosphorylationSLEKKVESCSTENLE
HHHHHHHHCCHHCHH		19.1626699800
330PhosphorylationEKKVESCSTENLELR
HHHHHHCCHHCHHHH		48.3026699800
331PhosphorylationKKVESCSTENLELRK
HHHHHCCHHCHHHHH		32.9726699800
338UbiquitinationTENLELRKKVEVLEN
HHCHHHHHHHHHHHH		74.02-
339UbiquitinationENLELRKKVEVLENT
HCHHHHHHHHHHHHH		36.87-
356UbiquitinationTLLQQLQKLQTLVMG
HHHHHHHHHHHHHHH		51.6721906983
356 (in isoform 2)Ubiquitination-51.6721890473
356 (in isoform 1)Ubiquitination-51.6721890473
364 (in isoform 2)Ubiquitination-20.9521890473
364UbiquitinationLQTLVMGKVSRTCKL
HHHHHHHCCCCCHHH		20.9521890473
364 (in isoform 1)Ubiquitination-20.9521890473
364AcetylationLQTLVMGKVSRTCKL
HHHHHHHCCCCCHHH		20.9526051181
368PhosphorylationVMGKVSRTCKLAGTQ
HHHCCCCCHHHCCCC		13.39-
457PhosphorylationLGGWDRGSSLLRVSG
CCCCCCCCCEEEECC		20.7826029660
458PhosphorylationGGWDRGSSLLRVSGL
CCCCCCCCEEEECCC		33.9624719451
480N-linked_GlycosylationLPHFIISNETSLEKS
CCEEEECCCCCHHHH		46.27UniProtKB CARBOHYD
482PhosphorylationHFIISNETSLEKSVL
EEEECCCCCHHHHHH		42.75-
504N-linked_GlycosylationVSAKLEGNETLKVVE
HHCCCCCCCEEEEEE		29.69UniProtKB CARBOHYD
517N-linked_GlycosylationVELDRRVNTTF----
EEEECCCCCCC----		31.43UniProtKB 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
-KUbiquitinationE3 ubiquitin ligaseFBXW7Q969H0
PMID:24658274
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CR3L2_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 CR3L2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PAXI_HUMANPXNphysical
21988832
RGS16_HUMANRGS16physical
21988832
GAS7_HUMANGAS7physical
21988832
GULP1_HUMANGULP1physical
21988832
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 CR3L2_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-191, AND MASSSPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-191, AND MASSSPECTROMETRY.

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