CRERF_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: CRERF_HUMAN
• UniProt AC: Q8IUR6
• Protein Name: CREB3 regulatory factor
• Gene Name: CREBRF
• Organism: Homo sapiens (Human).
• Sequence Length: 639
• Subcellular Localization: Nucleus . Colocalizes with CREB3 in nuclear foci.
• Protein Description: Acts as a negative regulator of the endoplasmic reticulum stress response or unfolded protein response (UPR). Represses the transcriptional activity of CREB3 during the UPR. Recruits CREB3 into nuclear foci..
• Protein Sequence: MPQPSVSGMDPPFGDAFRSHTFSEQTLMSTDLLANSSDPDFMYELDREMNYQQNPRDNFLSLEDCKDIENLESFTDVLDNEGALTSNWEQWDTYCEDLTKYTKLTSCDIWGTKEVDYLGLDDFSSPYQDEEVISKTPTLAQLNSEDSQSVSDSLYYPDSLFSVKQNPLPSSFPGKKITSRAAAPVCSSKTLQAEVPLSDCVQKASKPTSSTQIMVKTNMYHNEKVNFHVECKDYVKKAKVKINPVQQSRPLLSQIHTDAAKENTCYCGAVAKRQEKKGMEPLQGHATPALPFKETQELLLSPLPQEGPGSLAAGESSSLSASTSVSDSSQKKEEHNYSLFVSDNLGEQPTKCSPEEDEEDEEDVDDEDHDEGFGSEHELSENEEEEEEEEDYEDDKDDDISDTFSEPGYENDSVEDLKEVTSISSRKRGKRRYFWEYSEQLTPSQQERMLRPSEWNRDTLPSNMYQKNGLHHGKYAVKKSRRTDVEDLTPNPKKLLQIGNELRKLNKVISDLTPVSELPLTARPRSRKEKNKLASRACRLKKKAQYEANKVKLWGLNTEYDNLLFVINSIKQEIVNRVQNPRDERGPNMGQKLEILIKDTLGLPVAGQTSEFVNQVLEKTAEGNPTGGLVGLRIPTSKV

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
5	Phosphorylation	---MPQPSVSGMDPP ---CCCCCCCCCCCC	24.54	29083192
7	Phosphorylation	-MPQPSVSGMDPPFG -CCCCCCCCCCCCCH	32.51	29083192
102	Phosphorylation	CEDLTKYTKLTSCDI HHHHHHHCCCCCCCC	22.57	-
112	Phosphorylation	TSCDIWGTKEVDYLG CCCCCCCCCEEEECC	14.72	-
125	Phosphorylation	LGLDDFSSPYQDEEV CCCCCCCCCCCCHHH	27.85	-
134	Phosphorylation	YQDEEVISKTPTLAQ CCCHHHHHCCCCHHH	35.34	26074081
136	Phosphorylation	DEEVISKTPTLAQLN CHHHHHCCCCHHHCC	18.08	26074081
138	Phosphorylation	EVISKTPTLAQLNSE HHHHCCCCHHHCCCC	39.70	26074081
144	Phosphorylation	PTLAQLNSEDSQSVS CCHHHCCCCCCCCCC	51.91	26074081
147	Phosphorylation	AQLNSEDSQSVSDSL HHCCCCCCCCCCHHC	21.94	26657352
149	Phosphorylation	LNSEDSQSVSDSLYY CCCCCCCCCCHHCCC	27.78	26074081
151	Phosphorylation	SEDSQSVSDSLYYPD CCCCCCCCHHCCCCC	27.08	26074081
153	Phosphorylation	DSQSVSDSLYYPDSL CCCCCCHHCCCCCHH	15.68	26074081
155	Phosphorylation	QSVSDSLYYPDSLFS CCCCHHCCCCCHHCC	19.53	26074081
156	Phosphorylation	SVSDSLYYPDSLFSV CCCHHCCCCCHHCCC	13.07	26074081
175	Acetylation	LPSSFPGKKITSRAA CCCCCCCCCCCCCCC	41.04	25953088
287	Phosphorylation	EPLQGHATPALPFKE CCCCCCCCCCCCCHH	11.92	25159151
329	Phosphorylation	STSVSDSSQKKEEHN CCCCCCCCCCHHHCC	51.51	-
353	Phosphorylation	GEQPTKCSPEEDEED CCCCCCCCCCCCCCC	36.58	-
375	Phosphorylation	DHDEGFGSEHELSEN CCCCCCCCHHCCCCC	33.25	-
380	Phosphorylation	FGSEHELSENEEEEE CCCHHCCCCCHHHHH	35.08	-
421	Phosphorylation	VEDLKEVTSISSRKR HHHHHHHHCCCCCCC	22.79	-
422	Phosphorylation	EDLKEVTSISSRKRG HHHHHHHCCCCCCCC	26.16	-
424	Phosphorylation	LKEVTSISSRKRGKR HHHHHCCCCCCCCCC	24.69	-
425	Phosphorylation	KEVTSISSRKRGKRR HHHHCCCCCCCCCCC	39.90	-
444	Phosphorylation	YSEQLTPSQQERMLR CHHCCCHHHHHHHCC	38.98	17525332
513	Phosphorylation	NKVISDLTPVSELPL HHHHHCCCCHHHCCC	27.00	27251275
636	O-linked_Glycosylation	LVGLRIPTSKV---- EEEEECCCCCC----	38.52	29351928
637	O-linked_Glycosylation	VGLRIPTSKV----- EEEECCCCCC-----	26.52	29351928

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of CRERF_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of CRERF_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 CRERF_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
ATF1_HUMAN	ATF1	physical	28514442

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.

Related Literatures of Post-Translational Modification

Phosphorylation

"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage.";
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
Science 316:1160-1166(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-444, AND MASSSPECTROMETRY.
PubMed: 17525332