TRI22_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: TRI22_HUMAN
• UniProt AC: Q8IYM9
• Protein Name: E3 ubiquitin-protein ligase TRIM22
• Gene Name: TRIM22
• Organism: Homo sapiens (Human).
• Sequence Length: 498
• Subcellular Localization: Cytoplasm . Nucleus . Nucleus speckle. Nucleus, Cajal body. Localizes predominantly to the nucleus, found in cytoplasm to some extent. Forms distinct nuclear bodies that undergo dynamic changes during cell cycle progression. Nuclear bodies start to f
• Protein Description: Interferon-induced antiviral protein involved in cell innate immunity. The antiviral activity could in part be mediated by TRIM22-dependent ubiquitination of viral proteins. Plays a role in restricting the replication of HIV-1, encephalomyocarditis virus (EMCV) and hepatitis B virus (HBV). Acts as a transcriptional repressor of HBV core promoter. May have E3 ubiquitin-protein ligase activity..
• Protein Sequence: MDFSVKVDIEKEVTCPICLELLTEPLSLDCGHSFCQACITAKIKESVIISRGESSCPVCQTRFQPGNLRPNRHLANIVERVKEVKMSPQEGQKRDVCEHHGKKLQIFCKEDGKVICWVCELSQEHQGHQTFRINEVVKECQEKLQVALQRLIKEDQEAEKLEDDIRQERTAWKNYIQIERQKILKGFNEMRVILDNEEQRELQKLEEGEVNVLDNLAAATDQLVQQRQDASTLISDLQRRLRGSSVEMLQDVIDVMKRSESWTLKKPKSVSKKLKSVFRVPDLSGMLQVLKELTDVQYYWVDVMLNPGSATSNVAISVDQRQVKTVRTCTFKNSNPCDFSAFGVFGCQYFSSGKYYWEVDVSGKIAWILGVHSKISSLNKRKSSGFAFDPSVNYSKVYSRYRPQYGYWVIGLQNTCEYNAFEDSSSSDPKVLTLFMAVPPCRIGVFLDYEAGIVSFFNVTNHGALIYKFSGCRFSRPAYPYFNPWNCLVPMTVCPPSS

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
44	Ubiquitination	ACITAKIKESVIISR HHHHHEECCCEEEEC	43.14	-
46	Phosphorylation	ITAKIKESVIISRGE HHHEECCCEEEECCC	17.39	23403867
55	Phosphorylation	IISRGESSCPVCQTR EEECCCCCCCCCCCC	20.38	-
87	Phosphorylation	RVKEVKMSPQEGQKR HHHHHCCCCCCCCCC	20.08	23401153
173 (in isoform 1)	Ubiquitination	-	37.09	21890473
173	Ubiquitination	RQERTAWKNYIQIER HHHHHHHHHHHHHHH	37.09	21890473
182	Ubiquitination	YIQIERQKILKGFNE HHHHHHHHHHCCCCE	57.11	-
185	Ubiquitination	IERQKILKGFNEMRV HHHHHHHCCCCEEEE	66.00	-
204	Ubiquitination	EEQRELQKLEEGEVN HHHHHHHHHHCCCCC	71.18	-
261	Phosphorylation	DVMKRSESWTLKKPK HHHHHCCCCCCCCCC	26.97	28555341
325	Phosphorylation	VDQRQVKTVRTCTFK EEHHHEEEEEEEEEC	19.16	22817900
373	Phosphorylation	AWILGVHSKISSLNK EEEEEHHHHHHHCCC	29.31	-
376	Phosphorylation	LGVHSKISSLNKRKS EEHHHHHHHCCCCCC	32.29	27794612
377	Phosphorylation	GVHSKISSLNKRKSS EHHHHHHHCCCCCCC	39.16	23403867
380	Ubiquitination	SKISSLNKRKSSGFA HHHHHCCCCCCCCCC	67.50	-
382	Ubiquitination	ISSLNKRKSSGFAFD HHHCCCCCCCCCCCC	51.05	-
383	Phosphorylation	SSLNKRKSSGFAFDP HHCCCCCCCCCCCCC	39.46	23401153
384	Phosphorylation	SLNKRKSSGFAFDPS HCCCCCCCCCCCCCC	40.75	30266825
391	Phosphorylation	SGFAFDPSVNYSKVY CCCCCCCCCCHHHHH	25.49	23403867
392 (in isoform 2)	Ubiquitination	-	10.69	21890473
394	Phosphorylation	AFDPSVNYSKVYSRY CCCCCCCHHHHHHCC	14.02	23403867
396	Ubiquitination	DPSVNYSKVYSRYRP CCCCCHHHHHHCCCC	34.53	21890473
396 (in isoform 1)	Ubiquitination	-	34.53	21890473
405	Phosphorylation	YSRYRPQYGYWVIGL HHCCCCCCCEEEEEE	18.18	24043423
407	Phosphorylation	RYRPQYGYWVIGLQN CCCCCCCEEEEEEEC	7.49	24043423
415	Phosphorylation	WVIGLQNTCEYNAFE EEEEEECEEEEECCC	8.18	24043423
418	Phosphorylation	GLQNTCEYNAFEDSS EEECEEEEECCCCCC	17.59	24043423
424	Phosphorylation	EYNAFEDSSSSDPKV EEECCCCCCCCCCCC	25.56	24043423
425	Phosphorylation	YNAFEDSSSSDPKVL EECCCCCCCCCCCCE	46.30	24043423
426	Phosphorylation	NAFEDSSSSDPKVLT ECCCCCCCCCCCCEE	42.59	24043423
427	Phosphorylation	AFEDSSSSDPKVLTL CCCCCCCCCCCCEEE	60.94	24043423

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	TRIM22	Q8IYM9	PMID:18656448

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of TRI22_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 TRI22_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
ZZZ3_HUMAN	ZZZ3	physical	20211142
TRI22_HUMAN	TRIM22	physical	17156811
TAB2_HUMAN	TAB2	physical	23818111
IF4E_HUMAN	EIF4E	physical	22509910
IKKA_HUMAN	CHUK	physical	25510414
C2TA_HUMAN	CIITA	physical	28555140
PML_HUMAN	PML	physical	28555140
CCNT1_HUMAN	CCNT1	physical	28555140

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.