dbPTM

RNF32_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	RNF32_HUMAN
UniProt AC	Q9H0A6
Protein Name	RING finger protein 32
Gene Name	RNF32
Organism	Homo sapiens (Human).
Sequence Length	362
Subcellular Localization	Cytoplasm .
Protein Description	May play a role in sperm formation..
Protein Sequence	MLKNKGHSSKKDNLAVNAVALQDHILHDLQLRNLSVADHSKTQVQKKENKSLKRDTKAIIDTGLKKTTQCPKLEDSEKEYVLDPKPPPLTLAQKLGLIGPPPPPLSSDEWEKVKQRSLLQGDSVQPCPICKEEFELRPQVLLSCSHVFHKACLQAFEKFTNKKTCPLCRKNQYQTRVIHDGARLFRIKCVTRIQAYWRGCVVRKWYRNLRKTVPPTDAKLRKKFFEKKFTEISHRILCSYNTNIEELFAEIDQCLAINRSVLQQLEEKCGHEITEEEWEKIQVQALRRETHECSICLAPLSAAGGQRVGAGRRSREMALLSCSHVFHHACLLALEEFSVGDRPPFHACPLCRSCYQKKILEC

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference	Orthologous Protein Cluster
230	Phosphorylation	KFFEKKFTEISHRIL HHHHHHHHHHHHHHH	41.09	27966365

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 RNF32_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of RNF32_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 RNF32_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
A4_HUMAN	APP	physical	21832049
A4_HUMAN	APP	physical	21163940
APOE_HUMAN	APOE	physical	21163940
BLMH_HUMAN	BLMH	physical	21163940
CDK5_HUMAN	CDK5	physical	21163940
ECSIT_HUMAN	ECSIT	physical	21163940
ELAV3_HUMAN	ELAVL3	physical	21163940
EXOS1_HUMAN	EXOSC1	physical	21163940
FXL12_HUMAN	FBXL12	physical	21163940
GCDH_HUMAN	GCDH	physical	21163940
IFIT5_HUMAN	IFIT5	physical	21163940
LONM_HUMAN	LONP1	physical	21163940
OGA_HUMAN	MGEA5	physical	21163940
PRAM_HUMAN	PRAM1	physical	21163940
PRDX2_HUMAN	PRDX2	physical	21163940
RD23A_HUMAN	RAD23A	physical	21163940
STALP_HUMAN	STAMBPL1	physical	21163940
LZTS2_HUMAN	LZTS2	physical	21163940
FBXW4_HUMAN	FBXW4	physical	21163940
CP2C9_HUMAN	CYP2C9	physical	21163940
CEP55_HUMAN	CEP55	physical	21163940
CP2C8_HUMAN	CYP2C8	physical	21163940
EXOC6_HUMAN	EXOC6	physical	21163940
SYFA_HUMAN	FARSA	physical	21163940
IFIT3_HUMAN	IFIT3	physical	21163940
LOXL4_HUMAN	LOXL4	physical	21163940
MAST1_HUMAN	MAST1	physical	21163940
PAXI1_HUMAN	PAXIP1	physical	21163940
PSN1_HUMAN	PSEN1	physical	21163940
RAB3A_HUMAN	RAB3A	physical	21163940
RAB3D_HUMAN	RAB3D	physical	21163940
RNF32_HUMAN	RNF32	physical	21163940
RPP30_HUMAN	RPP30	physical	21163940
MKRN3_HUMAN	MKRN3	physical	22493164
TRI23_HUMAN	TRIM23	physical	22493164

Drug and Disease Associations

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

Regulatory Network of RNF32_HUMAN

Related Literatures of Post-Translational Modification