CRIP1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: CRIP1_HUMAN
• UniProt AC: P50238
• Protein Name: Cysteine-rich protein 1
• Gene Name: CRIP1
• Organism: Homo sapiens (Human).
• Sequence Length: 77
• Protein Description: Seems to have a role in zinc absorption and may function as an intracellular zinc transport protein..
• Protein Sequence: MPKCPKCNKEVYFAERVTSLGKDWHRPCLKCEKCGKTLTSGGHAEHEGKPYCNHPCYAAMFGPKGFGRGGAESHTFK

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
9	Acetylation	PKCPKCNKEVYFAER CCCCCCCCEEEEHHH	59.01	19608861
9	Ubiquitination	PKCPKCNKEVYFAER CCCCCCCCEEEEHHH	59.01	33845483
12	Phosphorylation	PKCNKEVYFAERVTS CCCCCEEEEHHHHHH	9.73	27273156
18	Phosphorylation	VYFAERVTSLGKDWH EEEHHHHHHCCCCCC	25.18	27251275
19	Phosphorylation	YFAERVTSLGKDWHR EEHHHHHHCCCCCCC	32.06	27080861
22	Ubiquitination	ERVTSLGKDWHRPCL HHHHHCCCCCCCCCC	64.04	29967540
22	Acetylation	ERVTSLGKDWHRPCL HHHHHCCCCCCCCCC	64.04	25825284
30	Acetylation	DWHRPCLKCEKCGKT CCCCCCCCCCCCCCE	47.25	25953088
36	Ubiquitination	LKCEKCGKTLTSGGH CCCCCCCCEECCCCC	50.24	33845483
37	Phosphorylation	KCEKCGKTLTSGGHA CCCCCCCEECCCCCC	22.13	28355574
39	Phosphorylation	EKCGKTLTSGGHAEH CCCCCEECCCCCCCC	30.47	23312004
40	Phosphorylation	KCGKTLTSGGHAEHE CCCCEECCCCCCCCC	45.98	25159151
49	Ubiquitination	GHAEHEGKPYCNHPC CCCCCCCCCCCCCCC	29.81	29967540
49	Acetylation	GHAEHEGKPYCNHPC CCCCCCCCCCCCCCC	29.81	26051181
51	Phosphorylation	AEHEGKPYCNHPCYA CCCCCCCCCCCCCEE	14.90	-
57	Phosphorylation	PYCNHPCYAAMFGPK CCCCCCCEEHHHCCC	11.22	27259358
64	"N6,N6-dimethyllysine"	YAAMFGPKGFGRGGA EEHHHCCCCCCCCCC	68.22	-
64	Ubiquitination	YAAMFGPKGFGRGGA EEHHHCCCCCCCCCC	68.22	33845483
64	Acetylation	YAAMFGPKGFGRGGA EEHHHCCCCCCCCCC	68.22	26051181
64	Methylation	YAAMFGPKGFGRGGA EEHHHCCCCCCCCCC	68.22	24129315
68	Dimethylation	FGPKGFGRGGAESHT HCCCCCCCCCCCCCC	37.80	-
68	Methylation	FGPKGFGRGGAESHT HCCCCCCCCCCCCCC	37.80	-
73	Phosphorylation	FGRGGAESHTFK--- CCCCCCCCCCCC---	27.56	24719451
75	Phosphorylation	RGGAESHTFK----- CCCCCCCCCC-----	42.26	24719451
77	Acetylation	GAESHTFK------- CCCCCCCC-------	61.66	129719
77	Ubiquitination	GAESHTFK------- CCCCCCCC-------	61.66	24816145

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

Oops, there are no upstream regulatory protein records of CRIP1_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of CRIP1_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 CRIP1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
GASP1_HUMAN	GPRASP1	physical	16169070
HAP1_HUMAN	HAP1	physical	16169070
SH3G3_HUMAN	SH3GL3	physical	16169070
PUR8_HUMAN	ADSL	physical	26344197
KAD2_HUMAN	AK2	physical	26344197
ATOX1_HUMAN	ATOX1	physical	26344197
COF1_HUMAN	CFL1	physical	26344197
COF2_HUMAN	CFL2	physical	26344197
KCRU_HUMAN	CKMT1B	physical	26344197
ACBP_HUMAN	DBI	physical	26344197
DEST_HUMAN	DSTN	physical	26344197
FUBP1_HUMAN	FUBP1	physical	26344197
AATC_HUMAN	GOT1	physical	26344197
ROA1_HUMAN	HNRNPA1	physical	26344197
ROA3_HUMAN	HNRNPA3	physical	26344197
LEG1_HUMAN	LGALS1	physical	26344197
LEG3_HUMAN	LGALS3	physical	26344197
MIF_HUMAN	MIF	physical	26344197
MSI2H_HUMAN	MSI2	physical	26344197
NDKA_HUMAN	NME1	physical	26344197
PIMT_HUMAN	PCMT1	physical	26344197
PGK1_HUMAN	PGK1	physical	26344197
PPIA_HUMAN	PPIA	physical	26344197
SNX3_HUMAN	SNX3	physical	26344197
UFC1_HUMAN	UFC1	physical	26344197
KITH_HUMAN	TK1	physical	28514442
2A5E_HUMAN	PPP2R5E	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

Acetylation

"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-9, AND MASS SPECTROMETRY.
PubMed: 19608861