dbPTM

PK1IP_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	PK1IP_HUMAN
UniProt AC	Q9NWT1
Protein Name	p21-activated protein kinase-interacting protein 1
Gene Name	PAK1IP1
Organism	Homo sapiens (Human).
Sequence Length	392
Subcellular Localization	Nucleus, nucleolus .
Protein Description	Negatively regulates the PAK1 kinase. PAK1 is a member of the PAK kinase family, which has been shown to play a positive role in the regulation of signaling pathways involving MAPK8 and RELA. PAK1 exists as an inactive homodimer, which is activated by binding of small GTPases such as CDC42 to an N-terminal regulatory domain. PAK1IP1 also binds to the N-terminus of PAK1, and inhibits the specific activation of PAK1 by CDC42. May be involved in ribosomal large subunit assembly. [PubMed: 24120868]
Protein Sequence	MELVAGCYEQVLFGFAVHPEPEACGDHEQWTLVADFTHHAHTASLSAVAVNSRFVVTGSKDETIHIYDMKKKIEHGALVHHSGTITCLKFYGNRHLISGAEDGLICIWDAKKWECLKSIKAHKGQVTFLSIHPSGKLALSVGTDKTLRTWNLVEGRSAFIKNIKQNAHIVEWSPRGEQYVVIIQNKIDIYQLDTASISGTITNEKRISSVKFLSESVLAVAGDEEVIRFFDCDSLVCLCEFKAHENRVKDMFSFEIPEHHVIVSASSDGFIKMWKLKQDKKVPPSLLCEINTNARLTCLGVWLDKVADMKESLPPAAEPSPVSKEQSKIGKKEPGDTVHKEEKRSKPNTKKRGLTGDSKKATKESGLISTKKRKMVEMLEKKRKKKKIKTMQ

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
60	Acetylation	RFVVTGSKDETIHIY EEEEEECCCCEEEEE	62.01	26051181
70	Acetylation	TIHIYDMKKKIEHGA EEEEEECCCCEECCC	48.28	26822725
89	Acetylation	SGTITCLKFYGNRHL CCCEEEEEEECCEEE	38.39	26051181
111	Acetylation	LICIWDAKKWECLKS EEEEEEHHHHHHHHH	56.82	26051181
117	Acetylation	AKKWECLKSIKAHKG HHHHHHHHHHHCCCC	62.89	26051181
118	Phosphorylation	KKWECLKSIKAHKGQ HHHHHHHHHHCCCCE	19.17	22817900
127	Phosphorylation	KAHKGQVTFLSIHPS HCCCCEEEEEEECCC	15.80	22817900
130	Phosphorylation	KGQVTFLSIHPSGKL CCEEEEEEECCCCCE	18.05	22817900
134	Phosphorylation	TFLSIHPSGKLALSV EEEEECCCCCEEEEE	34.10	28188228
145	Acetylation	ALSVGTDKTLRTWNL EEEEECCCCCEEEEE	49.66	26051181
145	Ubiquitination	ALSVGTDKTLRTWNL EEEEECCCCCEEEEE	49.66	-
161	Ubiquitination	EGRSAFIKNIKQNAH CCHHHHHHHHHHCEE	46.28	-
161	Acetylation	EGRSAFIKNIKQNAH CCHHHHHHHHHHCEE	46.28	26051181
164	Ubiquitination	SAFIKNIKQNAHIVE HHHHHHHHHCEEEEE	47.06	-
164	Acetylation	SAFIKNIKQNAHIVE HHHHHHHHHCEEEEE	47.06	25953088
173	Phosphorylation	NAHIVEWSPRGEQYV CEEEEEECCCCCEEE	7.39	24719451
179	Phosphorylation	WSPRGEQYVVIIQNK ECCCCCEEEEEEECC	7.74	-
214	Phosphorylation	ISSVKFLSESVLAVA CEEEEECCHHHHHHH	30.84	-
242	Acetylation	LVCLCEFKAHENRVK EEEEEEEECCCCCCE	26.92	26051181
312	Phosphorylation	KVADMKESLPPAAEP HHHHHHHHCCCCCCC	40.43	23663014
320	Phosphorylation	LPPAAEPSPVSKEQS CCCCCCCCCCCHHHH	29.46	29255136
323	Phosphorylation	AAEPSPVSKEQSKIG CCCCCCCCHHHHCCC	33.58	30266825
324	Acetylation	AEPSPVSKEQSKIGK CCCCCCCHHHHCCCC	61.07	26051181
327	Phosphorylation	SPVSKEQSKIGKKEP CCCCHHHHCCCCCCC	27.60	24732914
337	Phosphorylation	GKKEPGDTVHKEEKR CCCCCCCCCCHHHHC	30.35	-
363	Ubiquitination	GDSKKATKESGLIST CCHHHCHHHCCCCCH	55.53	-
365	Phosphorylation	SKKATKESGLISTKK HHHCHHHCCCCCHHH	40.22	19691289
369	Phosphorylation	TKESGLISTKKRKMV HHHCCCCCHHHHHHH	38.94	19691289
370	Phosphorylation	KESGLISTKKRKMVE HHCCCCCHHHHHHHH	33.32	19691289
371	Acetylation	ESGLISTKKRKMVEM HCCCCCHHHHHHHHH	43.73	25953088
372	Acetylation	SGLISTKKRKMVEML CCCCCHHHHHHHHHH	58.29	71135
381	Acetylation	KMVEMLEKKRKKKKI HHHHHHHHHHHHHHC	54.65	71139

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 PK1IP_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of PK1IP_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 PK1IP_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
PAK1_HUMAN	PAK1	physical	11371639
MDM2_HUMAN	MDM2	physical	21097889

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 PK1IP_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach."; Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.; Anal. Chem. 81:4493-4501(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-320 AND SER-323, ANDMASS SPECTROMETRY.	19413330 [Abstract]
"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-320, AND MASSSPECTROMETRY.	18669648 [Abstract]
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis."; Wang B., Malik R., Nigg E.A., Korner R.; Anal. Chem. 80:9526-9533(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-320, AND MASSSPECTROMETRY.	19007248 [Abstract]
"Large-scale characterization of HeLa cell nuclear phosphoproteins."; Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-320, AND MASSSPECTROMETRY.	15302935 [Abstract]