ZSC29_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: ZSC29_HUMAN
• UniProt AC: Q8IWY8
• Protein Name: Zinc finger and SCAN domain-containing protein 29
• Gene Name: ZSCAN29
• Organism: Homo sapiens (Human).
• Sequence Length: 852
• Subcellular Localization: Nucleus .
• Protein Description: May be involved in transcriptional regulation..
• Protein Sequence: MMAKSALRENGTNSETFRQRFRRFHYQEVAGPREAFSQLWELCCRWLRPEVRTKEQIVELLVLEQFLTVLPGEIQNWVQEQCPENGEEAVTLVEDLEREPGRPRSSVTVSVKGQEVRLEKMTPPKSSQELLSVRQESVEPQPRGVPKKERARSPDLGPQEQMNPKEKLKPFQRSGLPFPKSGVVSRLEQGEPWIPDLLGSKEKELPSGSHIGDRRVHADLLPSKKDRRSWVEQDHWSFEDEKVAGVHWGYEETRTLLAILSQTEFYEALRNCHRNSQVYGAVAERLREYGFLRTLEQCRTKFKGLQKSYRKVKSGHPPETCPFFEEMEALMSAQVIALPSNGLEAAASHSGLVGSDAETEEPGQRGWQHEEGAEEAVAQESDSDDMDLEATPQDPNSAAPVVFRSPGGVHWGYEETKTYLAILSETQFYEALRNCHRNSQLYGAVAERLWEYGFLRTPEQCRTKFKSLQTSYRKVKNGQAPETCPFFEEMDALVSVRVAAPPNDGQEETASCPVQGTSEAEAQKQAEEADEATEEDSDDDEEDTEIPPGAVITRAPVLFQSPRGFEAGFENEDNSKRDISEEVQLHRTLLARSERKIPRYLHQGKGNESDCRSGRQWAKTSGEKRGKLTLPEKSLSEVLSQQRPCLGERPYKYLKYSKSFGPNSLLMHQVSHQVENPYKCADCGKSFSRSARLIRHRRIHTGEKPYKCLDCGKSFRDSSNFITHRRIHTGEKPYQCGECGKCFNQSSSLIIHQRTHTGEKPYQCEECGKSFNNSSHFSAHRRIHTGERPHVCPDCGKSFSKSSDLRAHHRTHTGEKPYGCHDCGKCFSKSSALNKHGEIHAREKLLTQSAPK

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
112	Sumoylation	SSVTVSVKGQEVRLE CCEEEEECCEEEEEE	47.58	28112733
122	Phosphorylation	EVRLEKMTPPKSSQE EEEEEECCCCCCHHH	47.72	21712546
126	Phosphorylation	EKMTPPKSSQELLSV EECCCCCCHHHHHHH	42.92	23186163
127	Phosphorylation	KMTPPKSSQELLSVR ECCCCCCHHHHHHHH	33.52	23186163
132	Phosphorylation	KSSQELLSVRQESVE CCHHHHHHHHHHHCC	28.07	28450419
137	Phosphorylation	LLSVRQESVEPQPRG HHHHHHHHCCCCCCC	24.36	21815630
153	Phosphorylation	PKKERARSPDLGPQE CHHHHCCCCCCCHHH	23.06	30266825
169	Ubiquitination	MNPKEKLKPFQRSGL CCHHHHCCCCHHCCC	55.65	-
180	Sumoylation	RSGLPFPKSGVVSRL HCCCCCCCCCCHHHH	61.29	-
180	Acetylation	RSGLPFPKSGVVSRL HCCCCCCCCCCHHHH	61.29	20167786
180	Sumoylation	RSGLPFPKSGVVSRL HCCCCCCCCCCHHHH	61.29	28112733
201	Ubiquitination	IPDLLGSKEKELPSG CHHHHCCCCCCCCCC	71.63	-
223	Phosphorylation	VHADLLPSKKDRRSW CCHHCCCCHHHHCHH	52.92	24719451
237	Phosphorylation	WVEQDHWSFEDEKVA HHHCCCCCCCCCCCC	18.48	28348404
355	Phosphorylation	SHSGLVGSDAETEEP HHCCCCCCCCCCCCC	26.60	-
405	Phosphorylation	AAPVVFRSPGGVHWG CCCEEEECCCCCCCC	19.21	28985074
439	Phosphorylation	LRNCHRNSQLYGAVA HHHCCHHCHHHHHHH	22.86	28555341
466	Ubiquitination	EQCRTKFKSLQTSYR HHHHHHHHHHHHHHH	52.38	-
483	Phosphorylation	KNGQAPETCPFFEEM HCCCCCCCCCCHHHH	25.15	29759185
495	Phosphorylation	EEMDALVSVRVAAPP HHHCEEEEEEEECCC	12.69	24719451
561	Phosphorylation	RAPVLFQSPRGFEAG CCCEEECCCCCCCCC	14.83	25159151
576	Sumoylation	FENEDNSKRDISEEV CCCCCCCCCCHHHHH	61.41	28112733
605	Ubiquitination	PRYLHQGKGNESDCR CCCHHCCCCCHHHCC	52.58	-
620	Phosphorylation	SGRQWAKTSGEKRGK CCCCHHHHCCCCCCE	33.93	23403867
621	Phosphorylation	GRQWAKTSGEKRGKL CCCHHHHCCCCCCEE	44.22	23403867
652	Sumoylation	CLGERPYKYLKYSKS CCCCCCCHHHHCCHH	46.95	28112733
688	Phosphorylation	ADCGKSFSRSARLIR CCCCCCCCHHHHHHH	32.20	17081983
701	Phosphorylation	IRHRRIHTGEKPYKC HHHCCCCCCCCCEEE	44.67	29496963
706	Phosphorylation	IHTGEKPYKCLDCGK CCCCCCCEEEECCCC	25.96	-
718	Phosphorylation	CGKSFRDSSNFITHR CCCCCCCCCCCEECC	23.95	28555341
723	Phosphorylation	RDSSNFITHRRIHTG CCCCCCEECCEEECC	12.75	22210691
729	Phosphorylation	ITHRRIHTGEKPYQC EECCEEECCCCCEEC	44.67	28111955
746	Phosphorylation	CGKCFNQSSSLIIHQ CHHHCCCCCCEEEEE	24.01	23186163
747	Phosphorylation	GKCFNQSSSLIIHQR HHHCCCCCCEEEEEC	21.28	23186163
748	Phosphorylation	KCFNQSSSLIIHQRT HHCCCCCCEEEEECC	28.91	25106551
755	Phosphorylation	SLIIHQRTHTGEKPY CEEEEECCCCCCCCE	19.74	-
757	Phosphorylation	IIHQRTHTGEKPYQC EEEECCCCCCCCEEC	46.56	-
760	Acetylation	QRTHTGEKPYQCEEC ECCCCCCCCEECCCC	50.82	7428837
770	Phosphorylation	QCEECGKSFNNSSHF ECCCCCCCCCCCCCC	20.63	28555341
774	Phosphorylation	CGKSFNNSSHFSAHR CCCCCCCCCCCCCCC	26.71	28555341
785	Phosphorylation	SAHRRIHTGERPHVC CCCCCCCCCCCCCCC	38.06	28674419
798	Phosphorylation	VCPDCGKSFSKSSDL CCCCCCCCCCCCCCC	21.75	24719451
811	Phosphorylation	DLRAHHRTHTGEKPY CCHHHCCCCCCCCCC	21.31	-
813	Phosphorylation	RAHHRTHTGEKPYGC HHHCCCCCCCCCCCC	46.56	-
847	Phosphorylation	HAREKLLTQSAPK-- HHHHHHHHCCCCC--	30.80	30206219
849	Phosphorylation	REKLLTQSAPK---- HHHHHHCCCCC----	41.10	30206219

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

Oops, there are no upstream regulatory protein records of ZSC29_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of ZSC29_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 ZSC29_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
FTM_HUMAN	RPGRIP1L	physical	28514442
EHD2_HUMAN	EHD2	physical	28514442
LRP2_HUMAN	LRP2	physical	28514442
MD2BP_HUMAN	MAD2L1BP	physical	28514442
DFNA5_HUMAN	DFNA5	physical	28514442
GABT_HUMAN	ABAT	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

"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-561, AND MASSSPECTROMETRY.
PubMed: 18669648