dbPTM

CAND2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	CAND2_HUMAN
UniProt AC	O75155
Protein Name	Cullin-associated NEDD8-dissociated protein 2
Gene Name	CAND2
Organism	Homo sapiens (Human).
Sequence Length	1236
Subcellular Localization	Nucleus.
Protein Description	Probable assembly factor of SCF (SKP1-CUL1-F-box protein) E3 ubiquitin ligase complexes that promotes the exchange of the substrate-recognition F-box subunit in SCF complexes, thereby playing a key role in the cellular repertoire of SCF complexes..
Protein Sequence	MSTAAFHISSLLEKMTSSDKDFRFMATSDLMSELQKDSIQLDEDSERKVVKMLLRLLEDKNGEVQNLAVKCLGPLVVKVKEYQVETIVDTLCTNMRSDKEQLRDIAGIGLKTVLSELPPAATGSGLATNVCRKITGQLTSAIAQQEDVAVQLEALDILSDMLSRLGVPLGAFHASLLHCLLPQLSSPRLAVRKRAVGALGHLAAACSTDLFVELADHLLDRLPGPRVPTSPTAIRTLIQCLGSVGRQAGHRLGAHLDRLVPLVEDFCNLDDDELRESCLQAFEAFLRKCPKEMGPHVPNVTSLCLQYIKHDPNYNYDSDEDEEQMETEDSEFSEQESEDEYSDDDDMSWKVRRAAAKCIAALISSRPDLLPDFHCTLAPVLIRRFKEREENVKADVFTAYIVLLRQTQPPKGWLEAMEEPTQTGSNLHMLRGQVPLVVKALQRQLKDRSVRARQGCFSLLTELAGVLPGSLAEHMPVLVSGIIFSLADRSSSSTIRMDALAFLQGLLGTEPAEAFHPHLPILLPPVMACVADSFYKIAAEALVVLQELVRALWPLHRPRMLDPEPYVGEMSAVTLARLRATDLDQEVKERAISCMGHLVGHLGDRLGDDLEPTLLLLLDRLRNEITRLPAIKALTLVAVSPLQLDLQPILAEALHILASFLRKNQRALRLATLAALDALAQSQGLSLPPSAVQAVLAELPALVNESDMHVAQLAVDFLATVTQAQPASLVEVSGPVLSELLRLLRSPLLPAGVLAAAEGFLQALVGTRPPCVDYAKLISLLTAPVYEQAVDGGPGLHKQVFHSLARCVAALSAACPQEAASTASRLVCDARSPHSSTGVKVLAFLSLAEVGQVAGPGHQRELKAVLLEALGSPSEDVRAAASYALGRVGAGSLPDFLPFLLEQIEAEPRRQYLLLHSLREALGAAQPDSLKPYAEDIWALLFQRCEGAEEGTRGVVAECIGKLVLVNPSFLLPRLRKQLAAGRPHTRSTVITAVKFLISDQPHPIDPLLKSFIGEFMESLQDPDLNVRRATLAFFNSAVHNKPSLVRDLLDDILPLLYQETKIRRDLIREVEMGPFKHTVDDGLDVRKAAFECMYSLLESCLGQLDICEFLNHVEDGLKDHYDIRMLTFIMVARLATLCPAPVLQRVDRLIEPLRATCTAKVKAGSVKQEFEKQDELKRSAMRAVAALLTIPEVGKSPIMADFSSQIRSNPELAALFESIQKDSASAPSTDSMELS

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MSTAAFHIS ------CCHHHHHHH	37.75	-
10	Phosphorylation	TAAFHISSLLEKMTS HHHHHHHHHHHHHCC	36.05	24719451
16	Phosphorylation	SSLLEKMTSSDKDFR HHHHHHHCCCCCCHH	35.83	20071362
17	Phosphorylation	SLLEKMTSSDKDFRF HHHHHHCCCCCCHHH	32.80	24719451
20	Acetylation	EKMTSSDKDFRFMAT HHHCCCCCCHHHHHH	61.79	27452117
20	Neddylation	EKMTSSDKDFRFMAT HHHCCCCCCHHHHHH	61.79	32015554
20	Ubiquitination	EKMTSSDKDFRFMAT HHHCCCCCCHHHHHH	61.79	21890473
60	Acetylation	LLRLLEDKNGEVQNL HHHHHHCCCCCHHHH	58.43	25953088
60 (in isoform 2)	Ubiquitination	-	58.43	21906983
60 (in isoform 1)	Ubiquitination	-	58.43	21906983
60	Ubiquitination	LLRLLEDKNGEVQNL HHHHHHCCCCCHHHH	58.43	32015554
99	Ubiquitination	CTNMRSDKEQLRDIA HHCCCCCHHHHHHHH	48.91	29967540
122	Phosphorylation	SELPPAATGSGLATN HHCCCCCCCCCHHHH	33.71	-
124	Phosphorylation	LPPAATGSGLATNVC CCCCCCCCCHHHHHH	26.69	-
128	Phosphorylation	ATGSGLATNVCRKIT CCCCCHHHHHHHHHH	32.97	-
175	Phosphorylation	PLGAFHASLLHCLLP CHHHHHHHHHHHHHH	23.93	-
185	Phosphorylation	HCLLPQLSSPRLAVR HHHHHHCCCCHHHHH	32.80	17081983
186	Phosphorylation	CLLPQLSSPRLAVRK HHHHHCCCCHHHHHH	23.72	17081983
229	Phosphorylation	LPGPRVPTSPTAIRT CCCCCCCCCHHHHHH	44.47	19664995
230	Phosphorylation	PGPRVPTSPTAIRTL CCCCCCCCHHHHHHH	17.74	26437602
232	Phosphorylation	PRVPTSPTAIRTLIQ CCCCCCHHHHHHHHH	34.19	30001349
318	Phosphorylation	DPNYNYDSDEDEEQM CCCCCCCCCCCHHHH	32.32	24275569
333	Phosphorylation	ETEDSEFSEQESEDE HHCCCCCCCCCCCCC	34.03	-
337	Phosphorylation	SEFSEQESEDEYSDD CCCCCCCCCCCCCCC	50.47	-
341	Phosphorylation	EQESEDEYSDDDDMS CCCCCCCCCCCCCHH	29.71	-
342	Phosphorylation	QESEDEYSDDDDMSW CCCCCCCCCCCCHHH	32.30	-
365	Phosphorylation	CIAALISSRPDLLPD HHHHHHHCCCCCCCC	40.62	-
407	Phosphorylation	YIVLLRQTQPPKGWL HHHHHHCCCCCCCHH	36.29	-
495	Ubiquitination	DRSSSSTIRMDALAF CCCCCCCHHHHHHHH	3.57	30230243
581	Phosphorylation	TLARLRATDLDQEVK HHHHHHCCCCCHHHH	30.57	21406692
588	Ubiquitination	TDLDQEVKERAISCM CCCCHHHHHHHHHHH	40.50	30230243
635	Phosphorylation	LPAIKALTLVAVSPL HHHHHHHHHHEECCC	24.85	-
640	Phosphorylation	ALTLVAVSPLQLDLQ HHHHHEECCCCCCCH	15.34	-
659	Phosphorylation	EALHILASFLRKNQR HHHHHHHHHHHHCHH	22.74	24719451
872	Phosphorylation	VLLEALGSPSEDVRA HHHHHHCCCCHHHHH	26.55	21406692
874	Phosphorylation	LEALGSPSEDVRAAA HHHHCCCCHHHHHHH	48.39	21406692
929	Phosphorylation	LGAAQPDSLKPYAED HCCCCCCCCCCHHHH	45.00	27067055
929	O-linked_Glycosylation	LGAAQPDSLKPYAED HCCCCCCCCCCHHHH	45.00	29351928
1087	Methylation	VDDGLDVRKAAFECM CCCCCHHHHHHHHHH	23.67	-
1088	Methylation	DDGLDVRKAAFECMY CCCCHHHHHHHHHHH	43.87	-
1166	Phosphorylation	TAKVKAGSVKQEFEK CEEECCCCCCHHHHC	30.88	26437602
1173	Acetylation	SVKQEFEKQDELKRS CCCHHHHCHHHHHHH	69.26	25953088
1180	Phosphorylation	KQDELKRSAMRAVAA CHHHHHHHHHHHHHH	25.48	22210691
1224	Phosphorylation	FESIQKDSASAPSTD HHHHHCCCCCCCCCC	31.03	-
1226	Phosphorylation	SIQKDSASAPSTDSM HHHCCCCCCCCCCCC	44.67	-
1229	Phosphorylation	KDSASAPSTDSMELS CCCCCCCCCCCCCCC	44.56	-
1230	Phosphorylation	DSASAPSTDSMELS- CCCCCCCCCCCCCC-	30.91	-
1236	Phosphorylation	STDSMELS------- CCCCCCCC-------	25.52	-

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	UBE3C	Q15386	PMID:12692129

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of CAND2_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 CAND2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
CNOT3_HUMAN	CNOT3	physical	12207886
NAA15_HUMAN	NAA15	physical	26344197

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 CAND2_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"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-1173, AND MASS SPECTROMETRY.	19608861 [Abstract]