dbPTM

NSL1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	NSL1_HUMAN
UniProt AC	Q96IY1
Protein Name	Kinetochore-associated protein NSL1 homolog
Gene Name	NSL1
Organism	Homo sapiens (Human).
Sequence Length	281
Subcellular Localization	Nucleus . Chromosome, centromere, kinetochore . Associated with the kinetochore (PubMed:15502821, PubMed:16585270).
Protein Description	Part of the MIS12 complex which is required for normal chromosome alignment and segregation and kinetochore formation during mitosis..
Protein Sequence	MAGSPELVVLDPPWDKELAAGTESQALVSATPREDFRVRCTSKRAVTEMLQLCGRFVQKLGDALPEEIREPALRDAQWTFESAVQENISINGQAWQEASDNCFMDSDIKVLEDQFDEIIVDIATKRKQYPRKILECVIKTIKAKQEILKQYHPVVHPLDLKYDPDPAPHMENLKCRGETVAKEISEAMKSLPALIEQGEGFSQVLRMQPVIHLQRIHQEVFSSCHRKPDAKPENFITQIETTPTETASRKTSDMVLKRKQTKDCPQRKWYPLRPKKINLDT

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
4	Phosphorylation	----MAGSPELVVLD ----CCCCCCEEEEC	12.98	28355574
22	Phosphorylation	DKELAAGTESQALVS CHHHCCCCCCHHHHH	27.95	19691289
24	Phosphorylation	ELAAGTESQALVSAT HHCCCCCCHHHHHCC	22.16	17525332
29	Phosphorylation	TESQALVSATPREDF CCCHHHHHCCCCCCC	27.55	24719451
31	Phosphorylation	SQALVSATPREDFRV CHHHHHCCCCCCCCH	18.51	21815630
59	Ubiquitination	LCGRFVQKLGDALPE HHHHHHHHHHHCCCH	49.49	21906983
59	Acetylation	LCGRFVQKLGDALPE HHHHHHHHHHHCCCH	49.49	26051181
125	Ubiquitination	IIVDIATKRKQYPRK HHHHHHHCCCCCCHH	48.88	2190698
132	Ubiquitination	KRKQYPRKILECVIK CCCCCCHHHHHHHHH	47.33	-
139	Acetylation	KILECVIKTIKAKQE HHHHHHHHHHHHHHH	24.65	25953088
139	Ubiquitination	KILECVIKTIKAKQE HHHHHHHHHHHHHHH	24.65	-
149	Ubiquitination	KAKQEILKQYHPVVH HHHHHHHHHHCCCCC	55.24	-
161	Ubiquitination	VVHPLDLKYDPDPAP CCCCCCCCCCCCCCC	47.47	-
174	Ubiquitination	APHMENLKCRGETVA CCCHHHCCCCCHHHH	33.20	-
179	Phosphorylation	NLKCRGETVAKEISE HCCCCCHHHHHHHHH	28.70	29759185
189	Ubiquitination	KEISEAMKSLPALIE HHHHHHHHHHHHHHH	56.75	-
222	Phosphorylation	RIHQEVFSSCHRKPD HHHHHHHHHHCCCCC	36.91	23312004
223	Phosphorylation	IHQEVFSSCHRKPDA HHHHHHHHHCCCCCC	11.50	23312004
231	Acetylation	CHRKPDAKPENFITQ HCCCCCCCCCCCEEE	61.31	26051181
237	Phosphorylation	AKPENFITQIETTPT CCCCCCEEEEECCCC	21.25	24732914
241	Phosphorylation	NFITQIETTPTETAS CCEEEEECCCCHHHC	39.44	30266825
242	Phosphorylation	FITQIETTPTETASR CEEEEECCCCHHHCC	18.54	30266825
244	Phosphorylation	TQIETTPTETASRKT EEEECCCCHHHCCHH	43.82	30266825
246	Phosphorylation	IETTPTETASRKTSD EECCCCHHHCCHHHC	32.20	30266825
248	Phosphorylation	TTPTETASRKTSDMV CCCCHHHCCHHHCCH	41.55	30266825
281	Phosphorylation	PKKINLDT------- CCCCCCCC-------	43.61	20860994

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 NSL1_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of NSL1_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 NSL1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
MIS12_HUMAN	MIS12	physical	15502821
DSN1_HUMAN	DSN1	physical	15502821
CBX5_HUMAN	CBX5	physical	15502821
CBX1_HUMAN	CBX1	physical	20231385
CBX3_HUMAN	CBX3	physical	20231385
CBX5_HUMAN	CBX5	physical	20231385
MIS12_HUMAN	MIS12	physical	20231385
DSN1_HUMAN	DSN1	physical	20231385
KNL1_HUMAN	CASC5	physical	20231385
BUB1_HUMAN	BUB1	physical	20231385
ZWINT_HUMAN	ZWINT	physical	20231385
NDC80_HUMAN	NDC80	physical	20231385
MIS12_HUMAN	MIS12	physical	21199919
KNL1_HUMAN	CASC5	physical	21199919
BUB1_HUMAN	BUB1	physical	21199919
NDC80_HUMAN	NDC80	physical	21199919
ZWINT_HUMAN	ZWINT	physical	21199919
ANXA1_HUMAN	ANXA1	physical	26186194
KNL1_HUMAN	CASC5	physical	26186194
ZWINT_HUMAN	ZWINT	physical	26186194
DSN1_HUMAN	DSN1	physical	26186194
SPC24_HUMAN	SPC24	physical	26186194
NDC80_HUMAN	NDC80	physical	26186194
BRCA2_HUMAN	BRCA2	physical	26186194
PMF1_HUMAN	PMF1	physical	26186194
CRNN_HUMAN	CRNN	physical	26186194
MIS12_HUMAN	MIS12	physical	26186194
NUF2_HUMAN	NUF2	physical	26186194
SPC25_HUMAN	SPC25	physical	26186194
ZG16B_HUMAN	ZG16B	physical	26186194
SPRR3_HUMAN	SPRR3	physical	26186194
PMF1_HUMAN	PMF1	physical	21199919
DSN1_HUMAN	DSN1	physical	28514442
SPC25_HUMAN	SPC25	physical	28514442
SPC24_HUMAN	SPC24	physical	28514442
ZWINT_HUMAN	ZWINT	physical	28514442
MIS12_HUMAN	MIS12	physical	28514442
NDC80_HUMAN	NDC80	physical	28514442
KNL1_HUMAN	CASC5	physical	28514442
NUF2_HUMAN	NUF2	physical	28514442
SPRR3_HUMAN	SPRR3	physical	28514442
CRNN_HUMAN	CRNN	physical	28514442
ZG16B_HUMAN	ZG16B	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.

Regulatory Network of NSL1_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage."; Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.; Science 316:1160-1166(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-24, AND MASSSPECTROMETRY.	17525332 [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 THR-22, AND MASSSPECTROMETRY.	19007248 [Abstract]
"Phosphoproteome analysis of the human mitotic spindle."; Nousiainen M., Sillje H.H.W., Sauer G., Nigg E.A., Koerner R.; Proc. Natl. Acad. Sci. U.S.A. 103:5391-5396(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-242, AND MASSSPECTROMETRY.	16565220 [Abstract]