SPC25_HUMAN - dbPTM
SPC25_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SPC25_HUMAN
UniProt AC Q9HBM1
Protein Name Kinetochore protein Spc25
Gene Name SPC25
Organism Homo sapiens (Human).
Sequence Length 224
Subcellular Localization Nucleus. Chromosome, centromere, kinetochore . Localizes to kinetochores from late prophase to anaphase (PubMed:14738735). Localizes specifically to the outer plate of the kinetochore (PubMed:14738735, PubMed:14699129).
Protein Description Acts as a component of the essential kinetochore-associated NDC80 complex, which is required for chromosome segregation and spindle checkpoint activity. [PubMed: 14699129]
Protein Sequence MVEDELALFDKSINEFWNKFKSTDTSCQMAGLRDTYKDSIKAFAEKLSVKLKEEERMVEMFLEYQNQISRQNKLIQEKKDNLLKLIAEVKGKKQELEVLTANIQDLKEEYSRKKETISTANKANAERLKRLQKSADLYKDRLGLEIRKIYGEKLQFIFTNIDPKNPESPFMFSLHLNEARDYEVSDSAPHLEGLAEFQENVRKTNNFSAFLANVRKAFTATVYN
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 Orthologous
Protein Cluster
1Acetylation-------MVEDELAL
-------CCHHHHHH		7.22-
11UbiquitinationDELALFDKSINEFWN
HHHHHHHHHHHHHHH		45.9929967540
12PhosphorylationELALFDKSINEFWNK
HHHHHHHHHHHHHHH		32.2725159151
19UbiquitinationSINEFWNKFKSTDTS
HHHHHHHHHHCCCCC		44.7722817900
21UbiquitinationNEFWNKFKSTDTSCQ
HHHHHHHHCCCCCHH		54.8022817900
37UbiquitinationAGLRDTYKDSIKAFA
CCCHHHHHHHHHHHH		47.2829967540
41UbiquitinationDTYKDSIKAFAEKLS
HHHHHHHHHHHHHHC		41.2132015554
46UbiquitinationSIKAFAEKLSVKLKE
HHHHHHHHHCCCCHH		42.5029967540
48PhosphorylationKAFAEKLSVKLKEEE
HHHHHHHCCCCHHHH		28.4223186163
50UbiquitinationFAEKLSVKLKEEERM
HHHHHCCCCHHHHHH		50.93-
73UbiquitinationNQISRQNKLIQEKKD
HHHHHHHHHHHHHHH		38.3329967540
78UbiquitinationQNKLIQEKKDNLLKL
HHHHHHHHHHHHHHH		49.39-
79UbiquitinationNKLIQEKKDNLLKLI
HHHHHHHHHHHHHHH		51.61-
84UbiquitinationEKKDNLLKLIAEVKG
HHHHHHHHHHHHHCC		40.8029967540
90UbiquitinationLKLIAEVKGKKQELE
HHHHHHHCCCHHHHH		57.4232015554
92UbiquitinationLIAEVKGKKQELEVL
HHHHHCCCHHHHHHH		45.63-
93UbiquitinationIAEVKGKKQELEVLT
HHHHCCCHHHHHHHH		58.6429967540
107UbiquitinationTANIQDLKEEYSRKK
HHHHHHHHHHHHCHH		57.7132015554
107SumoylationTANIQDLKEEYSRKK
HHHHHHHHHHHHCHH		57.71-
113UbiquitinationLKEEYSRKKETISTA
HHHHHHCHHHHHHHH		49.3629967540
114UbiquitinationKEEYSRKKETISTAN
HHHHHCHHHHHHHHH		60.0029967540
122UbiquitinationETISTANKANAERLK
HHHHHHHHHHHHHHH		40.3224816145
133UbiquitinationERLKRLQKSADLYKD
HHHHHHHHHHHHHHH		52.8029967540
139UbiquitinationQKSADLYKDRLGLEI
HHHHHHHHHHHHHHH		43.6024816145
150PhosphorylationGLEIRKIYGEKLQFI
HHHHHHHHHCCCEEE		23.4423898821
182PhosphorylationHLNEARDYEVSDSAP
ECCCCCCCCCCCCCC		16.8127642862
203UbiquitinationEFQENVRKTNNFSAF
HHHHHHHHHCCHHHH		51.8523000965
204PhosphorylationFQENVRKTNNFSAFL
HHHHHHHHCCHHHHH		25.49-
216UbiquitinationAFLANVRKAFTATVY
HHHHHHHHHHHHHCC		43.5022505724
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 SPC25_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SPC25_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 SPC25_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
NDC80_HUMANNDC80physical
14699129
TB182_HUMANTNKS1BP1physical
22863883
CYTSA_HUMANSPECC1Lphysical
26186194
KNL1_HUMANCASC5physical
26186194
EPS15_HUMANEPS15physical
26186194
NDC80_HUMANNDC80physical
26186194
KTN1_HUMANKTN1physical
26186194
EP15R_HUMANEPS15L1physical
26186194
MY18A_HUMANMYO18Aphysical
26186194
AP2A1_HUMANAP2A1physical
26186194
HDGR2_HUMANHDGFRP2physical
26186194
PMF1_HUMANPMF1physical
26186194
NUF2_HUMANNUF2physical
26186194
FCHO2_HUMANFCHO2physical
26186194
MIS12_HUMANMIS12physical
26186194
SNP29_HUMANSNAP29physical
26186194
GCC2_HUMANGCC2physical
26186194
A16L1_HUMANATG16L1physical
26186194
CL043_HUMANC12orf43physical
26186194
NDC80_HUMANNDC80physical
28514442
EPS15_HUMANEPS15physical
28514442
MIS12_HUMANMIS12physical
28514442
NUF2_HUMANNUF2physical
28514442
FCHO2_HUMANFCHO2physical
28514442
EP15R_HUMANEPS15L1physical
28514442
KNL1_HUMANCASC5physical
28514442
A16L1_HUMANATG16L1physical
28514442
MY18A_HUMANMYO18Aphysical
28514442
CYTSA_HUMANSPECC1Lphysical
28514442
CL043_HUMANC12orf43physical
28514442
CSPP1_HUMANCSPP1physical
28514442
SNP29_HUMANSNAP29physical
28514442
KTN1_HUMANKTN1physical
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 SPC25_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"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: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY.

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