STN1_HUMAN - dbPTM
STN1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID STN1_HUMAN
UniProt AC Q9H668
Protein Name CST complex subunit STN1
Gene Name STN1 {ECO:0000312|HGNC:HGNC:26200}
Organism Homo sapiens (Human).
Sequence Length 368
Subcellular Localization Nucleus . Chromosome, telomere .
Protein Description Component of the CST complex proposed to act as a specialized replication factor promoting DNA replication under conditions of replication stress or natural replication barriers such as the telomere duplex. The CST complex binds single-stranded DNA with high affinity in a sequence-independent manner, while isolated subunits bind DNA with low affinity by themselves. Initially the CST complex has been proposed to protect telomeres from DNA degradation. [PubMed: 19854130 However, the CST complex has been shown to be involved in several aspects of telomere replication. The CST complex inhibits telomerase and is involved in telomere length homeostasis; it is proposed to bind to newly telomerase-synthesized 3' overhangs and to terminate telomerase action implicating the association with the ACD:POT1 complex thus interfering with its telomerase stimulation activity. The CST complex is also proposed to be involved in fill-in synthesis of the telomeric C-strand probably implicating recruitment and activation of DNA polymerase alpha]
Protein Sequence MQPGSSRCEEETPSLLWGLDPVFLAFAKLYIRDILDMKESRQVPGVFLYNGHPIKQVDVLGTVIGVRERDAFYSYGVDDSTGVINCICWKKLNTESVSAAPSAARELSLTSQLKKLQETIEQKTKIEIGDTIRVRGSIRTYREEREIHATTYYKVDDPVWNIQIARMLELPTIYRKVYDQPFHSSALEKEEALSNPGALDLPSLTSLLSEKAKEFLMENRVQSFYQQELEMVESLLSLANQPVIHSASSDQVNFKKDTTSKAIHSIFKNAIQLLQEKGLVFQKDDGFDNLYYVTREDKDLHRKIHRIIQQDCQKPNHMEKGCHFLHILACARLSIRPGLSEAVLQQVLELLEDQSDIVSTMEHYYTAF
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
38UbiquitinationIRDILDMKESRQVPG
HHHHHCCHHHCCCCC
52.8129967540
55UbiquitinationLYNGHPIKQVDVLGT
EECCEECCEEEEEEE
49.04-
90UbiquitinationVINCICWKKLNTESV
EEEEEEEEECCCCCC
42.8622817900
91UbiquitinationINCICWKKLNTESVS
EEEEEEEECCCCCCC
23.5921906983
114UbiquitinationLSLTSQLKKLQETIE
HHHHHHHHHHHHHHH
43.7429967540
115UbiquitinationSLTSQLKKLQETIEQ
HHHHHHHHHHHHHHH
65.09-
119PhosphorylationQLKKLQETIEQKTKI
HHHHHHHHHHHHHCC
19.49-
123UbiquitinationLQETIEQKTKIEIGD
HHHHHHHHHCCCCCC
38.7121906983
125UbiquitinationETIEQKTKIEIGDTI
HHHHHHHCCCCCCEE
45.4322817900
131PhosphorylationTKIEIGDTIRVRGSI
HCCCCCCEEEECCEE
12.8923403867
176UbiquitinationELPTIYRKVYDQPFH
CCCCCHHHHHCCCCC
28.3321906983
178PhosphorylationPTIYRKVYDQPFHSS
CCCHHHHHCCCCCCH
16.34-
189UbiquitinationFHSSALEKEEALSNP
CCCHHHHHHHHHCCC
62.8021906983
194PhosphorylationLEKEEALSNPGALDL
HHHHHHHCCCCCCCH
48.2924719451
203PhosphorylationPGALDLPSLTSLLSE
CCCCCHHHHHHHHHH
52.1324719451
205PhosphorylationALDLPSLTSLLSEKA
CCCHHHHHHHHHHHH
22.9726074081
206PhosphorylationLDLPSLTSLLSEKAK
CCHHHHHHHHHHHHH
32.3826074081
209PhosphorylationPSLTSLLSEKAKEFL
HHHHHHHHHHHHHHH
42.2026074081
211UbiquitinationLTSLLSEKAKEFLME
HHHHHHHHHHHHHHH
62.4721906983
213UbiquitinationSLLSEKAKEFLMENR
HHHHHHHHHHHHHHH
61.1321906983
261UbiquitinationFKKDTTSKAIHSIFK
CCCCHHHHHHHHHHH
49.6329967540
265PhosphorylationTTSKAIHSIFKNAIQ
HHHHHHHHHHHHHHH
24.4924719451
268UbiquitinationKAIHSIFKNAIQLLQ
HHHHHHHHHHHHHHH
43.7429967540
277UbiquitinationAIQLLQEKGLVFQKD
HHHHHHHCCCEEECC
44.5821906983
283UbiquitinationEKGLVFQKDDGFDNL
HCCCEEECCCCCCCE
46.4522817900
314UbiquitinationIIQQDCQKPNHMEKG
HHHHHCCCCCHHHCC
54.8629967540

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 STN1_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of STN1_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 STN1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MED12_HUMANMED12physical
20133760
MED13_HUMANMED13physical
20133760
MED25_HUMANMED25physical
20133760
MED16_HUMANMED16physical
20133760
MED17_HUMANMED17physical
20133760
MED1_HUMANMED1physical
20133760
MED24_HUMANMED24physical
20133760
MED23_HUMANMED23physical
20133760
MED4_HUMANMED4physical
20133760
MED29_HUMANMED29physical
20133760
MED8_HUMANMED8physical
20133760
MED6_HUMANMED6physical
20133760
MED14_HUMANMED14physical
20133760
MED30_HUMANMED30physical
20133760
RPB1_HUMANPOLR2Aphysical
20133760
MED9_HUMANMED9physical
20133760
RCOR1_HUMANRCOR1physical
20133760
MED27_HUMANMED27physical
20133760
A4_HUMANAPPphysical
21832049
TEN1L_HUMANTEN1physical
26186194
UBP47_HUMANUSP47physical
26186194
UBP4_HUMANUSP4physical
26186194
UBP15_HUMANUSP15physical
26186194
CYTSA_HUMANSPECC1Lphysical
26186194
GRN_HUMANGRNphysical
26186194
ARH_HUMANLDLRAP1physical
26186194
CTC1_HUMANCTC1physical
26186194
LRWD1_HUMANLRWD1physical
26186194
PRI2_HUMANPRIM2physical
26186194
DPOLA_HUMANPOLA1physical
26186194
OGA_HUMANMGEA5physical
26186194
F136A_HUMANFAM136Aphysical
26186194
ARP3C_HUMANACTR3Cphysical
26186194
NSE3_HUMANNDNL2physical
26186194
SMC6_HUMANSMC6physical
26186194
SMC5_HUMANSMC5physical
26186194
ORC3_HUMANORC3physical
26186194
UBP33_HUMANUSP33physical
26186194
SMCO3_HUMANSMCO3physical
26186194
KIF3A_HUMANKIF3Aphysical
26186194
ORC2_HUMANORC2physical
26186194
NSE1_HUMANNSMCE1physical
26186194
PRI1_HUMANPRIM1physical
26186194
TEN1L_HUMANTEN1physical
28514442
CTC1_HUMANCTC1physical
28514442
ORC3_HUMANORC3physical
28514442
ORC2_HUMANORC2physical
28514442
ARP3C_HUMANACTR3Cphysical
28514442
SMC5_HUMANSMC5physical
28514442
SMC6_HUMANSMC6physical
28514442
UBP4_HUMANUSP4physical
28514442
F136A_HUMANFAM136Aphysical
28514442
ARH_HUMANLDLRAP1physical
28514442
KIF3A_HUMANKIF3Aphysical
28514442
SMCO3_HUMANSMCO3physical
28514442
NSE3_HUMANNDNL2physical
28514442
UBP33_HUMANUSP33physical
28514442
UBP47_HUMANUSP47physical
28514442
CYTSA_HUMANSPECC1Lphysical
28514442
OGA_HUMANMGEA5physical
28514442
UBP15_HUMANUSP15physical
28514442
HNRPF_HUMANHNRNPFphysical
28514442
NSE1_HUMANNSMCE1physical
28514442
GRN_HUMANGRNphysical
28514442
DPOA2_HUMANPOLA2physical
28514442
PRI1_HUMANPRIM1physical
28514442
LRWD1_HUMANLRWD1physical
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 STN1_HUMAN

loading...

Related Literatures of Post-Translational Modification

TOP