HUS1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: HUS1_HUMAN
• UniProt AC: O60921
• Protein Name: Checkpoint protein HUS1
• Gene Name: HUS1
• Organism: Homo sapiens (Human).
• Sequence Length: 280
• Subcellular Localization: Nucleus . Cytoplasm, cytosol . In discrete nuclear foci upon DNA damage. According to PubMed:11077446, localized also in the cytoplasm. DNA damage induces its nuclear translocation. Shuttles between the nucleus and the cytoplasm.
• Protein Description: Component of the 9-1-1 cell-cycle checkpoint response complex that plays a major role in DNA repair. The 9-1-1 complex is recruited to DNA lesion upon damage by the RAD17-replication factor C (RFC) clamp loader complex. Acts then as a sliding clamp platform on DNA for several proteins involved in long-patch base excision repair (LP-BER). The 9-1-1 complex stimulates DNA polymerase beta (POLB) activity by increasing its affinity for the 3'-OH end of the primer-template and stabilizes POLB to those sites where LP-BER proceeds; endonuclease FEN1 cleavage activity on substrates with double, nick, or gap flaps of distinct sequences and lengths; and DNA ligase I (LIG1) on long-patch base excision repair substrates. The 9-1-1 complex is necessary for the recruitment of RHNO1 to sites of double-stranded breaks (DSB) occurring during the S phase..
• Protein Sequence: MKFRAKIVDGACLNHFTRISNMIAKLAKTCTLRISPDKLNFILCDKLANGGVSMWCELEQENFFNEFQMEGVSAENNEIYLELTSENLSRALKTAQNARALKIKLTNKHFPCLTVSVELLSMSSSSRIVTHDIPIKVIPRKLWKDLQEPVVPDPDVSIYLPVLKTMKSVVEKMKNISNHLVIEANLDGELNLKIETELVCVTTHFKDLGNPPLASESTHEDRNVEHMAEVHIDIRKLLQFLAGQQVNPTKALCNIVNNKMVHFDLLHEDVSLQYFIPALS

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
17	Ubiquitination	GACLNHFTRISNMIA HHHHHHHHHHHHHHH	21.39	-
28	Ubiquitination	NMIAKLAKTCTLRIS HHHHHHHCCCCEEEC	55.35	-
38	Ubiquitination	TLRISPDKLNFILCD CEEECHHHCCEEEEH	49.03	-
93	Ubiquitination	ENLSRALKTAQNARA HHHHHHHHHHHHHHH	40.61	-
115	Ubiquitination	KHFPCLTVSVELLSM CCCCEEEEEEEEECC	3.78	21890473
136	Ubiquitination	VTHDIPIKVIPRKLW EECCCCCEEECHHHH	28.85	21890473
143	Ubiquitination	KVIPRKLWKDLQEPV EEECHHHHHHCCCCC	8.64	21890473
146	Ubiquitination	PRKLWKDLQEPVVPD CHHHHHHCCCCCCCC	5.73	-
159	Phosphorylation	PDPDVSIYLPVLKTM CCCCCHHHHHHHHHH	9.46	-
164	Ubiquitination	SIYLPVLKTMKSVVE HHHHHHHHHHHHHHH	46.97	21890473
167	Ubiquitination	LPVLKTMKSVVEKMK HHHHHHHHHHHHHHH	45.38	-
202	Phosphorylation	ETELVCVTTHFKDLG EEEEEEEEEEHHHCC	14.93	18452278
215	Phosphorylation	LGNPPLASESTHEDR CCCCCCCCCCCCCCC	39.50	30266825
217	Phosphorylation	NPPLASESTHEDRNV CCCCCCCCCCCCCCH	32.35	30266825
218	Phosphorylation	PPLASESTHEDRNVE CCCCCCCCCCCCCHH	25.82	30266825
229	Ubiquitination	RNVEHMAEVHIDIRK CCHHHHEEEHHHHHH	27.36	-
236	Ubiquitination	EVHIDIRKLLQFLAG EEHHHHHHHHHHHHC	54.61	-
249	Phosphorylation	AGQQVNPTKALCNIV HCCCCCHHHHHHHHH	24.60	22468782
250	Ubiquitination	GQQVNPTKALCNIVN CCCCCHHHHHHHHHC	40.39	-

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

Oops, there are no upstream regulatory protein records of HUS1_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of HUS1_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 HUS1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
PCNA_HUMAN	PCNA	physical	11077446
PSA2_HUMAN	PSMA2	physical	17353931
HPRT_HUMAN	HPRT1	physical	17353931
HDAC1_HUMAN	HDAC1	physical	10846170
RAD9A_HUMAN	RAD9A	physical	9872989
RAD1_HUMAN	RAD1	physical	9872989
RAD1_HUMAN	RAD1	physical	11944979
RFA1_HUMAN	RPA1	physical	15897895
RFA2_HUMAN	RPA2	physical	15897895
RAD1_HUMAN	RAD1	physical	15122316
CSN5_HUMAN	COPS5	physical	17583730
MSH2_HUMAN	MSH2	physical	20188637
MSH6_HUMAN	MSH6	physical	20188637
MSH3_HUMAN	MSH3	physical	20188637
ZBT14_HUMAN	ZBTB14	physical	26186194
RAD17_HUMAN	RAD17	physical	26186194
RAD1_HUMAN	RAD1	physical	26186194
RAD9A_HUMAN	RAD9A	physical	26186194
RAD1_HUMAN	RAD1	physical	28514442
RAD9A_HUMAN	RAD9A	physical	28514442
ZBT14_HUMAN	ZBTB14	physical	28514442
RAD17_HUMAN	RAD17	physical	28514442
FANCA_HUMAN	FANCA	physical	28215707

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.