HOP2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: HOP2_HUMAN
• UniProt AC: Q9P2W1
• Protein Name: Homologous-pairing protein 2 homolog
• Gene Name: PSMC3IP
• Organism: Homo sapiens (Human).
• Sequence Length: 217
• Subcellular Localization: Nucleus .
• Protein Description: Plays an important role in meiotic recombination. Stimulates DMC1-mediated strand exchange required for pairing homologous chromosomes during meiosis. The complex PSMC3IP/MND1 binds DNA, stimulates the recombinase activity of DMC1 as well as DMC1 D-loop formation from double-strand DNA. This complex stabilizes presynaptic RAD51 and DMC1 filaments formed on single strand DNA to capture double-strand DNA. This complex stimulates both synaptic and presynaptic critical steps in RAD51 and DMC1-promoted homologous pairing. May inhibit HIV-1 viral protein TAT activity and modulate the activity of proteasomes through association with PSMC3. Acts as a tissue specific coactivator of hormone-dependent transcription mediated by nuclear receptors..
• Protein Sequence: MSKGRAEAAAGAAGILLRYLQEQNRPYSSQDVFGNLQREHGLGKAVVVKTLEQLAQQGKIKEKMYGKQKIYFADQDQFDMVSDADLQVLDGKIVALTAKVQSLQQSCRYMEAELKELSSALTTPEMQKEIQELKKECAGYRERLKNIKAATNHVTPEEKEQVYRERQKYCKEWRKRKRMATELSDAILEGYPKSKKQFFEEVGIETDEDYNVTLPDP

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
2	Phosphorylation	------MSKGRAEAA ------CCCHHHHHH	43.76	19664995
29	Phosphorylation	EQNRPYSSQDVFGNL HCCCCCCCCCHHHHH	25.26	17525332
34	Acetylation	YSSQDVFGNLQREHG CCCCCHHHHHHHHHC	33.51	-
44	Acetylation	QREHGLGKAVVVKTL HHHHCCCHHHHHHHH	42.95	25953088
99	Ubiquitination	KIVALTAKVQSLQQS CHHHHHHHHHHHHHH	35.26	-
99	Acetylation	KIVALTAKVQSLQQS CHHHHHHHHHHHHHH	35.26	25953088
102	Phosphorylation	ALTAKVQSLQQSCRY HHHHHHHHHHHHHHH	31.00	-
106	Phosphorylation	KVQSLQQSCRYMEAE HHHHHHHHHHHHHHH	6.39	-
109	Phosphorylation	SLQQSCRYMEAELKE HHHHHHHHHHHHHHH	12.02	-
118	Phosphorylation	EAELKELSSALTTPE HHHHHHHHHHHCCHH	18.04	-
119	Phosphorylation	AELKELSSALTTPEM HHHHHHHHHHCCHHH	39.66	27732954
122	Phosphorylation	KELSSALTTPEMQKE HHHHHHHCCHHHHHH	39.77	27732954
123	Phosphorylation	ELSSALTTPEMQKEI HHHHHHCCHHHHHHH	20.36	27732954
155	Phosphorylation	KAATNHVTPEEKEQV HHHHCCCCHHHHHHH	19.89	25159151
159	Ubiquitination	NHVTPEEKEQVYRER CCCCHHHHHHHHHHH	52.35	-
159	Acetylation	NHVTPEEKEQVYRER CCCCHHHHHHHHHHH	52.35	23749302
181	Phosphorylation	RKRKRMATELSDAIL HHHHHHHHHHHHHHH	28.28	-

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

Oops, there are no upstream regulatory protein records of HOP2_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of HOP2_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 HOP2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
GCR_HUMAN	NR3C1	physical	11739747
PRS6A_HUMAN	PSMC3	physical	19325002

Drug and Disease Associations

• Kegg Disease
• There are no disease associations of PTM sites.
• OMIM Disease
• 614324: Ovarian dysgenesis 3 (ODG3)
• Kegg Drug
• There are no disease associations of PTM sites.
• DrugBank
• There are no disease associations of PTM sites.

Related Literatures of Post-Translational Modification

Phosphorylation

"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-29, AND MASSSPECTROMETRY.
PubMed: 17525332