RXFP1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: RXFP1_HUMAN
• UniProt AC: Q9HBX9
• Protein Name: Relaxin receptor 1
• Gene Name: RXFP1
• Organism: Homo sapiens (Human).
• Sequence Length: 757
• Subcellular Localization: Cell membrane ; Multi-pass membrane protein .
• Protein Description: Receptor for relaxins. The activity of this receptor is mediated by G proteins leading to stimulation of adenylate cyclase and an increase of cAMP. Binding of the ligand may also activate a tyrosine kinase pathway that inhibits the activity of a phosphodiesterase that degrades cAMP..
• Protein Sequence: MTSGSVFFYILIFGKYFSHGGGQDVKCSLGYFPCGNITKCLPQLLHCNGVDDCGNQADEDNCGDNNGWSLQFDKYFASYYKMTSQYPFEAETPECLVGSVPVQCLCQGLELDCDETNLRAVPSVSSNVTAMSLQWNLIRKLPPDCFKNYHDLQKLYLQNNKITSISIYAFRGLNSLTKLYLSHNRITFLKPGVFEDLHRLEWLIIEDNHLSRISPPTFYGLNSLILLVLMNNVLTRLPDKPLCQHMPRLHWLDLEGNHIHNLRNLTFISCSNLTVLVMRKNKINHLNENTFAPLQKLDELDLGSNKIENLPPLIFKDLKELSQLNLSYNPIQKIQANQFDYLVKLKSLSLEGIEISNIQQRMFRPLMNLSHIYFKKFQYCGYAPHVRSCKPNTDGISSLENLLASIIQRVFVWVVSAVTCFGNIFVICMRPYIRSENKLYAMSIISLCCADCLMGIYLFVIGGFDLKFRGEYNKHAQLWMESTHCQLVGSLAILSTEVSVLLLTFLTLEKYICIVYPFRCVRPGKCRTITVLILIWITGFIVAFIPLSNKEFFKNYYGTNGVCFPLHSEDTESIGAQIYSVAIFLGINLAAFIIIVFSYGSMFYSVHQSAITATEIRNQVKKEMILAKRFFFIVFTDALCWIPIFVVKFLSLLQVEIPGTITSWVVIFILPINSALNPILYTLTTRPFKEMIHRFWYNYRQRKSMDSKGQKTYAPSFIWVEMWPLQEMPPELMKPDLFTYPCEMSLISQSTRLNSYS

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
36	N-linked_Glycosylation	LGYFPCGNITKCLPQ EEEECCCCHHHHHHH	45.53	18533687
127	N-linked_Glycosylation	AVPSVSSNVTAMSLQ CCCCCCCCCEEHHHH	27.87	18533687
156	Phosphorylation	YHDLQKLYLQNNKIT HHHHHHHHHCCCCCC	17.18	22210691
264	N-linked_Glycosylation	NHIHNLRNLTFISCS CCCCCCCCCEEEECC	46.74	18533687
272	N-linked_Glycosylation	LTFISCSNLTVLVMR CEEEECCCEEEEEEE	44.02	18533687
304	Phosphorylation	LDELDLGSNKIENLP CCCCCCCCCCCCCCC	42.10	29255136
325	N-linked_Glycosylation	LKELSQLNLSYNPIQ HHHHHCCCCCCCHHH	21.21	18533687
341	Phosphorylation	IQANQFDYLVKLKSL HHHCCCCCEEEEEEC	18.06	25003641
368	N-linked_Glycosylation	RMFRPLMNLSHIYFK HHHHHHHCHHHEEEE	46.18	18533687
504	Phosphorylation	EVSVLLLTFLTLEKY HHHHHHHHHHHHHHE	19.30	-
507	Phosphorylation	VLLLTFLTLEKYICI HHHHHHHHHHHEEEE	28.78	-
739	Phosphorylation	LMKPDLFTYPCEMSL HCCCCCCCCCCHHHH	33.57	23663014
740	Phosphorylation	MKPDLFTYPCEMSLI CCCCCCCCCCHHHHH	9.88	23663014
745	Phosphorylation	FTYPCEMSLISQSTR CCCCCHHHHHHCCCC	10.56	23663014
748	Phosphorylation	PCEMSLISQSTRLNS CCHHHHHHCCCCCCC	24.30	23663014
750	Phosphorylation	EMSLISQSTRLNSYS HHHHHHCCCCCCCCC	14.54	23663014
751	Phosphorylation	MSLISQSTRLNSYS- HHHHHCCCCCCCCC-	31.38	23663014
756	Phosphorylation	QSTRLNSYS------ CCCCCCCCC------	19.82	30576142
757	Phosphorylation	STRLNSYS------- CCCCCCCC-------	33.30	30576142

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

Oops, there are no upstream regulatory protein records of RXFP1_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of RXFP1_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 RXFP1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
REL3_HUMAN	RLN3	physical	22257012
C1QT8_HUMAN	C1QTNF8	physical	24014093

Drug and Disease Associations

• Kegg Disease
• OMIM Disease
• There are no disease associations of PTM sites.
• Kegg Drug
• DrugBank
• There are no disease associations of PTM sites.

Related Literatures of Post-Translational Modification

N-linked Glycosylation

"Identification of the N-linked glycosylation sites of the humanrelaxin receptor and effect of glycosylation on receptor function.";
Yan Y., Scott D.J., Wilkinson T.N., Ji J., Tregear G.W.,Bathgate R.A.;
Biochemistry 47:6953-6968(2008).
Cited for: GLYCOSYLATION AT ASN-36; ASN-127; ASN-264; ASN-272; ASN-325 ANDASN-368.
PubMed: 18533687