UniProt ID | RPA2_MOUSE | |
---|---|---|
UniProt AC | P70700 | |
Protein Name | DNA-directed RNA polymerase I subunit RPA2 | |
Gene Name | Polr1b | |
Organism | Mus musculus (Mouse). | |
Sequence Length | 1135 | |
Subcellular Localization | Nucleus, nucleolus. | |
Protein Description | DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Second largest core component of RNA polymerase I which synthesizes ribosomal RNA precursors. Proposed to contribute to the polymerase catalytic activity and forms the polymerase active center together with the largest subunit. Pol I is composed of mobile elements and RPA2 is part of the core element with the central large cleft and probably a clamp element that moves to open and close the cleft (By similarity).. | |
Protein Sequence | MDVDGRWRNLPSGPSLKHLTDPSYGIPPEQQKAALQDLTRAHVDSFNYAALEGLSHAVQAIPPFEFAFKDERISLTIVDAVISPPSVPKGTICKDLNVYPAECRGRKSTYRGRLTADISWAVNGVPKGIIKQFLGYVPIMVKSKLCNLYNLPPRVLIEHHEEAEEMGGYFIINGIEKVIRMLIVPRRNFPIAMVRPKWKSRGLGYTQFGVSMRCVREEHSAVNMNLHYVENGTVMLNFIYRKELFFLPLGFALKALVSFSDYQIFQELIKGKEEDSFFRNSVSQMLRIVIEEGCHSQKQVLNYLGECFRVKLSLPDWYPNVEAAEFLLNQCICIHLQSNTDKFYLLCLMTRKLFALARGECMDDNPDSLVNQEVLSPGQLFLMFLKEKMENWLVSIKIVLDKRAQKANVSINNENLMKIFSMGTELTRPFEYLLATGNLRSKTGLGFLQDSGLCVVADKLNFLRYLSHFRCVHRGAAFAKMRTTTVRRLLPESWGFLCPVHTPDGAPCGLLNHLTAVCEVVTKFVYTASIPALLCGLGVTPVDTAPCRPYSDCYPVLLDGVMVGWVDKDLAPEVADTLRRFKVLREKRIPPWMEVALIPMTGKPSLYPGLFLFTTPCRLVRPVQNLELGREELIGTMEQLFMNVAIFEDEVFGGISTHQELFPHSLLSVIANFIPFSDHNQSPRNMYQCQMGKQTMGFPLLTYQNRSDNKLYRLQTPQSPLVRPCMYDFYDMDNYPIGTNAIVAVISYTGYDMEDAMIVNKASWERGFAHGSVYKSEFIDLSEKFKQGEDNLVFGVKPGDPRVMQKLDDDGLPFIGAKLEYGDPYYSYLNLNTGEGFVVYYKSKENCVVDNIKVCSNDMGSGKFKCICITVRIPRNPTIGDKFASRHGQKGILSRLWPAEDMPFTESGMMPDILFNPHGFPSRMTIGMLIESMAGKSAALHGLCHDATPFIFSEENSALEYFGEMLKAAGYNFYGTERLYSGISGMELEADIFIGVVYYQRLRHMVSDKFQVRTTGARDKVTNQPLGGRNVQGGIRFGEMERDALLAHGTSFLLHDRLFNCSDRSVAHMCVECGSLLSPLLEKPPPSWSAMRNRKYNCTVCGRSDTIDTVSVPYVFRYFVAELAAMNIKVKLDVI | |
Overview of Protein Modification Sites with Functional and Structural Information | ||
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
83 | Phosphorylation | TIVDAVISPPSVPKG EEEEEECCCCCCCCC | 24.94 | 26745281 | |
86 | Phosphorylation | DAVISPPSVPKGTIC EEECCCCCCCCCCEE | 55.20 | 26745281 | |
459 | Ubiquitination | GLCVVADKLNFLRYL CEEEEECHHHHHHHH | 35.28 | 27667366 | |
607 | Phosphorylation | MTGKPSLYPGLFLFT CCCCCCCCCCEEEEE | 10.29 | - | |
693 | Ubiquitination | MYQCQMGKQTMGFPL EEECCCCCCCCCCCE | 36.93 | 22790023 | |
784 | Ubiquitination | EFIDLSEKFKQGEDN HEECHHHHHHCCCCC | 55.26 | 22790023 | |
844 | Ubiquitination | FVVYYKSKENCVVDN EEEEEECCCCEEEEE | 49.12 | - | |
882 | Ubiquitination | RNPTIGDKFASRHGQ CCCCCHHHHHHHHCC | 37.30 | 22790023 | |
966 | Ubiquitination | LEYFGEMLKAAGYNF HHHHHHHHHHCCCCE | 2.73 | 27667366 | |
1020 | Ubiquitination | RTTGARDKVTNQPLG ECCCCCCCCCCCCCC | 45.46 | 27667366 | |
1051 | Phosphorylation | ALLAHGTSFLLHDRL HHHHCCCHHHHCCHH | 20.63 | - | |
1118 | Phosphorylation | SVPYVFRYFVAELAA CHHHHHHHHHHHHHH | 7.31 | - |
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 RPA2_MOUSE !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of RPA2_MOUSE !! |
* 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 RPA2_MOUSE !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
GMEB2_MOUSE | Gmeb2 | physical | 20211142 |
Kegg Drug | ||||||
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DrugBank | ||||||
There are no disease associations of PTM sites. |
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