Overview
| Uniprot ID | P30876 |
| Protein Name | DNA-directed RNA polymerase II subunit RPB2 |
| Gene Name | POLR2B |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position |
Flanking peptide |
| 248 |
ARGGQGAKKSAIGQR |
| 249 |
RGGQGAKKSAIGQRI |
Function
Catalytic core component of RNA polymerase II (Pol II), a DNA-dependent RNA polymerase which synthesizes mRNA precursors and many functional non-coding RNAs using the four ribonucleoside triphosphates as substrates (By similarity) (PubMed:27193682, PubMed:30190596, PubMed:9852112). Pol II-mediated transcription cycle proceeds through transcription initiation, transcription elongation and transcription termination stages. During transcription initiation, Pol II pre-initiation complex (PIC) is recruited to DNA promoters, with focused-type promoters containing either the initiator (Inr) element, or the TATA-box found in cell-type specific genes and dispersed-type promoters that often contain hypomethylated CpG islands usually found in housekeeping genes. Once the polymerase has escaped from the promoter it enters the elongation phase during which RNA is actively polymerized, based on complementarity with the template DNA strand. Transcription termination involves the release of the RNA transcript and polymerase from the DNA (PubMed:27193682, PubMed:30190596, PubMed:9852112). Forms Pol II active center together with the largest subunit POLR2A/RPB1. Appends one nucleotide at a time to the 3' end of the nascent RNA, with POLR2A/RPB1 most likely contributing a Mg(2+)-coordinating DxDGD motif and POLR2B/RPB2 participating in the coordination of a second Mg(2+) ion and providing lysine residues believed to facilitate Watson-Crick base pairing between the incoming nucleotide and template base. Typically, Mg(2+) ions direct a 5' nucleoside triphosphate to form a phosphodiester bond with the 3' hydroxyl of the preceding nucleotide of the nascent RNA, with the elimination of pyrophosphate. The reversible pyrophosphorolysis can occur at high pyrophosphate concentrations (By similarity) (PubMed:30190596, PubMed:9852112). Can proofread the nascent RNA transcript by means of a 3' -> 5' exonuclease activity. If a ribonucleotide is mis-incorporated, backtracks along the template DNA and cleaves the phosphodiester bond releasing the mis-incorporated 5'-ribonucleotide (By similarity) (PubMed:8381534)
Protein Sequence
10
MYDADEDMQY
20
DEDDDEITPD
30
LWQEACWIVI
40
SSYFDEKGLV
50
RQQLDSFDEF
60
IQMSVQRIVE
70
DAPPIDLQAE
80
AQHASGEVEE
90
PPRYLLKFEQ
100
IYLSKPTHWE
110
RDGAPSPMMP
120
NEARLRNLTY
130
SAPLYVDITK
140
TVIKEGEEQL
150
QTQHQKTFIG
160
KIPIMLRSTY
170
CLLNGLTDRD
180
LCELNECPLD
190
PGGYFIINGS
200
EKVLIAQEKM
210
ATNTVYVFAK
220
KDSKYAYTGE
230
CRSCLENSSR
240
PTSTIWVSML
250
ARGGQGAKKS
260
AIGQRIVATL
270
PYIKQEVPII
280
IVFRALGFVS
290
DRDILEHIIY
300
DFEDPEMMEM
310
VKPSLDEAFV
320
IQEQNVALNF
330
IGSRGAKPGV
340
TKEKRIKYAK
350
EVLQKEMLPH
360
VGVSDFCETK
370
KAYFLGYMVH
380
RLLLAALGRR
390
ELDDRDHYGN
400
KRLDLAGPLL
410
AFLFRGMFKN
420
LLKEVRIYAQ
430
KFIDRGKDFN
440
LELAIKTRII
450
SDGLKYSLAT
460
GNWGDQKKAH
470
QARAGVSQVL
480
NRLTFASTLS
490
HLRRLNSPIG
500
RDGKLAKPRQ
510
LHNTLWGMVC
520
PAETPEGHAV
530
GLVKNLALMA
540
YISVGSQPSP
550
ILEFLEEWSM
560
ENLEEISPAA
570
IADATKIFVN
580
GCWVGIHKDP
590
EQLMNTLRKL
600
RRQMDIIVSE
610
VSMIRDIRER
620
EIRIYTDAGR
630
ICRPLLIVEK
640
QKLLLKKRHI
650
DQLKEREYNN
660
YSWQDLVASG
670
VVEYIDTLEE
680
ETVMLAMTPD
690
DLQEKEVAYC
700
STYTHCEIHP
710
SMILGVCASI
720
IPFPDHNQSP
730
RNTYQSAMGK
740
QAMGVYITNF
750
HVRMDTLAHV
760
LYYPQKPLVT
770
TRSMEYLRFR
780
ELPAGINSIV
790
AIASYTGYNQ
800
EDSVIMNRSA
810
VDRGFFRSVF
820
YRSYKEQESK
830
KGFDQEEVFE
840
KPTRETCQGM
850
RHAIYDKLDD
860
DGLIAPGVRV
870
SGDDVIIGKT
880
VTLPENEDEL
890
ESTNRRYTKR
900
DCSTFLRTSE
910
TGIVDQVMVT
920
LNQEGYKFCK
930
IRVRSVRIPQ
940
IGDKFASRHG
950
QKGTCGIQYR
960
QEDMPFTCEG
970
ITPDIIINPH
980
AIPSRMTIGH
990
LIECLQGKVS
1000
ANKGEIGDAT
1010
PFNDAVNVQK
1020
ISNLLSDYGY
1030
HLRGNEVLYN
1040
GFTGRKITSQ
1050
IFIGPTYYQR
1060
LKHMVDDKIH
1070
SRARGPIQIL
1080
NRQPMEGRSR
1090
DGGLRFGEME
1100
RDCQIAHGAA
1110
QFLRERLFEA
1120
SDPYQVHVCN
1130
LCGIMAIANT
1140
RTHTYECRGC
1150
RNKTQISLVR
1160
MPYACKLLFQ
1170
ELMSMSIAPR
MMSV
Gene Ontology
| Classification |
GO ID |
Description |
| Cellular Component |
GO:0016020 |
membrane |
| Cellular Component |
GO:0005654 |
nucleoplasm |
| Cellular Component |
GO:0005634 |
nucleus |
| Cellular Component |
GO:0005665 |
RNA polymerase II, core complex |
| Molecular Function |
GO:0003682 |
chromatin binding |
| Molecular Function |
GO:0003677 |
DNA binding |
| Molecular Function |
GO:0003899 |
DNA-directed RNA polymerase activity |
| Molecular Function |
GO:0016787 |
hydrolase activity |
| Molecular Function |
GO:0032549 |
ribonucleoside binding |
| Molecular Function |
GO:0003723 |
RNA binding |
| Molecular Function |
GO:0003968 |
RNA-directed RNA polymerase activity |
| Molecular Function |
GO:0008270 |
zinc ion binding |
| Biological Process |
GO:0006354 |
DNA-templated transcription elongation |
| Biological Process |
GO:0006366 |
transcription by RNA polymerase II |
| Biological Process |
GO:0006368 |
transcription elongation by RNA polymerase II |
| Biological Process |
GO:0006367 |
transcription initiation at RNA polymerase II promoter |
Reference
[1] Hong H, Chen X, Wang H, Gu X, Yuan Y et al.. Global profiling of protein lysine lactylation and potential target modified protein analysis in hepatocellular carcinoma.. Proteomics 23(9):e2200432. 2023 May. PMID: 36625413.