Search Results
Overview
| Uniprot ID | P38935 |
|---|---|
| Protein Name | DNA-binding protein SMUBP-2 |
| Gene Name | IGHMBP2 |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 150 | VTYRRLKKALIALKK |
| 976 | LQRRLDKKLSELSNQ |
Function
5' to 3' helicase that unwinds both RNA and DNA duplexes in an ATP-dependent reaction (Probable) (PubMed:19158098, PubMed:30218034). Specific to 5'-phosphorylated single-stranded guanine-rich sequences (PubMed:22999958, PubMed:8349627). May play a role in RNA metabolism, ribosome biogenesis or initiation of translation (PubMed:19158098, PubMed:19299493). May play a role in regulation of transcription (By similarity). Interacts with tRNA-Tyr (PubMed:19299493). Has low processivity (PubMed:30218034)
Protein Sequence
10
MASAAVESFV
20
TKQLDLLELE
30
RDAEVEERRS
40
WQENISLKEL
50
QSRGVCLLKL
60
QVSSQRTGLY
70
GRLLVTFEPR
80
RYGSAAALPS
90
NSFTSGDIVG
100
LYDAANEGSQ
110
LATGILTRVT
120
QKSVTVAFDE
130
SHDFQLSLDR
140
ENSYRLLKLA
150
NDVTYRRLKK
160
ALIALKKYHS
170
GPASSLIEVL
180
FGRSAPSPAS
190
EIHPLTFFNT
200
CLDTSQKEAV
210
LFALSQKELA
220
IIHGPPGTGK
230
TTTVVEIILQ
240
AVKQGLKVLC
250
CAPSNIAVDN
260
LVERLALCKQ
270
RILRLGHPAR
280
LLESIQQHSL
290
DAVLARSDSA
300
QIVADIRKDI
310
DQVFVKNKKT
320
QDKREKSNFR
330
NEIKLLRKEL
340
KEREEAAMLE
350
SLTSANVVLA
360
TNTGASADGP
370
LKLLPESYFD
380
VVVIDECAQA
390
LEASCWIPLL
400
KARKCILAGD
410
HKQLPPTTVS
420
HKAALAGLSL
430
SLMERLAEEY
440
GARVVRTLTV
450
QYRMHQAIMR
460
WASDTMYLGQ
470
LTAHSSVARH
480
LLRDLPGVAA
490
TEETGVPLLL
500
VDTAGCGLFE
510
LEEEDEQSKG
520
NPGEVRLVSL
530
HIQALVDAGV
540
PARDIAVVSP
550
YNLQVDLLRQ
560
SLVHRHPELE
570
IKSVDGFQGR
580
EKEAVILSFV
590
RSNRKGEVGF
600
LAEDRRINVA
610
VTRARRHVAV
620
ICDSRTVNNH
630
AFLKTLVEYF
640
TQHGEVRTAF
650
EYLDDIVPEN
660
YSHENSQGSS
670
HAATKPQGPA
680
TSTRTGSQRQ
690
EGGQEAAAPA
700
RQGRKKPAGK
710
SLASEAPSQP
720
SLNGGSPEGV
730
ESQDGVDHFR
740
AMIVEFMASK
750
KMQLEFPPSL
760
NSHDRLRVHQ
770
IAEEHGLRHD
780
SSGEGKRRFI
790
TVSKRAPRPR
800
AALGPPAGTG
810
GPAPLQPVPP
820
TPAQTEQPPR
830
EQRGPDQPDL
840
RTLHLERLQR
850
VRSAQGQPAS
860
KEQQASGQQK
870
LPEKKKKKAK
880
GHPATDLPTE
890
EDFEALVSAA
900
VKADNTCGFA
910
KCTAGVTTLG
920
QFCQLCSRRY
930
CLSHHLPEIH
940
GCGERARAHA
950
RQRISREGVL
960
YAGSGTKNGS
970
LDPAKRAQLQ
980
RRLDKKLSEL
990
SNQRTSRRKE
RGT
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0030424 | axon |
| Cellular Component | GO:0016020 | membrane |
| Cellular Component | GO:0016604 | nuclear body |
| Cellular Component | GO:0005654 | nucleoplasm |
| Cellular Component | GO:0005634 | nucleus |
| Cellular Component | GO:1990904 | ribonucleoprotein complex |
| Molecular Function | GO:0043139 | 5'-3' DNA helicase activity |
| Molecular Function | GO:0032574 | 5'-3' RNA helicase activity |
| Molecular Function | GO:0005524 | ATP binding |
| Molecular Function | GO:0016887 | ATP hydrolysis activity |
| Molecular Function | GO:0008094 | ATP-dependent activity, acting on DNA |
| Molecular Function | GO:0008186 | ATP-dependent activity, acting on RNA |
| Molecular Function | GO:0003677 | DNA binding |
| Molecular Function | GO:0003678 | DNA helicase activity |
| Molecular Function | GO:0036121 | double-stranded DNA helicase activity |
| Molecular Function | GO:0140296 | general transcription initiation factor binding |
| Molecular Function | GO:0042802 | identical protein binding |
| Molecular Function | GO:0043022 | ribosome binding |
| Molecular Function | GO:0003723 | RNA binding |
| Molecular Function | GO:0003697 | single-stranded DNA binding |
| Molecular Function | GO:0003727 | single-stranded RNA binding |
| Molecular Function | GO:0000049 | tRNA binding |
| Molecular Function | GO:0008270 | zinc ion binding |
| Biological Process | GO:0006974 | DNA damage response |
| Biological Process | GO:0006351 | DNA-templated transcription |
| Cellular Component | GO:0005737 | cytoplasm |
| Cellular Component | GO:0005829 | cytosol |
| Cellular Component | GO:0030426 | growth cone |
Reference
[1] Wu Q, Li Z, Gong T, Zheng X, Zhou X et al.. Porphyromonas gingivalis infection induces lysine lactylation reprogramming in human umbilical vein endothelial cells.. Front Cell Infect Microbiol 16:1706727. 2026. PMID: 41696360.