Search Results
Overview
| Uniprot ID | H0VDK8 |
|---|---|
| Protein Name | Structural maintenance of chromosomes protein |
| Gene Name | SMC3 |
| Organism | Cavia porcellus |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 106 | RRVIGAKKDQYFLDK |
| 1105 | IRVSFTGKQGEMREM |
| 756 | SEKTFMPKQRSLQSL |
Function
Central component of cohesin, a complex required for chromosome cohesion during the cell cycle. The cohesin complex may form a large proteinaceous ring within which sister chromatids can be trapped. At anaphase, the complex is cleaved and dissociates from chromatin, allowing sister chromatids to segregate. Cohesion is coupled to DNA replication and is involved in DNA repair. The cohesin complex also plays an important role in spindle pole assembly during mitosis and in chromosomes movement
Protein Sequence
10
MYIKQVIIQG
20
FRSYRDQTIV
30
DPFSSKHNVI
40
VGRNGSGKSN
50
FFYAIQFVLS
60
DEFSHLRPEQ
70
RLALLHEGTG
80
PRVISAFVEI
90
IFDNSDNRLP
100
IDKEEVSLRR
110
VIGAKKDQYF
120
LDKKMVTKND
130
VMNLLESAGF
140
SRSNPYYIVK
150
QGKINQMATA
160
PDSQRLKLLR
170
EVAGTRVYDE
180
RKEESISLMK
190
ETEGKREKIN
200
ELLKYIEERL
210
HTLEEEKEEL
220
AQYQKWDKMR
230
RALEYTIYNQ
240
ELNETRAKLD
250
ELSAKRETSG
260
EKSRQLRDAQ
270
QDARDKMEDI
280
ERQVRELKTK
290
ISAMKEEKEQ
300
LSAERQEQIK
310
QRTKLELKAK
320
DLQDELAGNS
330
EQRKRLLKER
340
QKLLEKIEEK
350
QKELAETEPK
360
FNSVKEKEER
370
GIARLAQATQ
380
ERTDLYAKQG
390
RGSQFTSKED
400
RDKWIKKELK
410
SLDQAINDKK
420
RQIAAIHKDL
430
EDTEANKEKN
440
LEQYNKLDQD
450
LNEVKARVEE
460
LDRKYYEVKN
470
KKDELQSERN
480
YLWREENAEQ
490
QALAAKREDL
500
EKKQQLLRAA
510
TGKAILNGID
520
SINKVLDHFR
530
RKGINQHVQN
540
GYHGIVMNNF
550
ECEPAFYTCV
560
EVTAGNRLFY
570
HIVDSDEVST
580
KILMEFNKMN
590
LPGEVTFLPL
600
NKLDVRDTAY
610
PETNDAIPMI
620
SKLRYNPRFD
630
KAFKHVFGKT
640
LICRSMEVST
650
QLARAFTMDC
660
ITLEGDQVSH
670
RGALTGGYYD
680
TRKSRLELQK
690
DVRKAEEELG
700
ELEAKLNENL
710
RRNIERINNE
720
IDQLMNQMQQ
730
IETQQRKFKA
740
SRDSILSEMK
750
MLKEKRQQSE
760
KTFMPKQRSL
770
QSLEASLHAM
780
ESTRESLKAE
790
LGTDLLSQLS
800
LEDQKRVDAL
810
NDEIRQLQQE
820
NRQLLNERIK
830
LEGIITRVET
840
YLNENLRKRL
850
DQVEQELNEL
860
RETEGGTVLT
870
ATTSELEAIN
880
KRVKDTMARS
890
EDLDNSIDKT
900
EAGIKELQKS
910
MERWKNMEKE
920
HMDAINHDTK
930
ELEKMTNRQG
940
MLLKKKEECM
950
KKIRELGSLP
960
QEAFEKYQTL
970
SLKQLFRKLE
980
QCNTELKKYS
990
HVNKKALDQF
1000
VNFSEQKEKL
1010
IKRQEELDRG
1020
YKSIMELMNV
1030
LELRKYEAIQ
1040
LTFKQVSKNF
1050
SEVFQKLVPG
1060
GKATLVMKKG
1070
DVEGSQSQDE
1080
GEGSGESERG
1090
SGSQSSVPSV
1100
DQFTGVGIRV
1110
SFTGKQGEMR
1120
EMQQLSGGQK
1130
SLVALALIFA
1140
IQKCDPAPFY
1150
LFDEIDQALD
1160
AQHRKAVSDM
1170
IMELAVHAQF
1180
ITTTFRPELL
1190
ESADKFYGVK
1200
FRNKVSHIDV
1210
ITAEMAKDFV
EDDTTHG
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0000785 | chromatin |
| Cellular Component | GO:0000775 | chromosome, centromeric region |
| Cellular Component | GO:0000800 | lateral element |
| Cellular Component | GO:0030893 | meiotic cohesin complex |
| Cellular Component | GO:0097431 | mitotic spindle pole |
| Cellular Component | GO:0016363 | nuclear matrix |
| Cellular Component | GO:0005654 | nucleoplasm |
| Molecular Function | GO:0005524 | ATP binding |
| Molecular Function | GO:0016887 | ATP hydrolysis activity |
| Molecular Function | GO:0048487 | beta-tubulin binding |
| Molecular Function | GO:0003682 | chromatin binding |
| Molecular Function | GO:0000987 | cis-regulatory region sequence-specific DNA binding |
| Molecular Function | GO:0070840 | dynein complex binding |
| Molecular Function | GO:0036033 | mediator complex binding |
| Molecular Function | GO:0046982 | protein heterodimerization activity |
| Biological Process | GO:0051301 | cell division |
| Biological Process | GO:0006281 | DNA repair |
| Biological Process | GO:0051321 | meiotic cell cycle |
| Biological Process | GO:0090307 | mitotic spindle assembly |
| Biological Process | GO:0006275 | regulation of DNA replication |
| Biological Process | GO:0007062 | sister chromatid cohesion |
Reference
[1] Feng J, Chen X, Li R, Xie Y, Zhang X et al.. Lactylome analysis reveals potential target modified proteins in the retina of form-deprivation myopia.. iScience 27(9):110606. 2024 Sep 20. PMID: 39246443.