Overview
| Uniprot ID | Q5T5Y3 |
| Protein Name | Calmodulin-regulated spectrin-associated protein 1 |
| Gene Name | CAMSAP1 |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position |
Flanking peptide |
| 1315 |
LEAEVELKRDEARRK |
| 222 |
LESPAHQKVRYRREH |
| 49 |
NLQWICAKAYGRDNI |
Function
Key microtubule-organizing protein that specifically binds the minus-end of non-centrosomal microtubules and regulates their dynamics and organization (PubMed:19508979, PubMed:21834987, PubMed:24117850, PubMed:24486153, PubMed:24706919). Specifically recognizes growing microtubule minus-ends and stabilizes microtubules (PubMed:24486153, PubMed:24706919). Acts on free microtubule minus-ends that are not capped by microtubule-nucleating proteins or other factors and protects microtubule minus-ends from depolymerization (PubMed:24486153, PubMed:24706919). In contrast to CAMSAP2 and CAMSAP3, tracks along the growing tips of minus-end microtubules without significantly affecting the polymerization rate: binds at the very tip of the microtubules minus-end and acts as a minus-end tracking protein (-TIP) that dissociates from microtubules after allowing tubulin incorporation (PubMed:24486153, PubMed:24706919). Through interaction with spectrin may regulate neurite outgrowth (PubMed:24117850)
Protein Sequence
10
MVDASGRAAA
20
EGWRKMEAPP
30
DGAADLVPLD
40
RYDAARAKIA
50
ANLQWICAKA
60
YGRDNIPEDL
70
RDPFYVDQYE
80
QEHIKPPVIK
90
LLLSSELYCR
100
VCSLILKGDQ
110
VAALQGHQSV
120
IQALSRKGIY
130
VMESDDTPVT
140
ESDLSRAPIK
150
MSAHMAMVDA
160
LMMAYTVEMI
170
SIEKVVASVK
180
RFSTFSASKE
190
LPYDLEDAMV
200
FWINKVNLKM
210
REITEKEVKL
220
KQQLLESPAH
230
QKVRYRREHL
240
SARQSPYFPL
250
LEDLMRDGSD
260
GAALLAVIHY
270
YCPEQMKLDD
280
ICLKEVTSMA
290
DSLYNIRLLR
300
EFSNEYLNKC
310
FYLTLEDMLY
320
APLVLKPNVM
330
VFIAELFWWF
340
ENVKPDFVQP
350
RDVQELKDAK
360
TVLHQKSSRP
370
PVPISNATKR
380
SFLGSPAAGT
390
LAELQPPVQL
400
PAEGCHRHYL
410
HPEEPEYLGK
420
GTAAFSPSHP
430
LLPLRQKQQK
440
SIQGEDIPDQ
450
RHRSNSLTRV
460
DGQPRGAAIA
470
WPEKKTRPAS
480
QPTPFALHHA
490
ASCEVDPSSG
500
DSISLARSIS
510
KDSLASNIVN
520
LTPQNQPHPT
530
ATKSHGKSLL
540
SNVSIEDEEE
550
ELVAIVRADV
560
VPQQADPEFP
570
RASPRALGLT
580
ANARSPQGQL
590
DTSESKPDSF
600
FLEPLMPAVL
610
KPAKEKQVIT
620
KEDERGEGRP
630
RSIVSRRPSE
640
GPQPLVRRKM
650
TGSRDLNRTF
660
TPIPCSEFPM
670
GIDPTETGPL
680
SVETAGEVCG
690
GPLALGGFDP
700
FPQGPSTDGF
710
FLHVGRADED
720
TEGRLYVSCS
730
KSPNSHDSEP
740
WTLLRQDSDS
750
DVVDIEEAEH
760
DFMGEAHPVV
770
FSRYIGEEES
780
AKLQEDMKVK
790
EHEDKDDASG
800
RSSPCLSTAS
810
QMSSVSMASG
820
SVKMTSFAER
830
KLQRLNSCET
840
KSSTSSSQKT
850
TPDASESCPA
860
PLTTWRQKRE
870
QSPSQHGKDP
880
ASLLASELVQ
890
LHMQLEEKRR
900
AIEAQKKKME
910
ALSARQRLKL
920
GKAAFLHVVK
930
KGKAEAAPPL
940
RPEHFAKEYS
950
QHNGEDCGDA
960
VSKTEDFLVK
970
EEQREELLHE
980
PQDVDKESLA
990
FAQQHKAKDP
1000
VALHELERNK
1010
VISAALLEDT
1020
VGEVVDVNEC
1030
DLSIEKLNET
1040
ISTLQQAILK
1050
ISQQQEQLLM
1060
KSPTVPVPGS
1070
KNNSQDHKVK
1080
APVHFVEPLS
1090
PTGVAGHRKA
1100
PRLGQGRNSR
1110
SGRPAELKVP
1120
KDRPQGSSRS
1130
KTPTPSVETL
1140
PHLRPFPASS
1150
HPRTPTDPGL
1160
DSALEPSGDP
1170
HGKCLFDSYR
1180
LHDESNQRTL
1190
TLSSSKDANI
1200
LSEQMSLKEV
1210
LDASVKEVGS
1220
SSSDVSGKES
1230
VPVEEPLRSR
1240
ASLIEVDLSD
1250
LKAPDEDGEL
1260
VSLDGSADLV
1270
SEGDQKPGVG
1280
FFFKDEQKAE
1290
DELAKKRAAF
1300
LLKQQRKAEE
1310
ARVRKQQLEA
1320
EVELKRDEAR
1330
RKAEEDRVRK
1340
EEEKARRELI
1350
KQEYLRRKQQ
1360
QILEEQGLGK
1370
PKSKPKKPRP
1380
KSVHREESCS
1390
DSGTKCSSTP
1400
DNLSRTQSGS
1410
SLSLASAATT
1420
EPESVHSGGT
1430
PSQRVESMEA
1440
LPILSRNPSR
1450
STDRDWETAS
1460
AASSLASVAE
1470
YTGPKLFKEP
1480
SSKSNKPIIH
1490
NAISHCCLAG
1500
KVNEPHKNSI
1510
LEELEKCDAN
1520
HYIILFRDAG
1530
CQFRALYCYY
1540
PDTEEIYKLT
1550
GTGPKNITKK
1560
MIDKLYKYSS
1570
DRKQFNLIPA
1580
KTMSVSVDAL
1590
TIHNHLWQPK
1600
RPAVPKKAQT
RK
Gene Ontology
| Classification |
GO ID |
Description |
| Cellular Component |
GO:0005829 |
cytosol |
| Cellular Component |
GO:0005874 |
microtubule |
| Cellular Component |
GO:0072686 |
mitotic spindle |
| Molecular Function |
GO:0005516 |
calmodulin binding |
| Molecular Function |
GO:0008017 |
microtubule binding |
| Molecular Function |
GO:0051011 |
microtubule minus-end binding |
| Molecular Function |
GO:0030507 |
spectrin binding |
| Biological Process |
GO:0000226 |
microtubule cytoskeleton organization |
| Biological Process |
GO:0031175 |
neuron projection development |
| Biological Process |
GO:0031113 |
regulation of microtubule polymerization |
Reference
[1] Cheng Z, Huang H, Li M, Chen Y. Proteomic analysis identifies PFKP lactylation in SW480 colon cancer cells.. iScience 27(1):108645. 2024 Jan 19. PMID: 38155775.
[2] He C, Zhang J, Bai X, Lu C, Zhang K. Lysine lactylation-based insight to understanding the characterization of cervical cancer.. Biochim Biophys Acta Mol Basis Dis 1870(7):167356. 2024 Oct. PMID: 39025375.