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Protein

Calmodulin-regulated spectrin-associated protein 3

Gene

Camsap3

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Microtubule minus-end binding protein that acts as a regulator of non-centrosomal microtubule dynamics and organization. Specifically required for the biogenesis and the maintenance of zonula adherens by anchoring the minus-end of microtubules to zonula adherens and by recruiting the kinesin KIFC3 to those junctional sites. May regulate the nucleation and the polymerization of microtubules. Indirectly, through the microtubule cytoskeleton, may regulate the organization of cellular organelles including the Golgi and the early endosomes.1 Publication

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
Calmodulin-regulated spectrin-associated protein 3
Alternative name(s):
Protein Nezha
Gene namesi
Name:Camsap3
Synonyms:Kiaa1543
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 8

Organism-specific databases

MGIiMGI:1916947. Camsap3.

Subcellular locationi

  • Cell junctionadherens junction By similarity
  • Cytoplasm By similarity
  • Cytoplasmcytoskeleton By similarity

  • Note: Scattered in the cytoplasm, associated with the minus-end of microtubules and also detected at the centrosomes. Localizes along zonula adherens only at mature cell-cell contacts (By similarity).By similarity

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • microtubule minus-end Source: UniProtKB
  • zonula adherens Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cytoplasm, Cytoskeleton, Microtubule

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 12521252Calmodulin-regulated spectrin-associated protein 3PRO_0000050800Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei184 – 1841PhosphothreonineBy similarity
Modified residuei193 – 1931PhosphoserineCombined sources
Modified residuei334 – 3341PhosphoserineBy similarity
Modified residuei347 – 3471PhosphoserineBy similarity
Modified residuei351 – 3511PhosphoserineCombined sources
Modified residuei368 – 3681PhosphoserineBy similarity
Modified residuei373 – 3731PhosphoserineBy similarity
Modified residuei382 – 3821PhosphoserineBy similarity
Modified residuei548 – 5481PhosphoserineBy similarity
Modified residuei555 – 5551PhosphoserineBy similarity
Modified residuei561 – 5611PhosphoserineBy similarity
Modified residuei683 – 6831PhosphoserineBy similarity
Modified residuei767 – 7671PhosphoserineBy similarity
Modified residuei797 – 7971PhosphothreonineCombined sources
Modified residuei812 – 8121PhosphoserineCombined sources
Modified residuei881 – 8811PhosphoserineCombined sources
Modified residuei1077 – 10771PhosphoserineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ80VC9.
PaxDbiQ80VC9.
PeptideAtlasiQ80VC9.
PRIDEiQ80VC9.

PTM databases

iPTMnetiQ80VC9.
PhosphoSiteiQ80VC9.

Expressioni

Gene expression databases

BgeeiQ80VC9.
CleanExiMM_2310057J16RIK.
ExpressionAtlasiQ80VC9. baseline and differential.
GenevisibleiQ80VC9. MM.

Interactioni

Subunit structurei

Interacts with PLEKHA7 (By similarity). Interacts with CAMSAP2.By similarity1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
Camsap2Q8C1B12EBI-2125556,EBI-8839434

GO - Molecular functioni

Protein-protein interaction databases

BioGridi213622. 1 interaction.
DIPiDIP-52404N.
IntActiQ80VC9. 3 interactions.
MINTiMINT-4112709.
STRINGi10090.ENSMUSP00000125993.

Structurei

Secondary structure

1
1252
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi1125 – 113410Combined sources
Turni1135 – 11373Combined sources
Helixi1143 – 115513Combined sources
Beta strandi1161 – 11699Combined sources
Beta strandi1171 – 11788Combined sources
Beta strandi1185 – 11928Combined sources
Beta strandi1194 – 11963Combined sources
Turni1198 – 12003Combined sources
Beta strandi1201 – 12088Combined sources
Turni1209 – 12124Combined sources
Beta strandi1213 – 12164Combined sources
Beta strandi1218 – 12214Combined sources
Beta strandi1227 – 12315Combined sources
Turni1234 – 12363Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1UGJNMR-A1113-1240[»]
ProteinModelPortaliQ80VC9.
SMRiQ80VC9. Positions 1111-1247.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ80VC9.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini163 – 312150CHAdd
BLAST
Domaini1112 – 1246135CKKPROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi496 – 54954Pro-richAdd
BLAST
Compositional biasi728 – 839112Pro-richAdd
BLAST

Domaini

The CKK domain binds microtubules.PROSITE-ProRule annotation

Sequence similaritiesi

Belongs to the CAMSAP1 family.PROSITE-ProRule annotation
Contains 1 CKK domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG3654. Eukaryota.
ENOG4111D0B. LUCA.
HOGENOMiHOG000059671.
InParanoidiQ80VC9.
KOiK17493.
OrthoDBiEOG7P8P6Z.
PhylomeDBiQ80VC9.

Family and domain databases

InterProiIPR032940. CAMSAP.
IPR031372. CAMSAP_CC1.
IPR022613. CAMSAP_CH.
IPR001715. CH-domain.
IPR014797. CKK_domain.
IPR011033. PRC_barrel-like.
[Graphical view]
PANTHERiPTHR21595. PTHR21595. 2 hits.
PfamiPF17095. CAMSAP_CC1. 1 hit.
PF11971. CAMSAP_CH. 1 hit.
PF08683. CAMSAP_CKK. 1 hit.
[Graphical view]
SMARTiSM01051. CAMSAP_CKK. 1 hit.
[Graphical view]
SUPFAMiSSF47576. SSF47576. 1 hit.
SSF50346. SSF50346. 1 hit.
PROSITEiPS51508. CKK. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q80VC9-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MVEAAPAGSG PLRRTFLVPE IKSLDQYDFS RAKAAASLAW VLRAAFGGAE
60 70 80 90 100
HVPPELWEPF YTDQYAQEHV KPPVTRLLLS AELYCRAWRQ ALPQLEPSPS
110 120 130 140 150
PSALLALLAR RGTVPSLPEH PVREADLKHQ PILMGAHLAV IDALMVAFSF
160 170 180 190 200
EWTKTLPGPL ALSSLEHKLL FWVDTTVRRL QEKTEQEAAQ RASPAAPLDG
210 220 230 240 250
ASPAQPSIRY RKDRAIARRA PCFPNVTTLQ DLASGAALAA TIHCYCPQLL
260 270 280 290 300
RLEEVCLKDP MSVADSLYNL QLVQDFCASH LPRGCPLSLE DLLYVPPPLK
310 320 330 340 350
VNLVVLLAEM YMCFEVLKPD FVQAKDLPDG HAVSPRNTET VPSQNNSGSS
360 370 380 390 400
SPVFNFRHPL LSPGGPQSPL RGSTGSLKSS PSMSHMEALG KAWNRQLSRP
410 420 430 440 450
LSQAVSFSTP FGLDSDVDVV MGDPVLLRSV SSDSLGPPRP VSTSSRNSAQ
460 470 480 490 500
PAPESGDLPT IEEALQIIHS AEPRLLPDGA ADGSFYLHSP EGLSKPPLSP
510 520 530 540 550
YPPEGASKPL SDRLNKAPIY ISHPENPSKS SPCSTGEILK PPPPSEGSPK
560 570 580 590 600
AVASSPAANN SEVKMTSFAE RKKQLVKAEA ESGLGSPTST PVAPEALSSE
610 620 630 640 650
MSELGARLEE KRRAIEAQKR RIEAIFAKHR QRLGKSAFLQ VQPREAAGEA
660 670 680 690 700
EEEAELGSVP GGERPAGEGQ GEPSLRHKSV TFSPDLGPVP PEGLGDYNRA
710 720 730 740 750
VSKLSAALSS LQRDMQRLTD QQQRLLAPPE APGPAPPPAA WVIPGPATGP
760 770 780 790 800
KAASPSPARR APAARRSPGP GPSPTPRSPK HARPAELKLA PLTRVLTPPH
810 820 830 840 850
DVDSLPHLRK FSPSQVPVQT RSSILLSEGT PPEEPTTKPA LIEIPLASLG
860 870 880 890 900
EPAADEEGDG SPPGAEDSLE EEASSEGEPR SGLGFFYKDE DKPEDEMAQK
910 920 930 940 950
RASLLERQQR RVEEARRRKQ WQEAEKEQKR EEAARLAQEA PGLAFTTPVV
960 970 980 990 1000
ASAAPVATLA PTTRAMAPAE EEVGPRRGDF TRLEYERRAQ LKLMDDLDKV
1010 1020 1030 1040 1050
LRPRASGTGG PGRGGRRATR PRSGCCDDSA LARSPARGLL GSRLSKVYSQ
1060 1070 1080 1090 1100
STLSLSTVAN EAPNNLGVKR PTSRAPSPSG LMSPSRLPGS RERDWENGSN
1110 1120 1130 1140 1150
ASSPASVPEY TGPRLYKEPS AKSNKFIIHN ALSHCCLAGK VNEPQKNRIL
1160 1170 1180 1190 1200
EEIEKSKANH FLILFRDSSC QFRALYTLSG ETEELSRLAG YGPRTVTPAM
1210 1220 1230 1240 1250
VEGIYKYNSD RKRFTQIPAK TMSMSVDAFT IQGHLWQSKK PTTPKKGGGT

PK
Length:1,252
Mass (Da):135,175
Last modified:June 1, 2003 - v1
Checksum:i1E14AA8640108CF4
GO
Isoform 2 (identifier: Q80VC9-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1042-1111: Missing.

Note: No experimental confirmation available.
Show »
Length:1,182
Mass (Da):127,774
Checksum:i0B344DA6F21D8D2F
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti199 – 2079DGASPAQPS → LTSLSSCPQ in BAD90256 (Ref. 3) Curated
Sequence conflicti892 – 8921K → E in BAC38313 (PubMed:16141072).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1042 – 111170Missing in isoform 2. 1 PublicationVSP_013705Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK081728 mRNA. Translation: BAC38313.1.
BC048787 mRNA. Translation: AAH48787.1.
AK220401 Transcribed RNA. Translation: BAD90256.1.
CCDSiCCDS22064.1. [Q80VC9-1]
RefSeqiNP_001157221.1. NM_001163749.1.
NP_081447.2. NM_027171.3. [Q80VC9-1]
UniGeneiMm.390010.

Genome annotation databases

EnsembliENSMUST00000057028; ENSMUSP00000058958; ENSMUSG00000044433. [Q80VC9-1]
GeneIDi69697.
KEGGimmu:69697.
UCSCiuc009krw.2. mouse. [Q80VC9-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK081728 mRNA. Translation: BAC38313.1.
BC048787 mRNA. Translation: AAH48787.1.
AK220401 Transcribed RNA. Translation: BAD90256.1.
CCDSiCCDS22064.1. [Q80VC9-1]
RefSeqiNP_001157221.1. NM_001163749.1.
NP_081447.2. NM_027171.3. [Q80VC9-1]
UniGeneiMm.390010.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1UGJNMR-A1113-1240[»]
ProteinModelPortaliQ80VC9.
SMRiQ80VC9. Positions 1111-1247.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi213622. 1 interaction.
DIPiDIP-52404N.
IntActiQ80VC9. 3 interactions.
MINTiMINT-4112709.
STRINGi10090.ENSMUSP00000125993.

PTM databases

iPTMnetiQ80VC9.
PhosphoSiteiQ80VC9.

Proteomic databases

MaxQBiQ80VC9.
PaxDbiQ80VC9.
PeptideAtlasiQ80VC9.
PRIDEiQ80VC9.

Protocols and materials databases

DNASUi69697.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000057028; ENSMUSP00000058958; ENSMUSG00000044433. [Q80VC9-1]
GeneIDi69697.
KEGGimmu:69697.
UCSCiuc009krw.2. mouse. [Q80VC9-1]

Organism-specific databases

CTDi57662.
MGIiMGI:1916947. Camsap3.
RougeiSearch...

Phylogenomic databases

eggNOGiKOG3654. Eukaryota.
ENOG4111D0B. LUCA.
HOGENOMiHOG000059671.
InParanoidiQ80VC9.
KOiK17493.
OrthoDBiEOG7P8P6Z.
PhylomeDBiQ80VC9.

Miscellaneous databases

EvolutionaryTraceiQ80VC9.
PROiQ80VC9.
SOURCEiSearch...

Gene expression databases

BgeeiQ80VC9.
CleanExiMM_2310057J16RIK.
ExpressionAtlasiQ80VC9. baseline and differential.
GenevisibleiQ80VC9. MM.

Family and domain databases

InterProiIPR032940. CAMSAP.
IPR031372. CAMSAP_CC1.
IPR022613. CAMSAP_CH.
IPR001715. CH-domain.
IPR014797. CKK_domain.
IPR011033. PRC_barrel-like.
[Graphical view]
PANTHERiPTHR21595. PTHR21595. 2 hits.
PfamiPF17095. CAMSAP_CC1. 1 hit.
PF11971. CAMSAP_CH. 1 hit.
PF08683. CAMSAP_CKK. 1 hit.
[Graphical view]
SMARTiSM01051. CAMSAP_CKK. 1 hit.
[Graphical view]
SUPFAMiSSF47576. SSF47576. 1 hit.
SSF50346. SSF50346. 1 hit.
PROSITEiPS51508. CKK. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Strain: C57BL/6J.
    Tissue: Head.
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Strain: FVB/N-3.
    Tissue: Mammary tumor.
  3. "Prediction of the coding sequences of mouse homologues of KIAA gene. The complete nucleotide sequences of mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
    Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O., Koga H.
    Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 198-1252 (ISOFORM 2).
    Tissue: Fetal brain.
  4. Lubec G., Sunyer B., Chen W.-Q.
    Submitted (JAN-2009) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 704-713, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: OF1.
    Tissue: Hippocampus.
  5. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-193; SER-351; THR-797; SER-812 AND SER-881, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Kidney, Liver, Lung, Pancreas and Testis.
  6. "Nezha/CAMSAP3 and CAMSAP2 cooperate in epithelial-specific organization of noncentrosomal microtubules."
    Tanaka N., Meng W., Nagae S., Takeichi M.
    Proc. Natl. Acad. Sci. U.S.A. 109:20029-20034(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH CAMSAP2.
  7. "Solution structure of a murine hypothetical protein from RIKEN cDNA 2310057j16."
    RIKEN structural genomics initiative (RSGI)
    Submitted (JUN-2003) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 1112-1240.

Entry informationi

Entry nameiCAMP3_MOUSE
AccessioniPrimary (citable) accession number: Q80VC9
Secondary accession number(s): Q5DTW9, Q8BUZ0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 15, 2005
Last sequence update: June 1, 2003
Last modified: July 6, 2016
This is version 122 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.