CAMP2_HUMAN
ID CAMP2_HUMAN Reviewed; 1489 AA.
AC Q08AD1; B1APG6; Q08AD2; Q6PGN8; Q96FB3; Q9UG20; Q9UPS4;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-OCT-2010, sequence version 3.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Calmodulin-regulated spectrin-associated protein 2 {ECO:0000305};
DE AltName: Full=Calmodulin-regulated spectrin-associated protein 1-like protein 1;
GN Name=CAMSAP2 {ECO:0000312|HGNC:HGNC:29188};
GN Synonyms=CAMSAP1L1 {ECO:0000312|HGNC:HGNC:29188},
GN KIAA1078 {ECO:0000303|PubMed:10470851};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Eye;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 125-1489 (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=10470851; DOI=10.1093/dnares/6.3.197;
RA Kikuno R., Nagase T., Ishikawa K., Hirosawa M., Miyajima N., Tanaka A.,
RA Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XIV. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 6:197-205(1999).
RN [5]
RP SEQUENCE REVISION.
RX PubMed=12168954; DOI=10.1093/dnares/9.3.99;
RA Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
RT "Construction of expression-ready cDNA clones for KIAA genes: manual
RT curation of 330 KIAA cDNA clones.";
RL DNA Res. 9:99-106(2002).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1288-1489 (ISOFORM 1).
RC TISSUE=Uterus;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-931; SER-936; SER-1313 AND
RP SER-1319, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-464; SER-598; SER-599;
RP SER-673; SER-931; SER-936; THR-997; THR-1002; THR-1004; SER-1008; SER-1019;
RP SER-1313 AND SER-1319, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-464; SER-599; SER-931;
RP SER-936; SER-1148 AND SER-1319, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-464 AND SER-599, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [15]
RP POSSIBLE INVOLVEMENT IN EPILEPSY.
RX PubMed=22116939; DOI=10.1093/hmg/ddr550;
RA Guo Y., Baum L.W., Sham P.C., Wong V., Ng P.W., Lui C.H., Sin N.C.,
RA Tsoi T.H., Tang C.S., Kwan J.S., Yip B.H., Xiao S.M., Thomas G.N.,
RA Lau Y.L., Yang W., Cherny S.S., Kwan P.;
RT "Two-stage genome-wide association study identifies variants in CAMSAP1L1
RT as susceptibility loci for epilepsy in Chinese.";
RL Hum. Mol. Genet. 21:1184-1189(2012).
RN [16]
RP FUNCTION, MICROTUBULE-BINDING, AND SUBCELLULAR LOCATION.
RX PubMed=23169647; DOI=10.1073/pnas.1218017109;
RA Tanaka N., Meng W., Nagae S., Takeichi M.;
RT "Nezha/CAMSAP3 and CAMSAP2 cooperate in epithelial-specific organization of
RT noncentrosomal microtubules.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:20029-20034(2012).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-416; SER-464; SER-599;
RP SER-673; SER-862; SER-931; SER-1148; SER-1313; SER-1319 AND SER-1321, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [18]
RP FUNCTION, SUBCELLULAR LOCATION, DOMAIN, AND INTERACTION WITH KATNA1 AND
RP KATNB1.
RX PubMed=24486153; DOI=10.1016/j.devcel.2014.01.001;
RA Jiang K., Hua S., Mohan R., Grigoriev I., Yau K.W., Liu Q., Katrukha E.A.,
RA Altelaar A.F., Heck A.J., Hoogenraad C.C., Akhmanova A.;
RT "Microtubule minus-end stabilization by polymerization-driven CAMSAP
RT deposition.";
RL Dev. Cell 28:295-309(2014).
RN [19]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=24908486; DOI=10.1016/j.neuron.2014.04.019;
RA Yau K.W., van Beuningen S.F., Cunha-Ferreira I., Cloin B.M.,
RA van Battum E.Y., Will L., Schaetzle P., Tas R.P., van Krugten J.,
RA Katrukha E.A., Jiang K., Wulf P.S., Mikhaylova M., Harterink M.,
RA Pasterkamp R.J., Akhmanova A., Kapitein L.C., Hoogenraad C.C.;
RT "Microtubule minus-end binding protein CAMSAP2 controls axon specification
RT and dendrite development.";
RL Neuron 82:1058-1073(2014).
RN [20]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=24706919; DOI=10.1073/pnas.1404133111;
RA Hendershott M.C., Vale R.D.;
RT "Regulation of microtubule minus-end dynamics by CAMSAPs and Patronin.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:5860-5865(2014).
RN [21]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH AKAP9 AND PDE4DIP.
RX PubMed=27666745; DOI=10.1016/j.devcel.2016.08.009;
RA Wu J., de Heus C., Liu Q., Bouchet B.P., Noordstra I., Jiang K., Hua S.,
RA Martin M., Yang C., Grigoriev I., Katrukha E.A., Altelaar A.F.,
RA Hoogenraad C.C., Qi R.Z., Klumperman J., Akhmanova A.;
RT "Molecular pathway of microtubule organization at the Golgi apparatus.";
RL Dev. Cell 39:44-60(2016).
RN [22]
RP FUNCTION, AND INTERACTION WITH MAPRE1.
RX PubMed=28726242; DOI=10.1002/1873-3468.12758;
RA Wei J., Xu H., Meng W.;
RT "Noncentrosomal microtubules regulate autophagosome transport through
RT CAMSAP2-EB1 cross-talk.";
RL FEBS Lett. 591:2379-2393(2017).
RN [23]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH MAPRE1; AKAP9 AND PDE4DIP.
RX PubMed=28814570; DOI=10.1083/jcb.201701024;
RA Yang C., Wu J., de Heus C., Grigoriev I., Liv N., Yao Y., Smal I.,
RA Meijering E., Klumperman J., Qi R.Z., Akhmanova A.;
RT "EB1 and EB3 regulate microtubule minus end organization and Golgi
RT morphology.";
RL J. Cell Biol. 216:3179-3198(2017).
RN [24]
RP VARIANT [LARGE SCALE ANALYSIS] LEU-361.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: Key microtubule-organizing protein that specifically binds
CC the minus-end of non-centrosomal microtubules and regulates their
CC dynamics and organization (PubMed:23169647, PubMed:24486153,
CC PubMed:24706919). Specifically recognizes growing microtubule minus-
CC ends and autonomously decorates and stabilizes microtubule lattice
CC formed by microtubule minus-end polymerization (PubMed:24486153,
CC PubMed:24706919). Acts on free microtubule minus-ends that are not
CC capped by microtubule-nucleating proteins or other factors and protects
CC microtubule minus-ends from depolymerization (PubMed:24486153,
CC PubMed:24706919). In addition, it also reduces the velocity of
CC microtubule polymerization (PubMed:24486153, PubMed:24706919). Through
CC the microtubule cytoskeleton, also regulates the organization of
CC cellular organelles including the Golgi and the early endosomes
CC (PubMed:27666745). Essential for the tethering, but not for nucleation
CC of non-centrosomal microtubules at the Golgi: together with Golgi-
CC associated proteins AKAP9 and PDE4DIP, required to tether non-
CC centrosomal minus-end microtubules to the Golgi, an important step for
CC polarized cell movement (PubMed:27666745). Also acts as a regulator of
CC neuronal polarity and development: localizes to non-centrosomal
CC microtubule minus-ends in neurons and stabilizes non-centrosomal
CC microtubules, which is required for neuronal polarity, axon
CC specification and dendritic branch formation (PubMed:24908486). Through
CC the microtubule cytoskeleton, regulates the autophagosome transport
CC (PubMed:28726242). {ECO:0000269|PubMed:23169647,
CC ECO:0000269|PubMed:24486153, ECO:0000269|PubMed:24706919,
CC ECO:0000269|PubMed:24908486, ECO:0000269|PubMed:27666745,
CC ECO:0000269|PubMed:28726242}.
CC -!- SUBUNIT: Interacts with CAMSAP3 (By similarity). Interacts with KATNA1
CC and KATNB1; leading to regulate the length of CAMSAP2-decorated
CC microtubule stretches (PubMed:24486153). Interacts with a complex
CC formed by AKAP9 and PDE4DIP isoform 13/MMG8/SMYLE, which recruits
CC CAMSAP2 to the Golgi (PubMed:27666745, PubMed:28814570). Interacts with
CC MAPRE1/EB1 (PubMed:28726242, PubMed:28814570).
CC {ECO:0000250|UniProtKB:Q8C1B1, ECO:0000269|PubMed:24486153,
CC ECO:0000269|PubMed:27666745, ECO:0000269|PubMed:28726242,
CC ECO:0000269|PubMed:28814570}.
CC -!- INTERACTION:
CC Q08AD1; P29692: EEF1D; NbExp=2; IntAct=EBI-1051869, EBI-358607;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:23169647, ECO:0000269|PubMed:24486153,
CC ECO:0000269|PubMed:24706919, ECO:0000269|PubMed:24908486,
CC ECO:0000269|PubMed:27666745, ECO:0000269|PubMed:28814570}. Golgi
CC apparatus {ECO:0000269|PubMed:27666745}. Cytoplasm, cytoskeleton,
CC cilium basal body {ECO:0000250|UniProtKB:Q8C1B1}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q8C1B1}. Note=Associated with the minus-end of
CC microtubules and also detected at the centrosomes (PubMed:23169647,
CC PubMed:24486153, PubMed:24908486, PubMed:24706919, PubMed:27666745,
CC PubMed:28814570). Decorates the minus-end of microtubules by decreasing
CC the rate of tubulin incorporation and remaining bound
CC (PubMed:24486153). The length of CAMSAP2-decorated stretches on the
CC minus-end of microtubules depends on MAPRE1/EB1 and MAPRE3/EB3, which
CC promote elongation of CAMSAP2-decorated microtubule stretches
CC (PubMed:28814570). Recruited to the Golgi apparatus by AKAP9 and
CC PDE4DIP isoform 13/MMG8/SMYLE (PubMed:27666745). In neurons, localizes
CC to the minus-end of microtubules in axon and dendrites
CC (PubMed:24908486). {ECO:0000269|PubMed:23169647,
CC ECO:0000269|PubMed:24486153, ECO:0000269|PubMed:24706919,
CC ECO:0000269|PubMed:27666745, ECO:0000269|PubMed:28814570}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q08AD1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q08AD1-2; Sequence=VSP_030805, VSP_030806;
CC Name=3;
CC IsoId=Q08AD1-3; Sequence=VSP_030805;
CC -!- DOMAIN: The CKK domain binds microtubules and specifically recognizes
CC the minus-end of microtubules (PubMed:24486153). {ECO:0000255|PROSITE-
CC ProRule:PRU00841, ECO:0000269|PubMed:24486153}.
CC -!- DOMAIN: The MBD (microtubule-binding domain) region can recognize some
CC features of the microtubule lattice, which might contribute to the
CC specific decoration of growing microtubule minus-ends by CAMSAP2.
CC {ECO:0000269|PubMed:24486153}.
CC -!- DISEASE: Note=Defects in CAMSAP2 may be a cause of susceptibility to
CC epilepsy in the Chinese population. {ECO:0000305|PubMed:22116939}.
CC -!- SIMILARITY: Belongs to the CAMSAP1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU00841}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH56910.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AL450104; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471067; EAW91320.1; -; Genomic_DNA.
DR EMBL; BC011385; AAH11385.1; -; mRNA.
DR EMBL; BC056910; AAH56910.1; ALT_INIT; mRNA.
DR EMBL; BC125229; AAI25230.1; -; mRNA.
DR EMBL; BC125230; AAI25231.1; -; mRNA.
DR EMBL; AB029001; BAA83030.2; -; mRNA.
DR EMBL; AL110158; CAB53664.2; -; mRNA.
DR CCDS; CCDS1404.1; -. [Q08AD1-3]
DR CCDS; CCDS72998.1; -. [Q08AD1-1]
DR CCDS; CCDS72999.1; -. [Q08AD1-2]
DR PIR; T14744; T14744.
DR RefSeq; NP_001284636.1; NM_001297707.1. [Q08AD1-1]
DR RefSeq; NP_001284637.1; NM_001297708.1. [Q08AD1-2]
DR RefSeq; NP_982284.1; NM_203459.2. [Q08AD1-3]
DR AlphaFoldDB; Q08AD1; -.
DR SMR; Q08AD1; -.
DR BioGRID; 116872; 151.
DR IntAct; Q08AD1; 35.
DR MINT; Q08AD1; -.
DR STRING; 9606.ENSP00000236925; -.
DR GlyGen; Q08AD1; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q08AD1; -.
DR PhosphoSitePlus; Q08AD1; -.
DR BioMuta; CAMSAP2; -.
DR DMDM; 308153626; -.
DR EPD; Q08AD1; -.
DR jPOST; Q08AD1; -.
DR MassIVE; Q08AD1; -.
DR MaxQB; Q08AD1; -.
DR PaxDb; Q08AD1; -.
DR PeptideAtlas; Q08AD1; -.
DR PRIDE; Q08AD1; -.
DR ProteomicsDB; 58654; -. [Q08AD1-1]
DR ProteomicsDB; 58655; -. [Q08AD1-2]
DR ProteomicsDB; 58656; -. [Q08AD1-3]
DR Antibodypedia; 20635; 79 antibodies from 19 providers.
DR DNASU; 23271; -.
DR Ensembl; ENST00000236925.8; ENSP00000236925.4; ENSG00000118200.15. [Q08AD1-1]
DR Ensembl; ENST00000358823.7; ENSP00000351684.2; ENSG00000118200.15. [Q08AD1-3]
DR Ensembl; ENST00000413307.6; ENSP00000416800.2; ENSG00000118200.15. [Q08AD1-2]
DR GeneID; 23271; -.
DR KEGG; hsa:23271; -.
DR MANE-Select; ENST00000358823.7; ENSP00000351684.2; NM_203459.4; NP_982284.1. [Q08AD1-3]
DR UCSC; uc001gvk.4; human. [Q08AD1-1]
DR CTD; 23271; -.
DR DisGeNET; 23271; -.
DR GeneCards; CAMSAP2; -.
DR HGNC; HGNC:29188; CAMSAP2.
DR HPA; ENSG00000118200; Low tissue specificity.
DR MIM; 613775; gene.
DR neXtProt; NX_Q08AD1; -.
DR OpenTargets; ENSG00000118200; -.
DR PharmGKB; PA142672206; -.
DR VEuPathDB; HostDB:ENSG00000118200; -.
DR eggNOG; KOG3654; Eukaryota.
DR GeneTree; ENSGT00950000182975; -.
DR HOGENOM; CLU_004833_1_0_1; -.
DR InParanoid; Q08AD1; -.
DR OMA; KVITCAQ; -.
DR PhylomeDB; Q08AD1; -.
DR TreeFam; TF315529; -.
DR PathwayCommons; Q08AD1; -.
DR SignaLink; Q08AD1; -.
DR BioGRID-ORCS; 23271; 27 hits in 1072 CRISPR screens.
DR ChiTaRS; CAMSAP2; human.
DR GenomeRNAi; 23271; -.
DR Pharos; Q08AD1; Tbio.
DR PRO; PR:Q08AD1; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q08AD1; protein.
DR Bgee; ENSG00000118200; Expressed in lateral nuclear group of thalamus and 207 other tissues.
DR ExpressionAtlas; Q08AD1; baseline and differential.
DR Genevisible; Q08AD1; HS.
DR GO; GO:0036064; C:ciliary basal body; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:1990752; C:microtubule end; IDA:HPA.
DR GO; GO:0005516; F:calmodulin binding; IEA:InterPro.
DR GO; GO:0051011; F:microtubule minus-end binding; IDA:UniProtKB.
DR GO; GO:0030507; F:spectrin binding; IEA:InterPro.
DR GO; GO:0061564; P:axon development; IDA:UniProtKB.
DR GO; GO:0031122; P:cytoplasmic microtubule organization; IBA:GO_Central.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; IDA:UniProtKB.
DR GO; GO:0007026; P:negative regulation of microtubule depolymerization; IBA:GO_Central.
DR GO; GO:0050773; P:regulation of dendrite development; IDA:UniProtKB.
DR GO; GO:1903358; P:regulation of Golgi organization; IDA:UniProtKB.
DR GO; GO:0031113; P:regulation of microtubule polymerization; IDA:UniProtKB.
DR GO; GO:0033043; P:regulation of organelle organization; IMP:UniProtKB.
DR Gene3D; 3.10.20.360; -; 1.
DR InterPro; IPR032940; CAMSAP.
DR InterPro; IPR022613; CAMSAP-like_CH_dom.
DR InterPro; IPR031372; CAMSAP_CC1.
DR InterPro; IPR001715; CH-domain.
DR InterPro; IPR036872; CH_dom_sf.
DR InterPro; IPR038209; CKK_dom_sf.
DR InterPro; IPR014797; CKK_domain.
DR InterPro; IPR011033; PRC_barrel-like_sf.
DR PANTHER; PTHR21595; PTHR21595; 1.
DR Pfam; PF17095; CAMSAP_CC1; 1.
DR Pfam; PF11971; CAMSAP_CH; 1.
DR Pfam; PF08683; CAMSAP_CKK; 1.
DR SMART; SM01051; CAMSAP_CKK; 1.
DR SUPFAM; SSF47576; SSF47576; 1.
DR SUPFAM; SSF50346; SSF50346; 1.
DR PROSITE; PS50021; CH; 1.
DR PROSITE; PS51508; CKK; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell projection; Coiled coil; Cytoplasm;
KW Cytoskeleton; Golgi apparatus; Microtubule; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..1489
FT /note="Calmodulin-regulated spectrin-associated protein 2"
FT /id="PRO_0000316832"
FT DOMAIN 222..335
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT DOMAIN 1349..1483
FT /note="CKK"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00841"
FT REGION 375..415
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 611..639
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 668..730
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 812..844
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 922..1034
FT /note="MBD region"
FT /evidence="ECO:0000269|PubMed:24486153"
FT REGION 925..1017
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1032..1078
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1096..1152
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1191..1349
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 756..793
FT /evidence="ECO:0000255"
FT COILED 887..926
FT /evidence="ECO:0000255"
FT COILED 1166..1238
FT /evidence="ECO:0000255"
FT COMPBIAS 670..699
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 712..728
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 925..943
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 953..1007
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1038..1077
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1102..1116
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1131..1152
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1191..1250
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1286..1302
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1330..1346
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 416
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 418
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8C1B1"
FT MOD_RES 426
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8C1B1"
FT MOD_RES 464
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 598
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 599
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 611
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8C1B1"
FT MOD_RES 673
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 678
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8C1B1"
FT MOD_RES 680
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8C1B1"
FT MOD_RES 862
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 931
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 936
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231"
FT MOD_RES 997
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 1002
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 1004
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 1008
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 1019
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 1148
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1313
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163"
FT MOD_RES 1319
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1321
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 216..226
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_030805"
FT VAR_SEQ 380..395
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_030806"
FT VARIANT 361
FT /note="I -> L (in a colorectal cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_038399"
FT VARIANT 958
FT /note="P -> L (in dbSNP:rs3753952)"
FT /id="VAR_038400"
FT VARIANT 969
FT /note="P -> L (in dbSNP:rs3753952)"
FT /id="VAR_057796"
FT VARIANT 1028
FT /note="R -> P (in dbSNP:rs6674599)"
FT /id="VAR_038401"
FT VARIANT 1039
FT /note="P -> R (in dbSNP:rs6674599)"
FT /id="VAR_057797"
FT CONFLICT 150
FT /note="E -> K (in Ref. 4; BAA83030)"
FT /evidence="ECO:0000305"
FT CONFLICT 1261
FT /note="Q -> K (in Ref. 3; AAH56910)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1489 AA; 168089 MW; 4E20A240E2691027 CRC64;
MGDAADPREM RKTFIVPAIK PFDHYDFSRA KIACNLAWLV AKAFGTENVP EELQEPFYTD
QYDQEHIKPP VVNLLLSAEL YCRAGSLILK SDAAKPLLGH DAVIQALAQK GLYVTDQEKL
VTERDLHKKP IQMSAHLAMI DTLMMAYTVE MVSIEKVIAC AQQYSAFFQA TDLPYDIEDA
VMYWINKVNE HLKDIMEQEQ KLKEHHTVEA PGGQKSPSKW FWKLVPARYR KEQTLLKQLP
CIPLVENLLK DGTDGCALAA LIHFYCPDVV RLEDICLKET MSLADSLYNL QLIQEFCQEY
LNQCCHFTLE DMLYAASSIK SNYLVFMAEL FWWFEVVKPS FVQPRVVRPQ GAEPVKDMPS
IPVLNAAKRN VLDSSSDFPS SGEGATFTQS HHHLPSRYSR PQAHSSASGG IRRSSSMSYV
DGFIGTWPKE KRSSVHGVSF DISFDKEDSV QRSTPNRGIT RSISNEGLTL NNSHVSKHIR
KNLSFKPING EEEAESIEEE LNIDSHSDLK SCVPLNTNEL NSNENIHYKL PNGALQNRIL
LDEFGNQIET PSIEEALQII HDTEKSPHTP QPDQIANGFF LHSQEMSILN SNIKLNQSSP
DNVTDTKGAL SPITDNTEVD TGIHVPSEDI PETMDEDSSL RDYTVSLDSD MDDASKFLQD
YDIRTGNTRE ALSPCPSTVS TKSQPGSSAS SSSGVKMTSF AEQKFRKLNH TDGKSSGSSS
QKTTPEGSEL NIPHVVAWAQ IPEETGLPQG RDTTQLLASE MVHLRMKLEE KRRAIEAQKK
KMEAAFTKQR QKMGRTAFLT VVKKKGDGIS PLREEAAGAE DEKVYTDRAK EKESQKTDGQ
RSKSLADIKE SMENPQAKWL KSPTTPIDPE KQWNLASPSE ETLNEGEILE YTKSIEKLNS
SLHFLQQEMQ RLSLQQEMLM QMREQQSWVI SPPQPSPQKQ IRDFKPSKQA GLSSAIAPFS
SDSPRPTHPS PQSSNRKSAS FSVKSQRTPR PNELKITPLN RTLTPPRSVD SLPRLRRFSP
SQVPIQTRSF VCFGDDGEPQ LKESKPKEEV KKEELESKGT LEQRGHNPEE KEIKPFESTV
SEVLSLPVTE TVCLTPNEDQ LNQPTEPPPK PVFPPTAPKN VNLIEVSLSD LKPPEKADVP
VEKYDGESDK EQFDDDQKVC CGFFFKDDQK AENDMAMKRA ALLEKRLRRE KETQLRKQQL
EAEMEHKKEE TRRKTEEERQ KKEDERARRE FIRQEYMRRK QLKLMEDMDT VIKPRPQVVK
QKKQRPKSIH RDHIESPKTP IKGPPVSSLS LASLNTGDNE SVHSGKRTPR SESVEGFLSP
SRCGSRNGEK DWENASTTSS VASGTEYTGP KLYKEPSAKS NKHIIQNALA HCCLAGKVNE
GQKKKILEEM EKSDANNFLI LFRDSGCQFR SLYTYCPETE EINKLTGIGP KSITKKMIEG
LYKYNSDRKQ FSHIPAKTLS ASVDAITIHS HLWQTKRPVT PKKLLPTKA
