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Calmodulin-regulated spectrin-associated protein 2 (Calmodulin-regulated spectrin-associated protein 1-like protein 1)

 CAMP2_HUMAN             Reviewed;        1489 AA.
Q08AD1; B1APG6; Q08AD2; Q6PGN8; Q96FB3; Q9UG20; Q9UPS4;
26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
05-OCT-2010, sequence version 3.
18-JUL-2018, entry version 111.
RecName: Full=Calmodulin-regulated spectrin-associated protein 2 {ECO:0000305};
AltName: Full=Calmodulin-regulated spectrin-associated protein 1-like protein 1;
Name=CAMSAP2 {ECO:0000312|HGNC:HGNC:29188};
Synonyms=CAMSAP1L1 {ECO:0000312|HGNC:HGNC:29188},
KIAA1078 {ECO:0000303|PubMed:10470851};
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Eye;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 125-1489 (ISOFORM 1).
TISSUE=Brain;
PubMed=10470851; DOI=10.1093/dnares/6.3.197;
Kikuno R., Nagase T., Ishikawa K., Hirosawa M., Miyajima N.,
Tanaka A., Kotani H., Nomura N., Ohara O.;
"Prediction of the coding sequences of unidentified human genes. XIV.
The complete sequences of 100 new cDNA clones from brain which code
for large proteins in vitro.";
DNA Res. 6:197-205(1999).
[5]
SEQUENCE REVISION.
PubMed=12168954; DOI=10.1093/dnares/9.3.99;
Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
"Construction of expression-ready cDNA clones for KIAA genes: manual
curation of 330 KIAA cDNA clones.";
DNA Res. 9:99-106(2002).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1288-1489 (ISOFORM 1).
TISSUE=Uterus;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-931; SER-936; SER-1313
AND SER-1319, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=16964243; DOI=10.1038/nbt1240;
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
"A probability-based approach for high-throughput protein
phosphorylation analysis and site localization.";
Nat. Biotechnol. 24:1285-1292(2006).
[8]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18220336; DOI=10.1021/pr0705441;
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,
Yates J.R. III;
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
efficient phosphoproteomic analysis.";
J. Proteome Res. 7:1346-1351(2008).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-464; SER-598; SER-599;
SER-673; SER-931; SER-936; THR-997; THR-1002; THR-1004; SER-1008;
SER-1019; SER-1313 AND SER-1319, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[11]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-464; SER-599; SER-931;
SER-936; SER-1148 AND SER-1319, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[13]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-464 AND SER-599, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[15]
POSSIBLE INVOLVEMENT IN EPILEPSY.
PubMed=22116939; DOI=10.1093/hmg/ddr550;
Guo Y., Baum L.W., Sham P.C., Wong V., Ng P.W., Lui C.H., Sin N.C.,
Tsoi T.H., Tang C.S., Kwan J.S., Yip B.H., Xiao S.M., Thomas G.N.,
Lau Y.L., Yang W., Cherny S.S., Kwan P.;
"Two-stage genome-wide association study identifies variants in
CAMSAP1L1 as susceptibility loci for epilepsy in Chinese.";
Hum. Mol. Genet. 21:1184-1189(2012).
[16]
FUNCTION, MICROTUBULE-BINDING, AND SUBCELLULAR LOCATION.
PubMed=23169647; DOI=10.1073/pnas.1218017109;
Tanaka N., Meng W., Nagae S., Takeichi M.;
"Nezha/CAMSAP3 and CAMSAP2 cooperate in epithelial-specific
organization of noncentrosomal microtubules.";
Proc. Natl. Acad. Sci. U.S.A. 109:20029-20034(2012).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-416; SER-464; SER-599;
SER-673; SER-862; SER-931; SER-1148; SER-1313; SER-1319 AND SER-1321,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[18]
FUNCTION, SUBCELLULAR LOCATION, DOMAIN, AND INTERACTION WITH KATNA1
AND KATNB1.
PubMed=24486153; DOI=10.1016/j.devcel.2014.01.001;
Jiang K., Hua S., Mohan R., Grigoriev I., Yau K.W., Liu Q.,
Katrukha E.A., Altelaar A.F., Heck A.J., Hoogenraad C.C.,
Akhmanova A.;
"Microtubule minus-end stabilization by polymerization-driven CAMSAP
deposition.";
Dev. Cell 28:295-309(2014).
[19]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=24908486; DOI=10.1016/j.neuron.2014.04.019;
Yau K.W., van Beuningen S.F., Cunha-Ferreira I., Cloin B.M.,
van Battum E.Y., Will L., Schaetzle P., Tas R.P., van Krugten J.,
Katrukha E.A., Jiang K., Wulf P.S., Mikhaylova M., Harterink M.,
Pasterkamp R.J., Akhmanova A., Kapitein L.C., Hoogenraad C.C.;
"Microtubule minus-end binding protein CAMSAP2 controls axon
specification and dendrite development.";
Neuron 82:1058-1073(2014).
[20]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=24706919; DOI=10.1073/pnas.1404133111;
Hendershott M.C., Vale R.D.;
"Regulation of microtubule minus-end dynamics by CAMSAPs and
Patronin.";
Proc. Natl. Acad. Sci. U.S.A. 111:5860-5865(2014).
[21]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH AKAP9 AND
PDE4DIP.
PubMed=27666745; DOI=10.1016/j.devcel.2016.08.009;
Wu J., de Heus C., Liu Q., Bouchet B.P., Noordstra I., Jiang K.,
Hua S., Martin M., Yang C., Grigoriev I., Katrukha E.A.,
Altelaar A.F., Hoogenraad C.C., Qi R.Z., Klumperman J., Akhmanova A.;
"Molecular pathway of microtubule organization at the Golgi
apparatus.";
Dev. Cell 39:44-60(2016).
[22]
FUNCTION, AND INTERACTION WITH MAPRE1.
PubMed=28726242; DOI=10.1002/1873-3468.12758;
Wei J., Xu H., Meng W.;
"Noncentrosomal microtubules regulate autophagosome transport through
CAMSAP2-EB1 cross-talk.";
FEBS Lett. 591:2379-2393(2017).
[23]
SUBCELLULAR LOCATION, AND INTERACTION WITH MAPRE1; AKAP9 AND PDE4DIP.
PubMed=28814570; DOI=10.1083/jcb.201701024;
Yang C., Wu J., de Heus C., Grigoriev I., Liv N., Yao Y., Smal I.,
Meijering E., Klumperman J., Qi R.Z., Akhmanova A.;
"EB1 and EB3 regulate microtubule minus end organization and Golgi
morphology.";
J. Cell Biol. 216:3179-3198(2017).
[24]
VARIANT [LARGE SCALE ANALYSIS] LEU-361.
PubMed=16959974; DOI=10.1126/science.1133427;
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
Vogelstein B., Kinzler K.W., Velculescu V.E.;
"The consensus coding sequences of human breast and colorectal
cancers.";
Science 314:268-274(2006).
-!- FUNCTION: Key microtubule-organizing protein that specifically
binds the minus-end of non-centrosomal microtubules and regulates
their dynamics and organization (PubMed:23169647, PubMed:24486153,
PubMed:24706919). Specifically recognizes growing microtubule
minus-ends and autonomously decorates and stabilizes microtubule
lattice formed by microtubule minus-end polymerization
(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 addition,
it also reduces the velocity of microtubule polymerization
(PubMed:24486153, PubMed:24706919). Through the microtubule
cytoskeleton, also regulates the organization of cellular
organelles including the Golgi and the early endosomes
(PubMed:27666745). Essential for the tethering, but not for
nucleation of non-centrosomal microtubules at the Golgi: together
with Golgi-associated proteins AKAP9 and PDE4DIP, required to
tether non-centrosomal minus-end microtubules to the Golgi, an
important step for polarized cell movement (PubMed:27666745). Also
acts as a regulator of neuronal polarity and development:
localizes to non-centrosomal microtubule minus-ends in neurons and
stabilizes non-centrosomal microtubules, which is required for
neuronal polarity, axon specification and dendritic branch
formation (PubMed:24908486). Through the microtubule cytoskeleton,
regulates the autophagosome transport (PubMed:28726242).
{ECO:0000269|PubMed:23169647, ECO:0000269|PubMed:24486153,
ECO:0000269|PubMed:24706919, ECO:0000269|PubMed:24908486,
ECO:0000269|PubMed:27666745, ECO:0000269|PubMed:28726242}.
-!- SUBUNIT: Interacts with CAMSAP3 (By similarity). Interacts with
KATNA1 and KATNB1; leading to regulate the length of CAMSAP2-
decorated microtubule stretches (PubMed:24486153). Interacts with
a complex formed by AKAP9 and PDE4DIP isoform 13/MMG8/SMYLE, which
recruits CAMSAP2 to the Golgi (PubMed:27666745, PubMed:28814570).
Interacts with MAPRE1/EB1 (PubMed:28726242, PubMed:28814570).
{ECO:0000250|UniProtKB:Q8C1B1, ECO:0000269|PubMed:24486153,
ECO:0000269|PubMed:27666745, ECO:0000269|PubMed:28726242,
ECO:0000269|PubMed:28814570}.
-!- INTERACTION:
P29692:EEF1D; NbExp=2; IntAct=EBI-1051869, EBI-358607;
-!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
{ECO:0000269|PubMed:23169647, ECO:0000269|PubMed:24486153,
ECO:0000269|PubMed:24706919, ECO:0000269|PubMed:24908486,
ECO:0000269|PubMed:27666745, ECO:0000269|PubMed:28814570}. Golgi
apparatus {ECO:0000269|PubMed:27666745}. Note=Associated with the
minus-end of microtubules and also detected at the centrosomes
(PubMed:23169647, PubMed:24486153, PubMed:24908486,
PubMed:24706919, PubMed:27666745, PubMed:28814570). Decorates the
minus-end of microtubules by decreasing the rate of tubulin
incorporation and remaining bound (PubMed:24486153). The length of
CAMSAP2-decorated stretches on the minus-end of microtubules
depends on MAPRE1/EB1 and MAPRE3/EB3, which promote elongation of
CAMSAP2-decorated microtubule stretches (PubMed:28814570).
Recruited to the Golgi apparatus by AKAP9 and PDE4DIP isoform
13/MMG8/SMYLE (PubMed:27666745). In neurons, localizes to the
minus-end of microtubules in axon and dendrites (PubMed:24908486).
{ECO:0000269|PubMed:23169647, ECO:0000269|PubMed:24486153,
ECO:0000269|PubMed:24706919, ECO:0000269|PubMed:27666745,
ECO:0000269|PubMed:28814570}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=Q08AD1-1; Sequence=Displayed;
Name=2;
IsoId=Q08AD1-2; Sequence=VSP_030805, VSP_030806;
Note=No experimental confirmation available.;
Name=3;
IsoId=Q08AD1-3; Sequence=VSP_030805;
Note=No experimental confirmation available.;
-!- DOMAIN: The CKK domain binds microtubules and specifically
recognizes the minus-end of microtubules (PubMed:24486153).
{ECO:0000255|PROSITE-ProRule:PRU00841,
ECO:0000269|PubMed:24486153}.
-!- DOMAIN: The MBD (microtubule-binding domain) region can recognize
some features of the microtubule lattice, which might contribute
to the specific decoration of growing microtubule minus-ends by
CAMSAP2. {ECO:0000269|PubMed:24486153}.
-!- DISEASE: Note=Defects in CAMSAP2 may be a cause of susceptibility
to epilepsy in the Chinese population.
{ECO:0000305|PubMed:22116939}.
-!- SIMILARITY: Belongs to the CAMSAP1 family. {ECO:0000255|PROSITE-
ProRule:PRU00841}.
-!- SEQUENCE CAUTION:
Sequence=AAH56910.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
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EMBL; AL450104; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471067; EAW91320.1; -; Genomic_DNA.
EMBL; BC011385; AAH11385.1; -; mRNA.
EMBL; BC056910; AAH56910.1; ALT_INIT; mRNA.
EMBL; BC125229; AAI25230.1; -; mRNA.
EMBL; BC125230; AAI25231.1; -; mRNA.
EMBL; AB029001; BAA83030.2; -; mRNA.
EMBL; AL110158; CAB53664.2; -; mRNA.
CCDS; CCDS1404.1; -. [Q08AD1-3]
CCDS; CCDS72998.1; -. [Q08AD1-1]
CCDS; CCDS72999.1; -. [Q08AD1-2]
PIR; T14744; T14744.
RefSeq; NP_001284636.1; NM_001297707.1. [Q08AD1-1]
RefSeq; NP_001284637.1; NM_001297708.1. [Q08AD1-2]
RefSeq; NP_982284.1; NM_203459.2. [Q08AD1-3]
UniGene; Hs.23585; -.
ProteinModelPortal; Q08AD1; -.
SMR; Q08AD1; -.
BioGrid; 116872; 68.
IntAct; Q08AD1; 68.
MINT; Q08AD1; -.
iPTMnet; Q08AD1; -.
PhosphoSitePlus; Q08AD1; -.
BioMuta; CAMSAP2; -.
DMDM; 308153626; -.
EPD; Q08AD1; -.
MaxQB; Q08AD1; -.
PaxDb; Q08AD1; -.
PeptideAtlas; Q08AD1; -.
PRIDE; Q08AD1; -.
ProteomicsDB; 58654; -.
ProteomicsDB; 58655; -. [Q08AD1-2]
ProteomicsDB; 58656; -. [Q08AD1-3]
DNASU; 23271; -.
Ensembl; ENST00000236925; ENSP00000236925; ENSG00000118200. [Q08AD1-1]
Ensembl; ENST00000358823; ENSP00000351684; ENSG00000118200. [Q08AD1-3]
Ensembl; ENST00000413307; ENSP00000416800; ENSG00000118200. [Q08AD1-2]
GeneID; 23271; -.
KEGG; hsa:23271; -.
UCSC; uc001gvk.4; human. [Q08AD1-1]
CTD; 23271; -.
DisGeNET; 23271; -.
EuPathDB; HostDB:ENSG00000118200.14; -.
GeneCards; CAMSAP2; -.
H-InvDB; HIX0001450; -.
HGNC; HGNC:29188; CAMSAP2.
HPA; HPA026304; -.
HPA; HPA026511; -.
HPA; HPA027302; -.
MIM; 613775; gene.
neXtProt; NX_Q08AD1; -.
OpenTargets; ENSG00000118200; -.
PharmGKB; PA142672206; -.
eggNOG; ENOG410IU7J; Eukaryota.
eggNOG; ENOG411033G; LUCA.
GeneTree; ENSGT00390000010026; -.
InParanoid; Q08AD1; -.
KO; K17493; -.
OMA; WENASTT; -.
OrthoDB; EOG091G00FI; -.
PhylomeDB; Q08AD1; -.
TreeFam; TF315529; -.
ChiTaRS; CAMSAP2; human.
GenomeRNAi; 23271; -.
PRO; PR:Q08AD1; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000118200; -.
CleanEx; HS_CAMSAP1L1; -.
ExpressionAtlas; Q08AD1; baseline and differential.
Genevisible; Q08AD1; HS.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
GO; GO:1990752; C:microtubule end; IDA:HPA.
GO; GO:0005516; F:calmodulin binding; IEA:InterPro.
GO; GO:0051011; F:microtubule minus-end binding; IDA:UniProtKB.
GO; GO:0030507; F:spectrin binding; IEA:InterPro.
GO; GO:0061564; P:axon development; IDA:UniProtKB.
GO; GO:0000226; P:microtubule cytoskeleton organization; IDA:UniProtKB.
GO; GO:0050773; P:regulation of dendrite development; IDA:UniProtKB.
GO; GO:1903358; P:regulation of Golgi organization; IDA:UniProtKB.
GO; GO:0031113; P:regulation of microtubule polymerization; IDA:UniProtKB.
GO; GO:0033043; P:regulation of organelle organization; IMP:UniProtKB.
Gene3D; 3.10.20.360; -; 1.
InterPro; IPR032940; CAMSAP.
InterPro; IPR031372; CAMSAP_CC1.
InterPro; IPR022613; CAMSAP_CH.
InterPro; IPR001715; CH-domain.
InterPro; IPR036872; CH_dom_sf.
InterPro; IPR038209; CKK_dom_sf.
InterPro; IPR014797; CKK_domain.
InterPro; IPR011033; PRC_barrel-like_sf.
PANTHER; PTHR21595; PTHR21595; 1.
Pfam; PF17095; CAMSAP_CC1; 1.
Pfam; PF11971; CAMSAP_CH; 1.
Pfam; PF08683; CAMSAP_CKK; 1.
SMART; SM01051; CAMSAP_CKK; 1.
SUPFAM; SSF47576; SSF47576; 1.
SUPFAM; SSF50346; SSF50346; 1.
PROSITE; PS50021; CH; 1.
PROSITE; PS51508; CKK; 1.
1: Evidence at protein level;
Alternative splicing; Coiled coil; Complete proteome; Cytoplasm;
Cytoskeleton; Golgi apparatus; Microtubule; Phosphoprotein;
Polymorphism; Reference proteome.
CHAIN 1 1489 Calmodulin-regulated spectrin-associated
protein 2.
/FTId=PRO_0000316832.
DOMAIN 222 335 Calponin-homology (CH).
{ECO:0000255|PROSITE-ProRule:PRU00044}.
DOMAIN 1349 1483 CKK. {ECO:0000255|PROSITE-
ProRule:PRU00841}.
REGION 922 1034 MBD region.
{ECO:0000269|PubMed:24486153}.
COILED 756 793 {ECO:0000255}.
COILED 887 926 {ECO:0000255}.
COILED 1166 1238 {ECO:0000255}.
MOD_RES 416 416 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 418 418 Phosphoserine.
{ECO:0000250|UniProtKB:Q8C1B1}.
MOD_RES 426 426 Phosphothreonine.
{ECO:0000250|UniProtKB:Q8C1B1}.
MOD_RES 464 464 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 598 598 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 599 599 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 611 611 Phosphoserine.
{ECO:0000250|UniProtKB:Q8C1B1}.
MOD_RES 673 673 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 678 678 Phosphothreonine.
{ECO:0000250|UniProtKB:Q8C1B1}.
MOD_RES 680 680 Phosphoserine.
{ECO:0000250|UniProtKB:Q8C1B1}.
MOD_RES 862 862 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 931 931 Phosphoserine.
{ECO:0000244|PubMed:16964243,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 936 936 Phosphoserine.
{ECO:0000244|PubMed:16964243,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231}.
MOD_RES 997 997 Phosphothreonine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 1002 1002 Phosphothreonine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 1004 1004 Phosphothreonine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 1008 1008 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 1019 1019 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 1148 1148 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 1313 1313 Phosphoserine.
{ECO:0000244|PubMed:16964243,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 1319 1319 Phosphoserine.
{ECO:0000244|PubMed:16964243,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 1321 1321 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
VAR_SEQ 216 226 Missing (in isoform 2 and isoform 3).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_030805.
VAR_SEQ 380 395 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_030806.
VARIANT 361 361 I -> L (in a colorectal cancer sample;
somatic mutation).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_038399.
VARIANT 958 958 P -> L (in dbSNP:rs3753952).
/FTId=VAR_038400.
VARIANT 969 969 P -> L (in dbSNP:rs3753952).
/FTId=VAR_057796.
VARIANT 1028 1028 R -> P (in dbSNP:rs6674599).
/FTId=VAR_038401.
VARIANT 1039 1039 P -> R (in dbSNP:rs6674599).
/FTId=VAR_057797.
CONFLICT 150 150 E -> K (in Ref. 4; BAA83030).
{ECO:0000305}.
CONFLICT 1261 1261 Q -> K (in Ref. 3; AAH56910).
{ECO:0000305}.
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


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