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Protein

Calmodulin-regulated spectrin-associated protein 2

Gene

CAMSAP2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Microtubule minus-end binding protein that may regulate the organization of non-centrosomal microtubules. 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

  • microtubule minus-end binding Source: UniProtKB

GO - Biological processi

  • microtubule cytoskeleton organization Source: UniProtKB
  • neuron projection development Source: InterPro
  • regulation of organelle organization Source: UniProtKB
Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
Calmodulin-regulated spectrin-associated protein 2
Alternative name(s):
Calmodulin-regulated spectrin-associated protein 1-like protein 1
Gene namesi
Name:CAMSAP2
Synonyms:CAMSAP1L1, KIAA1078
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:29188. CAMSAP2.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Microtubule

Pathology & Biotechi

Involvement in diseasei

Defects in CAMSAP2 may be a cause of susceptibility to epilepsy in the Chinese population.

Organism-specific databases

PharmGKBiPA142672206.

Polymorphism and mutation databases

BioMutaiCAMSAP2.
DMDMi308153626.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 14891489Calmodulin-regulated spectrin-associated protein 2PRO_0000316832Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei416 – 4161PhosphoserineBy similarity
Modified residuei418 – 4181PhosphoserineBy similarity
Modified residuei426 – 4261PhosphothreonineBy similarity
Modified residuei464 – 4641PhosphoserineCombined sources
Modified residuei598 – 5981PhosphoserineCombined sources
Modified residuei599 – 5991PhosphoserineCombined sources
Modified residuei611 – 6111PhosphoserineBy similarity
Modified residuei673 – 6731PhosphoserineCombined sources
Modified residuei678 – 6781PhosphothreonineBy similarity
Modified residuei680 – 6801PhosphoserineBy similarity
Modified residuei862 – 8621PhosphoserineBy similarity
Modified residuei931 – 9311PhosphoserineCombined sources
Modified residuei936 – 9361PhosphoserineCombined sources
Modified residuei997 – 9971PhosphothreonineCombined sources
Modified residuei1002 – 10021PhosphothreonineCombined sources
Modified residuei1004 – 10041PhosphothreonineCombined sources
Modified residuei1008 – 10081PhosphoserineCombined sources
Modified residuei1019 – 10191PhosphoserineCombined sources
Modified residuei1148 – 11481PhosphoserineCombined sources
Modified residuei1313 – 13131PhosphoserineCombined sources
Modified residuei1319 – 13191PhosphoserineCombined sources
Modified residuei1321 – 13211PhosphoserineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ08AD1.
MaxQBiQ08AD1.
PaxDbiQ08AD1.
PRIDEiQ08AD1.

PTM databases

iPTMnetiQ08AD1.

Expressioni

Gene expression databases

BgeeiQ08AD1.
CleanExiHS_CAMSAP1L1.
ExpressionAtlasiQ08AD1. baseline and differential.
GenevisibleiQ08AD1. HS.

Organism-specific databases

HPAiHPA026304.
HPA026511.
HPA027302.

Interactioni

Subunit structurei

Interacts with CAMSAP3.By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
EEF1DP296922EBI-1051869,EBI-358607

GO - Molecular functioni

  • microtubule minus-end binding Source: UniProtKB

Protein-protein interaction databases

BioGridi116872. 24 interactions.
IntActiQ08AD1. 22 interactions.
MINTiMINT-8330034.
STRINGi9606.ENSP00000351684.

Structurei

3D structure databases

ProteinModelPortaliQ08AD1.
SMRiQ08AD1. Positions 1348-1477.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini211 – 332122CHAdd
BLAST
Domaini1349 – 1483135CKKPROSITE-ProRule annotationAdd
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

eggNOGiENOG410IU7J. Eukaryota.
ENOG411033G. LUCA.
GeneTreeiENSGT00390000010026.
InParanoidiQ08AD1.
KOiK17493.
OMAiNINRMPK.
OrthoDBiEOG7P8P6Z.
PhylomeDBiQ08AD1.
TreeFamiTF315529.

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. 1 hit.
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 (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q08AD1-1) [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
MGDAADPREM RKTFIVPAIK PFDHYDFSRA KIACNLAWLV AKAFGTENVP
60 70 80 90 100
EELQEPFYTD QYDQEHIKPP VVNLLLSAEL YCRAGSLILK SDAAKPLLGH
110 120 130 140 150
DAVIQALAQK GLYVTDQEKL VTERDLHKKP IQMSAHLAMI DTLMMAYTVE
160 170 180 190 200
MVSIEKVIAC AQQYSAFFQA TDLPYDIEDA VMYWINKVNE HLKDIMEQEQ
210 220 230 240 250
KLKEHHTVEA PGGQKSPSKW FWKLVPARYR KEQTLLKQLP CIPLVENLLK
260 270 280 290 300
DGTDGCALAA LIHFYCPDVV RLEDICLKET MSLADSLYNL QLIQEFCQEY
310 320 330 340 350
LNQCCHFTLE DMLYAASSIK SNYLVFMAEL FWWFEVVKPS FVQPRVVRPQ
360 370 380 390 400
GAEPVKDMPS IPVLNAAKRN VLDSSSDFPS SGEGATFTQS HHHLPSRYSR
410 420 430 440 450
PQAHSSASGG IRRSSSMSYV DGFIGTWPKE KRSSVHGVSF DISFDKEDSV
460 470 480 490 500
QRSTPNRGIT RSISNEGLTL NNSHVSKHIR KNLSFKPING EEEAESIEEE
510 520 530 540 550
LNIDSHSDLK SCVPLNTNEL NSNENIHYKL PNGALQNRIL LDEFGNQIET
560 570 580 590 600
PSIEEALQII HDTEKSPHTP QPDQIANGFF LHSQEMSILN SNIKLNQSSP
610 620 630 640 650
DNVTDTKGAL SPITDNTEVD TGIHVPSEDI PETMDEDSSL RDYTVSLDSD
660 670 680 690 700
MDDASKFLQD YDIRTGNTRE ALSPCPSTVS TKSQPGSSAS SSSGVKMTSF
710 720 730 740 750
AEQKFRKLNH TDGKSSGSSS QKTTPEGSEL NIPHVVAWAQ IPEETGLPQG
760 770 780 790 800
RDTTQLLASE MVHLRMKLEE KRRAIEAQKK KMEAAFTKQR QKMGRTAFLT
810 820 830 840 850
VVKKKGDGIS PLREEAAGAE DEKVYTDRAK EKESQKTDGQ RSKSLADIKE
860 870 880 890 900
SMENPQAKWL KSPTTPIDPE KQWNLASPSE ETLNEGEILE YTKSIEKLNS
910 920 930 940 950
SLHFLQQEMQ RLSLQQEMLM QMREQQSWVI SPPQPSPQKQ IRDFKPSKQA
960 970 980 990 1000
GLSSAIAPFS SDSPRPTHPS PQSSNRKSAS FSVKSQRTPR PNELKITPLN
1010 1020 1030 1040 1050
RTLTPPRSVD SLPRLRRFSP SQVPIQTRSF VCFGDDGEPQ LKESKPKEEV
1060 1070 1080 1090 1100
KKEELESKGT LEQRGHNPEE KEIKPFESTV SEVLSLPVTE TVCLTPNEDQ
1110 1120 1130 1140 1150
LNQPTEPPPK PVFPPTAPKN VNLIEVSLSD LKPPEKADVP VEKYDGESDK
1160 1170 1180 1190 1200
EQFDDDQKVC CGFFFKDDQK AENDMAMKRA ALLEKRLRRE KETQLRKQQL
1210 1220 1230 1240 1250
EAEMEHKKEE TRRKTEEERQ KKEDERARRE FIRQEYMRRK QLKLMEDMDT
1260 1270 1280 1290 1300
VIKPRPQVVK QKKQRPKSIH RDHIESPKTP IKGPPVSSLS LASLNTGDNE
1310 1320 1330 1340 1350
SVHSGKRTPR SESVEGFLSP SRCGSRNGEK DWENASTTSS VASGTEYTGP
1360 1370 1380 1390 1400
KLYKEPSAKS NKHIIQNALA HCCLAGKVNE GQKKKILEEM EKSDANNFLI
1410 1420 1430 1440 1450
LFRDSGCQFR SLYTYCPETE EINKLTGIGP KSITKKMIEG LYKYNSDRKQ
1460 1470 1480
FSHIPAKTLS ASVDAITIHS HLWQTKRPVT PKKLLPTKA
Length:1,489
Mass (Da):168,089
Last modified:October 5, 2010 - v3
Checksum:i4E20A240E2691027
GO
Isoform 2 (identifier: Q08AD1-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     216-226: Missing.
     380-395: Missing.

Note: No experimental confirmation available.
Show »
Length:1,462
Mass (Da):165,058
Checksum:iE036B5F830A186F1
GO
Isoform 3 (identifier: Q08AD1-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     216-226: Missing.

Note: No experimental confirmation available.
Show »
Length:1,478
Mass (Da):166,732
Checksum:iD2979D7D328FB53D
GO

Sequence cautioni

The sequence AAH56910.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti150 – 1501E → K in BAA83030 (PubMed:10470851).Curated
Sequence conflicti1261 – 12611Q → K in AAH56910 (PubMed:15489334).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti361 – 3611I → L in a colorectal cancer sample; somatic mutation. 1 Publication
VAR_038399
Natural varianti958 – 9581P → L.
Corresponds to variant rs3753952 [ dbSNP | Ensembl ].
VAR_038400
Natural varianti969 – 9691P → L.
Corresponds to variant rs3753952 [ dbSNP | Ensembl ].
VAR_057796
Natural varianti1028 – 10281R → P.
Corresponds to variant rs6674599 [ dbSNP | Ensembl ].
VAR_038401
Natural varianti1039 – 10391P → R.
Corresponds to variant rs6674599 [ dbSNP | Ensembl ].
VAR_057797

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei216 – 22611Missing in isoform 2 and isoform 3. 1 PublicationVSP_030805Add
BLAST
Alternative sequencei380 – 39516Missing in isoform 2. 1 PublicationVSP_030806Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL450104 Genomic DNA. Translation: CAI17077.1.
CH471067 Genomic DNA. Translation: EAW91320.1.
BC011385 mRNA. Translation: AAH11385.1.
BC056910 mRNA. Translation: AAH56910.1. Different initiation.
BC125229 mRNA. Translation: AAI25230.1.
BC125230 mRNA. Translation: AAI25231.1.
AB029001 mRNA. Translation: BAA83030.2.
AL110158 mRNA. Translation: CAB53664.2.
CCDSiCCDS1404.1. [Q08AD1-3]
CCDS72998.1. [Q08AD1-1]
CCDS72999.1. [Q08AD1-2]
PIRiT14744.
RefSeqiNP_001284636.1. NM_001297707.1. [Q08AD1-1]
NP_001284637.1. NM_001297708.1. [Q08AD1-2]
NP_982284.1. NM_203459.2. [Q08AD1-3]
UniGeneiHs.23585.

Genome annotation databases

EnsembliENST00000236925; ENSP00000236925; ENSG00000118200. [Q08AD1-1]
ENST00000358823; ENSP00000351684; ENSG00000118200. [Q08AD1-3]
ENST00000413307; ENSP00000416800; ENSG00000118200. [Q08AD1-2]
GeneIDi23271.
KEGGihsa:23271.
UCSCiuc001gvk.4. human. [Q08AD1-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL450104 Genomic DNA. Translation: CAI17077.1.
CH471067 Genomic DNA. Translation: EAW91320.1.
BC011385 mRNA. Translation: AAH11385.1.
BC056910 mRNA. Translation: AAH56910.1. Different initiation.
BC125229 mRNA. Translation: AAI25230.1.
BC125230 mRNA. Translation: AAI25231.1.
AB029001 mRNA. Translation: BAA83030.2.
AL110158 mRNA. Translation: CAB53664.2.
CCDSiCCDS1404.1. [Q08AD1-3]
CCDS72998.1. [Q08AD1-1]
CCDS72999.1. [Q08AD1-2]
PIRiT14744.
RefSeqiNP_001284636.1. NM_001297707.1. [Q08AD1-1]
NP_001284637.1. NM_001297708.1. [Q08AD1-2]
NP_982284.1. NM_203459.2. [Q08AD1-3]
UniGeneiHs.23585.

3D structure databases

ProteinModelPortaliQ08AD1.
SMRiQ08AD1. Positions 1348-1477.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi116872. 24 interactions.
IntActiQ08AD1. 22 interactions.
MINTiMINT-8330034.
STRINGi9606.ENSP00000351684.

PTM databases

iPTMnetiQ08AD1.

Polymorphism and mutation databases

BioMutaiCAMSAP2.
DMDMi308153626.

Proteomic databases

EPDiQ08AD1.
MaxQBiQ08AD1.
PaxDbiQ08AD1.
PRIDEiQ08AD1.

Protocols and materials databases

DNASUi23271.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000236925; ENSP00000236925; ENSG00000118200. [Q08AD1-1]
ENST00000358823; ENSP00000351684; ENSG00000118200. [Q08AD1-3]
ENST00000413307; ENSP00000416800; ENSG00000118200. [Q08AD1-2]
GeneIDi23271.
KEGGihsa:23271.
UCSCiuc001gvk.4. human. [Q08AD1-1]

Organism-specific databases

CTDi23271.
GeneCardsiCAMSAP2.
H-InvDBHIX0001450.
HGNCiHGNC:29188. CAMSAP2.
HPAiHPA026304.
HPA026511.
HPA027302.
MIMi613775. gene.
neXtProtiNX_Q08AD1.
PharmGKBiPA142672206.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IU7J. Eukaryota.
ENOG411033G. LUCA.
GeneTreeiENSGT00390000010026.
InParanoidiQ08AD1.
KOiK17493.
OMAiNINRMPK.
OrthoDBiEOG7P8P6Z.
PhylomeDBiQ08AD1.
TreeFamiTF315529.

Miscellaneous databases

ChiTaRSiCAMSAP2. human.
GenomeRNAii23271.
PROiQ08AD1.
SOURCEiSearch...

Gene expression databases

BgeeiQ08AD1.
CleanExiHS_CAMSAP1L1.
ExpressionAtlasiQ08AD1. baseline and differential.
GenevisibleiQ08AD1. HS.

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. 1 hit.
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 DNA sequence and biological annotation of human chromosome 1."
    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.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "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] (ISOFORMS 1 AND 2).
    Tissue: Eye.
  4. "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."
    Kikuno R., Nagase T., Ishikawa K., Hirosawa M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
    DNA Res. 6:197-205(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 125-1489 (ISOFORM 1).
    Tissue: Brain.
  5. "Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones."
    Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.
    DNA Res. 9:99-106(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: SEQUENCE REVISION.
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1288-1489 (ISOFORM 1).
    Tissue: Uterus.
  7. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
    Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
    Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-931; SER-936; SER-1313 AND SER-1319, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
    Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
    J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. Cited for: 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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  12. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    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.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-464; SER-599; SER-931; SER-936; SER-1148 AND SER-1319, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-464 AND SER-599, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. "Two-stage genome-wide association study identifies variants in CAMSAP1L1 as susceptibility loci for epilepsy in Chinese."
    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.
    Hum. Mol. Genet. 21:1184-1189(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: POSSIBLE INVOLVEMENT IN EPILEPSY.
  16. "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, MICROTUBULE-BINDING, SUBCELLULAR LOCATION.
  17. Cited for: VARIANT [LARGE SCALE ANALYSIS] LEU-361.

Entry informationi

Entry nameiCAMP2_HUMAN
AccessioniPrimary (citable) accession number: Q08AD1
Secondary accession number(s): B1APG6
, Q08AD2, Q6PGN8, Q96FB3, Q9UG20, Q9UPS4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 26, 2008
Last sequence update: October 5, 2010
Last modified: June 8, 2016
This is version 90 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. 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.