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Protein

CAP-Gly domain-containing linker protein 2

Gene

Clip2

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Seems to link microtubules to dendritic lamellar body (DLB), a membranous organelle predominantly present in bulbous dendritic appendages of neurons linked by dendrodendritic gap junctions. May operate in the control of brain-specific organelle translocations.1 Publication

GO - Molecular functioni

  • microtubule binding Source: RGD
  • microtubule plus-end binding Source: UniProtKB

GO - Biological processi

  • negative regulation of microtubule depolymerization Source: UniProtKB
Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
CAP-Gly domain-containing linker protein 2
Alternative name(s):
Cytoplasmic linker protein 115
Short name:
CLIP-115
Cytoplasmic linker protein 2
Gene namesi
Name:Clip2
Synonyms:Cyln2
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi62019. Clip2.

Subcellular locationi

GO - Cellular componenti

  • cytoplasmic microtubule Source: UniProtKB
  • dendrite Source: UniProtKB
  • dendritic microtubule Source: RGD
  • lamellar body Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Microtubule

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 10461046CAP-Gly domain-containing linker protein 2PRO_0000083517Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei50 – 501PhosphoserineBy similarity
Modified residuei203 – 2031PhosphoserineCombined sources
Modified residuei208 – 2081PhosphoserineCombined sources
Modified residuei212 – 2121PhosphoserineBy similarity
Modified residuei315 – 3151PhosphoserineBy similarity
Modified residuei923 – 9231PhosphoserineCombined sources
Modified residuei973 – 9731PhosphoserineBy similarity
Modified residuei979 – 9791PhosphoserineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiO55156.
PRIDEiO55156.

PTM databases

iPTMnetiO55156.
PhosphoSiteiO55156.

Expressioni

Tissue specificityi

Brain-specific, expressed in the hippocampus, inferior olive, and piriform cortex and in the cerebellum (at protein level).1 Publication

Interactioni

Subunit structurei

Interacts with CLASP1 and CLASP2.By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
CLASP1Q7Z4603EBI-349416,EBI-913476From a different organism.
Clasp1Q80TV83EBI-349416,EBI-908322From a different organism.
CLASP2O751223EBI-349416,EBI-913524From a different organism.

GO - Molecular functioni

  • microtubule binding Source: RGD
  • microtubule plus-end binding Source: UniProtKB

Protein-protein interaction databases

BioGridi247936. 2 interactions.
IntActiO55156. 4 interactions.
STRINGi10116.ENSRNOP00000035734.

Structurei

3D structure databases

ProteinModelPortaliO55156.
SMRiO55156. Positions 69-156, 174-345.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini100 – 14243CAP-Gly 1PROSITE-ProRule annotationAdd
BLAST
Domaini240 – 28243CAP-Gly 2PROSITE-ProRule annotationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili355 – 525171Sequence analysisAdd
BLAST
Coiled coili564 – 63774Sequence analysisAdd
BLAST
Coiled coili675 – 966292Sequence analysisAdd
BLAST
Coiled coili994 – 101421Sequence analysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi315 – 34632Ser-richAdd
BLAST

Sequence similaritiesi

Contains 2 CAP-Gly domains.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil, Repeat

Phylogenomic databases

eggNOGiKOG4568. Eukaryota.
COG5244. LUCA.
HOGENOMiHOG000092755.
HOVERGENiHBG007123.
InParanoidiO55156.
PhylomeDBiO55156.

Family and domain databases

Gene3Di2.30.30.190. 2 hits.
InterProiIPR000938. CAP-Gly_domain.
IPR028394. CLIP2.
[Graphical view]
PANTHERiPTHR18916:SF10. PTHR18916:SF10. 1 hit.
PfamiPF01302. CAP_GLY. 2 hits.
[Graphical view]
SMARTiSM01052. CAP_GLY. 2 hits.
[Graphical view]
SUPFAMiSSF74924. SSF74924. 2 hits.
PROSITEiPS00845. CAP_GLY_1. 2 hits.
PS50245. CAP_GLY_2. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O55156-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQKPSGLKPP GRGGKHSSPV GRPSIGSASS SVVASASGSK EGSPLHKQAS
60 70 80 90 100
GPSSAGATTT VSEKPGPKAA EVGDDFLGDF VVGERVWVNG VKPGVVQYLG
110 120 130 140 150
ETQFAPGQWA GVVLDDPVGK NDGAVGGLRY FECPALQGIF TRPSKLTRQP
160 170 180 190 200
AAEGSGSDGH SVESLTAQNL SLHSGTATPP LTGRVIPLRE SVLNSSVKTG
210 220 230 240 250
NESGSNLSDS GSVKRGDKDL HLGDRVLVGG TKTGVVRYVG ETDFAKGEWC
260 270 280 290 300
GVELDEPLGK NDGAVAGTRY FQCPPKFGLF APIHKVIRIG FPSTSPAKAK
310 320 330 340 350
KTKRMAMGVS ALTHSPSSSS ISSVSSVASS VGGRPSRSGL LTETSSRYAR
360 370 380 390 400
KISGTTALQE ALKEKQQHIE QLLAERDLER AEVAKATSHI CEVEKEIALL
410 420 430 440 450
KAQHEQYVAE AEEKLQRARL LVENVRKEKV DLSNQLEEER RKVEDLQFRV
460 470 480 490 500
EEESITKGDL ETQTQLEHAR IGELEQSLLL EKAQAERLLR ELADNRLTTV
510 520 530 540 550
AEKSRVLQLE EELSLRRGEI EELQHCLLQS GPPPADHPEA AETLRLRERL
560 570 580 590 600
LSASKEHQRD STLLQDKYEH MLKTYQTEVD KLRAANEKYA QEVADLKAKV
610 620 630 640 650
QQATTENMGL MDNWKSKLDS LASDHQKSLE DLKATLNSGP GAQQKEIGEL
660 670 680 690 700
KALVEGIKME HQLELGNLQA KHDLETAMHG KEKEGLRQKL QEAQEELAGL
710 720 730 740 750
QQHWRAQLEE QAAAPAELQE AQDQCRDAQL RVQELEGLDV EYRGQAQAIE
760 770 780 790 800
FLKEQISLAE KKMLDYEMLQ RAEAQSRQEA ERLREKLLVA ENRLQAVESL
810 820 830 840 850
CSAQHSHVIE SNDLSEEKIR MKETVEGLQD KLNKRDKEVA ALTSQMDMLR
860 870 880 890 900
AQVSALENKC KSGEKKIDSL LKEKRRLEAE LEAVSRKTHD ASGQLVHISQ
910 920 930 940 950
ELLRKERSLN ELRVLLLEAN RHSPGPERDL SREVHKAEWR IKEQKLKDDI
960 970 980 990 1000
RGLREKLTGL DKEKSLSEQK RYSLIDPASA PELLRLQHQL VSTEGCLRDA
1010 1020 1030 1040
LDQAQQVERL VEALRGCSDR TQTISNSGSA NGIHQPDKAH KQEDKH
Length:1,046
Mass (Da):115,480
Last modified:June 1, 1998 - v1
Checksum:i72E6CE9F76D2A1D0
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ000485 mRNA. Translation: CAA04123.1.
PIRiT42734.
UniGeneiRn.10893.

Genome annotation databases

UCSCiRGD:62019. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ000485 mRNA. Translation: CAA04123.1.
PIRiT42734.
UniGeneiRn.10893.

3D structure databases

ProteinModelPortaliO55156.
SMRiO55156. Positions 69-156, 174-345.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi247936. 2 interactions.
IntActiO55156. 4 interactions.
STRINGi10116.ENSRNOP00000035734.

PTM databases

iPTMnetiO55156.
PhosphoSiteiO55156.

Proteomic databases

PaxDbiO55156.
PRIDEiO55156.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

UCSCiRGD:62019. rat.

Organism-specific databases

RGDi62019. Clip2.

Phylogenomic databases

eggNOGiKOG4568. Eukaryota.
COG5244. LUCA.
HOGENOMiHOG000092755.
HOVERGENiHBG007123.
InParanoidiO55156.
PhylomeDBiO55156.

Miscellaneous databases

PROiO55156.

Family and domain databases

Gene3Di2.30.30.190. 2 hits.
InterProiIPR000938. CAP-Gly_domain.
IPR028394. CLIP2.
[Graphical view]
PANTHERiPTHR18916:SF10. PTHR18916:SF10. 1 hit.
PfamiPF01302. CAP_GLY. 2 hits.
[Graphical view]
SMARTiSM01052. CAP_GLY. 2 hits.
[Graphical view]
SUPFAMiSSF74924. SSF74924. 2 hits.
PROSITEiPS00845. CAP_GLY_1. 2 hits.
PS50245. CAP_GLY_2. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "CLIP-115, a novel brain specific cytoplasmic linker protein, mediates the localisation of dendritic lamellar bodies."
    de Zeeuw C.I., Hoogenraad C.C., Goedknegt E., Hertzberg E., Neubauer A., Grosveld F.G., Galjart N.J.
    Neuron 19:1187-1199(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY.
  2. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-203; SER-208 AND SER-923, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiCLIP2_RAT
AccessioniPrimary (citable) accession number: O55156
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 27, 2005
Last sequence update: June 1, 1998
Last modified: June 8, 2016
This is version 109 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

Complete proteome, Reference proteome

Documents

  1. 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.