Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

CAP-Gly domain-containing linker protein 1

Gene

Clip1

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

Functioni

Binds to the plus end of microtubules and regulates the dynamics of the microtubule cytoskeleton. Promotes microtubule growth and microtubule bundling. Links cytoplasmic vesicles to microtubules and thereby plays an important role in intracellular vesicle trafficking. Plays a role macropinocytosis and endosome trafficking.By similarity

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri1370 – 1387CCHC-typeBy similarityAdd BLAST18

GO - Molecular functioni

  • microtubule binding Source: UniProtKB
  • microtubule plus-end binding Source: MGI
  • tubulin binding Source: UniProtKB
  • zinc ion binding Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Transport

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiR-MMU-2467813. Separation of Sister Chromatids.
R-MMU-2500257. Resolution of Sister Chromatid Cohesion.
R-MMU-5626467. RHO GTPases activate IQGAPs.
R-MMU-5663220. RHO GTPases Activate Formins.
R-MMU-68877. Mitotic Prometaphase.

Names & Taxonomyi

Protein namesi
Recommended name:
CAP-Gly domain-containing linker protein 1
Alternative name(s):
Cytoplasmic linker protein 1701 Publication
Short name:
CLIP-1701 Publication
Restin
Gene namesi
Name:Clip1
Synonyms:Kiaa4046, Rsn
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 5

Organism-specific databases

MGIiMGI:1928401. Clip1.

Subcellular locationi

GO - Cellular componenti

  • centrosome Source: MGI
  • cytoplasm Source: MGI
  • cytoplasmic vesicle membrane Source: UniProtKB-SubCell
  • macropinosome Source: Ensembl
  • microtubule Source: UniProtKB
  • microtubule cytoskeleton Source: UniProtKB
  • microtubule end Source: MGI
  • microtubule plus-end Source: UniProtKB
  • nuclear envelope Source: WormBase
  • ruffle Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell projection, Cytoplasm, Cytoplasmic vesicle, Cytoskeleton, Membrane, Microtubule

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002406721 – 1391CAP-Gly domain-containing linker protein 1Add BLAST1391

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei48PhosphoserineBy similarity1
Modified residuei50PhosphothreonineBy similarity1
Modified residuei146PhosphoserineBy similarity1
Modified residuei181PhosphothreonineBy similarity1
Modified residuei194PhosphoserineCombined sources1
Modified residuei196PhosphoserineBy similarity1
Modified residuei199PhosphoserineCombined sources1
Modified residuei203PhosphoserineCombined sources1
Modified residuei309PhosphoserineBy similarity1
Modified residuei311Phosphoserine; by PKABy similarity1
Modified residuei314PhosphoserineCombined sources1
Modified residuei347PhosphoserineBy similarity1
Modified residuei1317PhosphoserineCombined sources1

Post-translational modificationi

Phosphorylated (PubMed:26972003). Phosphorylation induces conformational changes by increasing the affinity of the N-terminus for C-terminus, resulting in inhibition of its function thus decreasing its binding to microtubules and DCTN1. Exhibits a folded, autoinhibited conformation when phosphorylated and an open conformation when dephosphorylated with increased binding affinity to microtubules and DCTN1. Phosphorylation regulates its recruitment to tyrosinated microtubules and the recruitment of vesicular cargo to microtubules in neurons. Phosphorylation by MTOR may positively regulate CLIP1 association with microtubules (By similarity).By similarity1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ922J3.
PaxDbiQ922J3.
PeptideAtlasiQ922J3.
PRIDEiQ922J3.

PTM databases

iPTMnetiQ922J3.
PhosphoSitePlusiQ922J3.

Expressioni

Gene expression databases

BgeeiENSMUSG00000049550.
CleanExiMM_CLIP1.
ExpressionAtlasiQ922J3. baseline and differential.
GenevisibleiQ922J3. MM.

Interactioni

Subunit structurei

Interacts with MTOR; phosphorylates and regulates CLIP1. Interacts (via CAP-Gly domains) with tubulin. Interacts with SLAIN2. Interacts with TUBA1B, MAPRE1 and MAPRE3. Interacts (via zinc finger) with DCTN1 (By similarity). Binds preferentially to tyrosinated microtubules, and only marginally to detyrosinated microtubules (PubMed:16954346).By similarity1 Publication

GO - Molecular functioni

  • microtubule binding Source: UniProtKB
  • microtubule plus-end binding Source: MGI
  • tubulin binding Source: UniProtKB

Protein-protein interaction databases

BioGridi207974. 4 interactors.
IntActiQ922J3. 4 interactors.
MINTiMINT-4122817.
STRINGi10090.ENSMUSP00000107192.

Structurei

Secondary structure

11391
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi63 – 66Combined sources4
Beta strandi71 – 79Combined sources9
Beta strandi81 – 83Combined sources3
Beta strandi85 – 95Combined sources11
Beta strandi97 – 103Combined sources7
Beta strandi116 – 119Combined sources4
Helixi121 – 123Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2CP7NMR-A58-128[»]
ProteinModelPortaliQ922J3.
SMRiQ922J3.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ922J3.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini78 – 120CAP-Gly 1PROSITE-ProRule annotationAdd BLAST43
Domaini231 – 273CAP-Gly 2PROSITE-ProRule annotationAdd BLAST43

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni97 – 101Important for tubulin bindingBy similarity5

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili349 – 1306Sequence analysisAdd BLAST958

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi305 – 330Ser-richAdd BLAST26

Domaini

Intramolecular interaction between the zinc finger domain and the CAP-Gly domains may inhibit interaction with tubulin.By similarity

Sequence similaritiesi

Contains 2 CAP-Gly domains.PROSITE-ProRule annotation
Contains 1 CCHC-type zinc finger.Curated

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri1370 – 1387CCHC-typeBy similarityAdd BLAST18

Keywords - Domaini

Coiled coil, Repeat, Zinc-finger

Phylogenomic databases

eggNOGiKOG4568. Eukaryota.
COG5244. LUCA.
GeneTreeiENSGT00760000119173.
HOGENOMiHOG000092755.
HOVERGENiHBG007123.
InParanoidiQ922J3.
KOiK10421.
PhylomeDBiQ922J3.
TreeFamiTF326096.

Family and domain databases

Gene3Di2.30.30.190. 2 hits.
InterProiIPR000938. CAP-Gly_domain.
IPR032108. CLIP1_ZNF.
[Graphical view]
PfamiPF01302. CAP_GLY. 2 hits.
PF16641. CLIP1_ZNF. 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]

Sequences (2)i

Sequence statusi: Complete.

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

Isoform 1 (identifier: Q922J3-1) [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
MSMLKPSGLK APTKILKPGS TALKTPAAAA APVEKTIPSE KASGPPSSET
60 70 80 90 100
QEEFVDDFRV GERVWVNGNK PGFIQFLGET QFAPGQWAGI VLDEPIGKND
110 120 130 140 150
GSVAGVRYFQ CEPLKGIFTR PSKLTRKVQA EDEANGLQAA PGRTASPLST
160 170 180 190 200
AAATMVSSSP ATPSNIPHKP SQSTAKEPSA TPQISNLTKT ASESISNLSE
210 220 230 240 250
AGSVKKGERE LKVGDRVLVG GTKAGVVRFL GETDFAKGEW CGVELDEPLG
260 270 280 290 300
KNDGAVAGTR YFQCQPKYGL FAPVHKVTKI GFPSTTPAKA KAAAVRRVMA
310 320 330 340 350
ATPASLKRSP SASSLSSMSS VASSVSSKPS RTGLLTETSS RYARKISGTT
360 370 380 390 400
ALQEALKEKQ QHIEQLLAER DLERAEVAKA TSHVGEIEQE LALARDGHDQ
410 420 430 440 450
HVLELEAKMD QLRTMVEAAD REKVELLNQL EEEKRKVEDL QFRVEEESIT
460 470 480 490 500
KGDLEVATVS EKSRIMELEK DLALRAQEVA ELRRRLESSK PPGDVDMSLS
510 520 530 540 550
LLQEISALQE KLEAIHTDHQ GEMTSLKEHF GAREEAFQKE IKALHTATEK
560 570 580 590 600
LSKENESLRS KLDHANKENS DVIALWKSKL ETAIASHQQA MEELKVSFSK
610 620 630 640 650
GIGTDSAEFA ELKTQIERLR LDYQHEIESL QSKQDSERSA HAKEMETMQA
660 670 680 690 700
KLMKIIKEKE DSLEAVKARL DSAEDQHLVE MEDTLNKLQE AEIKVKELEV
710 720 730 740 750
LQAKYTEQSE VIGNFTSQLS AVKEKLLDLD ALRKANSEGK LELETLRQQL
760 770 780 790 800
EGAEKQIKNL ETERNAESSK ANSITKELQE KELVLTGLQD SLNQVNQVKE
810 820 830 840 850
TLEKELQTLK EKFASTSEEA VSAQTRMQDT VNKLHQKEEQ FNVLSSELEK
860 870 880 890 900
LRENLTDMEA KFKEKDDRED QLVKAKEKLE NDIAEIMKMS GDNSSQLTKM
910 920 930 940 950
NDELRLKERS VEELQLKLTK ANENASFLQK SIGEVTLKAE QSQQQAARKH
960 970 980 990 1000
EEEKKELEEK LLELEKKMET SYNQCQDLKA KYEKASSETK TKHEEILQNL
1010 1020 1030 1040 1050
QKMLADTEDK LKAAQEANRD LMQDMEELKT QADKAKAAQT AEDAMQIMEQ
1060 1070 1080 1090 1100
MTKEKTETLA SLEDTKQTNA RLQNELDTLK ENNLKTVEEL NKSKELLSVE
1110 1120 1130 1140 1150
NQKMEEFKKE IETLKQAAAQ KSQQLSALQE ENVKLAEELG RTRDEVTSHQ
1160 1170 1180 1190 1200
KLEEERSVLN NQLLEMKKRE SEFRKDADEE KASLQKSISL TSALLTEKDA
1210 1220 1230 1240 1250
ELEKLRNEVT VLRGENATAK SLHSVVQTLE SDKVKLELKV KNLELQLKEN
1260 1270 1280 1290 1300
KRQLSSSSGN TDAQAEEDER AQESQIDFLN SVIVDLQRKN QDLKMKVEMM
1310 1320 1330 1340 1350
SEAALNGNGE DLNSYDSDDQ EKQSKKKPRL FCDICDCFDL HDTEDCPTQA
1360 1370 1380 1390
QMSEDPPHST HHGSRSEERP YCEICEMFGH WATNCNDDET F
Length:1,391
Mass (Da):155,814
Last modified:December 1, 2001 - v1
Checksum:i061BED1FB3D4068D
GO
Isoform 2 (identifier: Q922J3-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     695-770: Missing.

Show »
Length:1,315
Mass (Da):147,242
Checksum:i449A0909164DFB02
GO

Sequence cautioni

The sequence BAD90357 differs from that shown. Reason: Erroneous initiation.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti47S → F in BAD90357 (Ref. 1) Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_019425695 – 770Missing in isoform 2. 1 PublicationAdd BLAST76

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK220172 mRNA. Translation: BAD90357.1. Different initiation.
BC007191 mRNA. Translation: AAH07191.1.
CCDSiCCDS19667.1. [Q922J3-1]
CCDS71663.1. [Q922J3-2]
RefSeqiNP_001278158.1. NM_001291229.1. [Q922J3-2]
NP_062739.2. NM_019765.5. [Q922J3-1]
UniGeneiMm.241109.
Mm.441802.

Genome annotation databases

EnsembliENSMUST00000111564; ENSMUSP00000107190; ENSMUSG00000049550. [Q922J3-2]
ENSMUST00000111566; ENSMUSP00000107192; ENSMUSG00000049550. [Q922J3-1]
GeneIDi56430.
KEGGimmu:56430.
UCSCiuc008zoa.2. mouse. [Q922J3-1]
uc008zob.2. mouse. [Q922J3-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK220172 mRNA. Translation: BAD90357.1. Different initiation.
BC007191 mRNA. Translation: AAH07191.1.
CCDSiCCDS19667.1. [Q922J3-1]
CCDS71663.1. [Q922J3-2]
RefSeqiNP_001278158.1. NM_001291229.1. [Q922J3-2]
NP_062739.2. NM_019765.5. [Q922J3-1]
UniGeneiMm.241109.
Mm.441802.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2CP7NMR-A58-128[»]
ProteinModelPortaliQ922J3.
SMRiQ922J3.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi207974. 4 interactors.
IntActiQ922J3. 4 interactors.
MINTiMINT-4122817.
STRINGi10090.ENSMUSP00000107192.

PTM databases

iPTMnetiQ922J3.
PhosphoSitePlusiQ922J3.

Proteomic databases

EPDiQ922J3.
PaxDbiQ922J3.
PeptideAtlasiQ922J3.
PRIDEiQ922J3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000111564; ENSMUSP00000107190; ENSMUSG00000049550. [Q922J3-2]
ENSMUST00000111566; ENSMUSP00000107192; ENSMUSG00000049550. [Q922J3-1]
GeneIDi56430.
KEGGimmu:56430.
UCSCiuc008zoa.2. mouse. [Q922J3-1]
uc008zob.2. mouse. [Q922J3-2]

Organism-specific databases

CTDi6249.
MGIiMGI:1928401. Clip1.
RougeiSearch...

Phylogenomic databases

eggNOGiKOG4568. Eukaryota.
COG5244. LUCA.
GeneTreeiENSGT00760000119173.
HOGENOMiHOG000092755.
HOVERGENiHBG007123.
InParanoidiQ922J3.
KOiK10421.
PhylomeDBiQ922J3.
TreeFamiTF326096.

Enzyme and pathway databases

ReactomeiR-MMU-2467813. Separation of Sister Chromatids.
R-MMU-2500257. Resolution of Sister Chromatid Cohesion.
R-MMU-5626467. RHO GTPases activate IQGAPs.
R-MMU-5663220. RHO GTPases Activate Formins.
R-MMU-68877. Mitotic Prometaphase.

Miscellaneous databases

ChiTaRSiClip1. mouse.
EvolutionaryTraceiQ922J3.
PROiQ922J3.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000049550.
CleanExiMM_CLIP1.
ExpressionAtlasiQ922J3. baseline and differential.
GenevisibleiQ922J3. MM.

Family and domain databases

Gene3Di2.30.30.190. 2 hits.
InterProiIPR000938. CAP-Gly_domain.
IPR032108. CLIP1_ZNF.
[Graphical view]
PfamiPF01302. CAP_GLY. 2 hits.
PF16641. CLIP1_ZNF. 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...

Entry informationi

Entry nameiCLIP1_MOUSE
AccessioniPrimary (citable) accession number: Q922J3
Secondary accession number(s): Q571L7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 27, 2006
Last sequence update: December 1, 2001
Last modified: November 30, 2016
This is version 124 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, 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.