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Q922J3 (CLIP1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 101. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
CAP-Gly domain-containing linker protein 1
Alternative name(s):
Restin
Gene names
Name:Clip1
Synonyms:Kiaa4046, Rsn
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length1391 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Subunit structure

Interacts with MTOR; phosphorylates and regulates CLIP1. Interacts (via CAP-Gly domains) with tubulin. Interacts with SLAIN2. Interacts with MAPRE1 and MAPRE3. Interacts (via zinc finger) with DCTN1 By similarity.

Subcellular location

Cytoplasm By similarity. Cytoplasmcytoskeleton By similarity. Cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side By similarity. Cell projectionruffle By similarity. Note: Associated with the cytoskeleton. Detected at the plus ends of microtubules in the cytosol, and close to plasma membrane ruffles. Associates with the membranes of intermediate macropinocytic vesicles By similarity. Ref.5

Domain

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

Post-translational modification

Phosphorylated. Phosphorylation by MTOR may positively regulate CLIP1 association with microtubules By similarity.

Sequence similarities

Contains 2 CAP-Gly domains.

Contains 1 CCHC-type zinc finger.

Sequence caution

The sequence BAD90357.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processTransport
   Cellular componentCell projection
Cytoplasm
Cytoplasmic vesicle
Cytoskeleton
Membrane
Microtubule
   Coding sequence diversityAlternative splicing
   DomainCoiled coil
Repeat
Zinc-finger
   LigandMetal-binding
Zinc
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processmicrotubule bundle formation

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of microtubule polymerization

Inferred from sequence or structural similarity. Source: UniProtKB

transport

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcentrosome

Inferred from electronic annotation. Source: Ensembl

cytoplasmic vesicle membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

macropinosome

Inferred from electronic annotation. Source: Ensembl

microtubule

Inferred from direct assay Ref.5. Source: UniProtKB

microtubule cytoskeleton

Inferred from sequence or structural similarity. Source: UniProtKB

microtubule plus-end

Inferred from electronic annotation. Source: Ensembl

ruffle

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionmicrotubule binding

Inferred from direct assay PubMed 11290329. Source: MGI

nucleic acid binding

Inferred from electronic annotation. Source: InterPro

protein binding

Inferred from physical interaction PubMed 11290329PubMed 11940666PubMed 16148041. Source: MGI

tubulin binding

Inferred from sequence or structural similarity. Source: UniProtKB

zinc ion binding

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q922J3-1)

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.
Isoform 2 (identifier: Q922J3-2)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 13911391CAP-Gly domain-containing linker protein 1
PRO_0000240672

Regions

Domain78 – 12043CAP-Gly 1
Domain231 – 27343CAP-Gly 2
Zinc finger1370 – 138718CCHC-type
Region97 – 1015Important for tubulin binding By similarity
Coiled coil349 – 1306958 Potential
Compositional bias305 – 33026Ser-rich

Amino acid modifications

Modified residue481Phosphoserine By similarity
Modified residue1461Phosphoserine By similarity
Modified residue1811Phosphothreonine By similarity
Modified residue1941Phosphoserine By similarity
Modified residue1961Phosphoserine By similarity
Modified residue1991Phosphoserine Ref.4
Modified residue2031Phosphoserine Ref.3 Ref.4
Modified residue13171Phosphoserine By similarity

Natural variations

Alternative sequence695 – 77076Missing in isoform 2.
VSP_019425

Experimental info

Sequence conflict471S → F in BAD90357. Ref.1

Secondary structure

............... 1391
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified December 1, 2001. Version 1.
Checksum: 061BED1FB3D4068D

FASTA1,391155,814
        10         20         30         40         50         60 
MSMLKPSGLK APTKILKPGS TALKTPAAAA APVEKTIPSE KASGPPSSET QEEFVDDFRV 

        70         80         90        100        110        120 
GERVWVNGNK PGFIQFLGET QFAPGQWAGI VLDEPIGKND GSVAGVRYFQ CEPLKGIFTR 

       130        140        150        160        170        180 
PSKLTRKVQA EDEANGLQAA PGRTASPLST AAATMVSSSP ATPSNIPHKP SQSTAKEPSA 

       190        200        210        220        230        240 
TPQISNLTKT ASESISNLSE AGSVKKGERE LKVGDRVLVG GTKAGVVRFL GETDFAKGEW 

       250        260        270        280        290        300 
CGVELDEPLG KNDGAVAGTR YFQCQPKYGL FAPVHKVTKI GFPSTTPAKA KAAAVRRVMA 

       310        320        330        340        350        360 
ATPASLKRSP SASSLSSMSS VASSVSSKPS RTGLLTETSS RYARKISGTT ALQEALKEKQ 

       370        380        390        400        410        420 
QHIEQLLAER DLERAEVAKA TSHVGEIEQE LALARDGHDQ HVLELEAKMD QLRTMVEAAD 

       430        440        450        460        470        480 
REKVELLNQL EEEKRKVEDL QFRVEEESIT KGDLEVATVS EKSRIMELEK DLALRAQEVA 

       490        500        510        520        530        540 
ELRRRLESSK PPGDVDMSLS LLQEISALQE KLEAIHTDHQ GEMTSLKEHF GAREEAFQKE 

       550        560        570        580        590        600 
IKALHTATEK LSKENESLRS KLDHANKENS DVIALWKSKL ETAIASHQQA MEELKVSFSK 

       610        620        630        640        650        660 
GIGTDSAEFA ELKTQIERLR LDYQHEIESL QSKQDSERSA HAKEMETMQA KLMKIIKEKE 

       670        680        690        700        710        720 
DSLEAVKARL DSAEDQHLVE MEDTLNKLQE AEIKVKELEV LQAKYTEQSE VIGNFTSQLS 

       730        740        750        760        770        780 
AVKEKLLDLD ALRKANSEGK LELETLRQQL EGAEKQIKNL ETERNAESSK ANSITKELQE 

       790        800        810        820        830        840 
KELVLTGLQD SLNQVNQVKE TLEKELQTLK EKFASTSEEA VSAQTRMQDT VNKLHQKEEQ 

       850        860        870        880        890        900 
FNVLSSELEK LRENLTDMEA KFKEKDDRED QLVKAKEKLE NDIAEIMKMS GDNSSQLTKM 

       910        920        930        940        950        960 
NDELRLKERS VEELQLKLTK ANENASFLQK SIGEVTLKAE QSQQQAARKH EEEKKELEEK 

       970        980        990       1000       1010       1020 
LLELEKKMET SYNQCQDLKA KYEKASSETK TKHEEILQNL QKMLADTEDK LKAAQEANRD 

      1030       1040       1050       1060       1070       1080 
LMQDMEELKT QADKAKAAQT AEDAMQIMEQ MTKEKTETLA SLEDTKQTNA RLQNELDTLK 

      1090       1100       1110       1120       1130       1140 
ENNLKTVEEL NKSKELLSVE NQKMEEFKKE IETLKQAAAQ KSQQLSALQE ENVKLAEELG 

      1150       1160       1170       1180       1190       1200 
RTRDEVTSHQ KLEEERSVLN NQLLEMKKRE SEFRKDADEE KASLQKSISL TSALLTEKDA 

      1210       1220       1230       1240       1250       1260 
ELEKLRNEVT VLRGENATAK SLHSVVQTLE SDKVKLELKV KNLELQLKEN KRQLSSSSGN 

      1270       1280       1290       1300       1310       1320 
TDAQAEEDER AQESQIDFLN SVIVDLQRKN QDLKMKVEMM SEAALNGNGE DLNSYDSDDQ 

      1330       1340       1350       1360       1370       1380 
EKQSKKKPRL FCDICDCFDL HDTEDCPTQA QMSEDPPHST HHGSRSEERP YCEICEMFGH 

      1390 
WATNCNDDET F 

« Hide

Isoform 2 [UniParc].

Checksum: 449A0909164DFB02
Show »

FASTA1,315147,242

References

« Hide 'large scale' references
[1]"Prediction of the coding sequences of mouse homologues of KIAA gene. The complete nucleotide sequences of mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Koseki H., Hiraoka S., Saga Y., Nagase T., Ohara O., Koga H.
Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Embryonic tail.
[2]"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] (ISOFORM 1).
Strain: FVB/N.
Tissue: Mammary tumor.
[3]"Phosphoproteomic analysis of the developing mouse brain."
Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.
Mol. Cell. Proteomics 3:1093-1101(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-203, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic brain.
[4]"Large-scale phosphorylation analysis of mouse liver."
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-199 AND SER-203, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
[5]"ACF7 regulates cytoskeletal-focal adhesion dynamics and migration and has ATPase activity."
Wu X., Kodama A., Fuchs E.
Cell 135:137-148(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[6]"Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic fibroblast.
[7]"Solution structure of the 1st CAP-Gly domain in mouse CLIP-170/Restin."
RIKEN structural genomics initiative (RSGI)
Submitted (NOV-2005) to the PDB data bank
Cited for: STRUCTURE BY NMR OF 58-128.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK220172 mRNA. Translation: BAD90357.1. Different initiation.
BC007191 mRNA. Translation: AAH07191.1.
CCDSCCDS19667.1. [Q922J3-1]
RefSeqNP_001278158.1. NM_001291229.1. [Q922J3-2]
NP_062739.2. NM_019765.5. [Q922J3-1]
UniGeneMm.241109.
Mm.441802.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2CP7NMR-A58-128[»]
ProteinModelPortalQ922J3.
SMRQ922J3. Positions 4-130, 180-339.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid207974. 3 interactions.
IntActQ922J3. 4 interactions.
MINTMINT-4122817.
STRING10090.ENSMUSP00000031382.

PTM databases

PhosphoSiteQ922J3.

Proteomic databases

MaxQBQ922J3.
PaxDbQ922J3.
PRIDEQ922J3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000111564; ENSMUSP00000107190; ENSMUSG00000049550. [Q922J3-2]
ENSMUST00000111566; ENSMUSP00000107192; ENSMUSG00000049550. [Q922J3-1]
GeneID56430.
KEGGmmu:56430.
UCSCuc008zoa.1. mouse. [Q922J3-1]
uc008zob.1. mouse. [Q922J3-2]

Organism-specific databases

CTD6249.
MGIMGI:1928401. Clip1.
RougeSearch...

Phylogenomic databases

eggNOGCOG5244.
GeneTreeENSGT00740000115338.
HOGENOMHOG000092755.
HOVERGENHBG007123.
KOK10421.
OrthoDBEOG7992PN.
PhylomeDBQ922J3.
TreeFamTF326096.

Gene expression databases

ArrayExpressQ922J3.
BgeeQ922J3.
CleanExMM_CLIP1.
GenevestigatorQ922J3.

Family and domain databases

Gene3D2.30.30.190. 2 hits.
InterProIPR000938. CAP-Gly_domain.
IPR001878. Znf_CCHC.
[Graphical view]
PfamPF01302. CAP_GLY. 2 hits.
[Graphical view]
SMARTSM01052. CAP_GLY. 2 hits.
SM00343. ZnF_C2HC. 1 hit.
[Graphical view]
SUPFAMSSF74924. SSF74924. 2 hits.
PROSITEPS00845. CAP_GLY_1. 2 hits.
PS50245. CAP_GLY_2. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ922J3.
NextBio312602.
PROQ922J3.
SOURCESearch...

Entry information

Entry nameCLIP1_MOUSE
AccessionPrimary (citable) accession number: Q922J3
Secondary accession number(s): Q571L7
Entry history
Integrated into UniProtKB/Swiss-Prot: June 27, 2006
Last sequence update: December 1, 2001
Last modified: July 9, 2014
This is version 101 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot