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CAP-Gly domain-containing linker protein 1 (Cytoplasmic linker protein 1) (Cytoplasmic linker protein 170 alpha-2) (CLIP-170) (Reed-Sternberg intermediate filament-associated protein) (Restin)

 CLIP1_HUMAN             Reviewed;        1438 AA.
P30622; A0AVD3; Q17RS4; Q29RG0;
01-APR-1993, integrated into UniProtKB/Swiss-Prot.
13-OCT-2009, sequence version 2.
25-OCT-2017, entry version 182.
RecName: Full=CAP-Gly domain-containing linker protein 1;
AltName: Full=Cytoplasmic linker protein 1;
AltName: Full=Cytoplasmic linker protein 170 alpha-2;
Short=CLIP-170;
AltName: Full=Reed-Sternberg intermediate filament-associated protein;
AltName: Full=Restin;
Name=CLIP1; Synonyms=CYLN1, RSN;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND TISSUE SPECIFICITY.
TISSUE=Peripheral blood monocyte;
PubMed=1600942;
Bilbe G., Delabie J., Brueggen J., Richener H., Asselbergs F.A.M.,
Cerletti N., Sorg C., Odink K., Tarcsay L., Wiesendanger W.,
de Wolf-Peeters C., Shipman R.;
"Restin: a novel intermediate filament-associated protein highly
expressed in the Reed-Sternberg cells of Hodgkin's disease.";
EMBO J. 11:2103-2113(1992).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), AND VARIANT GLU-1080.
PubMed=1356075; DOI=10.1016/0092-8674(92)90240-D;
Pierre P., Scheel J., Rickard J.E., Kreis T.E.;
"CLIP-170 links endocytic vesicles to microtubules.";
Cell 70:887-900(1992).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3), AND
VARIANTS PRO-941 AND GLU-1080.
TISSUE=Colon;
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]
FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=12433698; DOI=10.1182/blood.V100.12.4139;
Sahin U., Neumann F., Tureci O., Schmits R., Perez F.,
Pfreundschuh M.;
"Hodgkin and Reed-Sternberg cell-associated autoantigen CLIP-
170/restin is a marker for dendritic cells and is involved in the
trafficking of macropinosomes to the cytoskeleton, supporting a
function-based concept of Hodgkin and Reed-Sternberg cells.";
Blood 100:4139-4145(2002).
[5]
INTERACTION WITH MTOR, AND PHOSPHORYLATION BY MTOR.
PubMed=12231510; DOI=10.1093/embo-reports/kvf197;
Choi J.H., Bertram P.G., Drenan R., Carvalho J., Zhou H.H.,
Zheng X.F.;
"The FKBP12-rapamycin-associated protein (FRAP) is a CLIP-170
kinase.";
EMBO Rep. 3:988-994(2002).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-200 AND SER-204, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-195, 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]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-48; THR-140; SER-143;
SER-147; THR-182; SER-197; SER-200 AND SER-204, 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).
[9]
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).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-195; SER-200 AND
SER-204, AND 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).
[11]
INTERACTION WITH DCTN1.
PubMed=20679239; DOI=10.1073/pnas.1006615107;
Li H., Liu X.S., Yang X., Song B., Wang Y., Liu X.;
"Polo-like kinase 1 phosphorylation of p150Glued facilitates nuclear
envelope breakdown during prophase.";
Proc. Natl. Acad. Sci. U.S.A. 107:14633-14638(2010).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-48; THR-140; SER-143;
SER-200; SER-204 AND SER-1364, 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 THR-50; THR-140; SER-143;
THR-182; SER-195; SER-200 AND SER-204, 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).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-200 AND THR-1310, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[16]
STRUCTURE BY NMR OF 1-340.
RIKEN structural genomics initiative (RSGI);
"Solution structure of the 1st and 2nd CAP-Gly domain in human CLIP-
170/Restin.";
Submitted (NOV-2005) to the PDB data bank.
[17]
X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 57-128, FUNCTION, SUBUNIT,
SUBCELLULAR LOCATION, MUTAGENESIS OF 98-LYS-ASN-99, AND INTERACTION
WITH TUBULIN.
PubMed=17889670; DOI=10.1016/j.molcel.2007.07.023;
Slep K.C., Vale R.D.;
"Structural basis of microtubule plus end tracking by XMAP215, CLIP-
170, and EB1.";
Mol. Cell 27:976-991(2007).
[18]
X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 1388-1427 IN COMPLEX WITH
DCTN1.
PubMed=17828277; DOI=10.1038/nsmb1291;
Weisbrich A., Honnappa S., Jaussi R., Okhrimenko O., Frey D.,
Jelesarov I., Akhmanova A., Steinmetz M.O.;
"Structure-function relationship of CAP-Gly domains.";
Nat. Struct. Mol. Biol. 14:959-967(2007).
[19]
X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 1416-1438 IN COMPLEX WITH
DCTN1 AND ZINC, INTERACTION WITH DCTN1, AND ZINC-FINGER.
PubMed=17828275; DOI=10.1038/nsmb1299;
Hayashi I., Plevin M.J., Ikura M.;
"CLIP170 autoinhibition mimics intermolecular interactions with
p150Glued or EB1.";
Nat. Struct. Mol. Biol. 14:980-981(2007).
[20]
X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) OF 211-300, STRUCTURE BY NMR OF
203-300 IN COMPLEX WITH TUBA1B, INTERACTION WITH TUBULIN; TUBA1B;
MAPRE1 AND MAPRE3, FUNCTION, AND ZINC-FINGER DOMAIN.
PubMed=17563362; DOI=10.1073/pnas.0703876104;
Mishima M., Maesaki R., Kasa M., Watanabe T., Fukata M., Kaibuchi K.,
Hakoshima T.;
"Structural basis for tubulin recognition by cytoplasmic linker
protein 170 and its autoinhibition.";
Proc. Natl. Acad. Sci. U.S.A. 104:10346-10351(2007).
[21]
X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 56-127 IN COMPLEX WITH
SLAIN2, SUBCELLULAR LOCATION, AND INTERACTION WITH SLAIN2.
PubMed=21646404; DOI=10.1083/jcb.201012179;
van der Vaart B., Manatschal C., Grigoriev I., Olieric V.,
Gouveia S.M., Bjelic S., Demmers J., Vorobjev I., Hoogenraad C.C.,
Steinmetz M.O., Akhmanova A.;
"SLAIN2 links microtubule plus end-tracking proteins and controls
microtubule growth in interphase.";
J. Cell Biol. 193:1083-1099(2011).
[22]
VARIANT [LARGE SCALE ANALYSIS] ILE-1213.
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: 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. {ECO:0000269|PubMed:12433698,
ECO:0000269|PubMed:17563362, ECO:0000269|PubMed:17889670}.
-!- SUBUNIT: Interacts with MTOR; phosphorylates and regulates CLIP1
(PubMed:12231510). Interacts (via CAP-Gly domains) with tubulin
(PubMed:17563362, PubMed:17889670). Interacts with SLAIN2
(PubMed:21646404). Interacts (via zinc finger) with DCTN1
(PubMed:17828275, PubMed:20679239). Interacts with TUBA1B, MAPRE1
and MAPRE3 (PubMed:17563362). Binds preferentially to tyrosinated
microtubules, and only marginally to detyrosinated microtubules
(By similarity). {ECO:0000250|UniProtKB:Q922J3,
ECO:0000269|PubMed:12231510, ECO:0000269|PubMed:17563362,
ECO:0000269|PubMed:17828275, ECO:0000269|PubMed:17828277,
ECO:0000269|PubMed:17889670, ECO:0000269|PubMed:20679239,
ECO:0000269|PubMed:21646404}.
-!- INTERACTION:
Q14203:DCTN1; NbExp=7; IntAct=EBI-9640673, EBI-724352;
Q15691:MAPRE1; NbExp=4; IntAct=EBI-6479976, EBI-1004115;
Q71U36:TUBA1A; NbExp=3; IntAct=EBI-6479976, EBI-302552;
P68366:TUBA4A; NbExp=3; IntAct=EBI-2683569, EBI-351772;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. Cytoplasm,
cytoskeleton {ECO:0000269|PubMed:17889670,
ECO:0000269|PubMed:21646404}. Cytoplasmic vesicle membrane
{ECO:0000269|PubMed:12433698}; Peripheral membrane protein;
Cytoplasmic side. Cell projection, ruffle
{ECO:0000269|PubMed:12433698}. Note=Localizes to microtubule plus
ends (PubMed:21646404, PubMed:17889670). Localizes preferentially
to the ends of tyrosinated microtubules (By similarity).
Accumulates in plasma membrane regions with ruffling and
protrusions. Associates with the membranes of intermediate
macropinocytic vesicles (PubMed:12433698).
{ECO:0000250|UniProtKB:Q922J3, ECO:0000269|PubMed:12433698,
ECO:0000269|PubMed:17889670, ECO:0000269|PubMed:21646404}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=P30622-3; Sequence=Displayed;
Name=2; Synonyms=Long;
IsoId=P30622-1; Sequence=VSP_038201;
Name=3; Synonyms=Short;
IsoId=P30622-2; Sequence=VSP_000765;
-!- TISSUE SPECIFICITY: Detected in dendritic cells (at protein
level). Highly expressed in the Reed-Sternberg cells of Hodgkin
disease. {ECO:0000269|PubMed:12433698,
ECO:0000269|PubMed:1600942}.
-!- DOMAIN: Intramolecular interaction between the zinc finger domain
and the CAP-Gly domains may inhibit interaction with tubulin.
{ECO:0000269|PubMed:17563362}.
-!- PTM: Phosphorylated. 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 (By similarity).
Phosphorylation by MTOR may positively regulate CLIP1 association
with microtubules (PubMed:12231510).
{ECO:0000250|UniProtKB:Q9JK25, ECO:0000269|PubMed:12231510}.
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EMBL; X64838; CAA46050.1; -; mRNA.
EMBL; M97501; AAA35693.1; -; mRNA.
EMBL; BC114213; AAI14214.1; -; mRNA.
EMBL; BC117209; AAI17210.1; -; mRNA.
EMBL; BC126305; AAI26306.1; -; mRNA.
CCDS; CCDS58285.1; -. [P30622-3]
CCDS; CCDS9232.1; -. [P30622-1]
CCDS; CCDS9233.1; -. [P30622-2]
PIR; A43336; A43336.
PIR; S22695; S22695.
RefSeq; NP_001234926.1; NM_001247997.1. [P30622-3]
RefSeq; NP_002947.1; NM_002956.2. [P30622-1]
RefSeq; NP_937883.1; NM_198240.1. [P30622-2]
RefSeq; XP_016875275.1; XM_017019786.1. [P30622-1]
RefSeq; XP_016875279.1; XM_017019790.1. [P30622-2]
UniGene; Hs.524809; -.
PDB; 2CP5; NMR; -; A=1-128.
PDB; 2CP6; NMR; -; A=181-339.
PDB; 2E3H; X-ray; 1.45 A; A=211-300.
PDB; 2E3I; X-ray; 2.00 A; A=56-141.
PDB; 2E4H; NMR; -; A=203-300.
PDB; 2HQH; X-ray; 1.80 A; E/F/G/H=1416-1438.
PDB; 2QK0; X-ray; 2.00 A; A=57-128.
PDB; 3E2U; X-ray; 2.60 A; E/F/G/H=1399-1438.
PDB; 3RDV; X-ray; 1.75 A; A/B/C/D=56-127.
PDBsum; 2CP5; -.
PDBsum; 2CP6; -.
PDBsum; 2E3H; -.
PDBsum; 2E3I; -.
PDBsum; 2E4H; -.
PDBsum; 2HQH; -.
PDBsum; 2QK0; -.
PDBsum; 3E2U; -.
PDBsum; 3RDV; -.
ProteinModelPortal; P30622; -.
SMR; P30622; -.
BioGrid; 112163; 34.
CORUM; P30622; -.
DIP; DIP-42826N; -.
ELM; P30622; -.
IntAct; P30622; 25.
MINT; MINT-1781312; -.
STRING; 9606.ENSP00000303585; -.
iPTMnet; P30622; -.
PhosphoSitePlus; P30622; -.
UniCarbKB; P30622; -.
BioMuta; CLIP1; -.
DMDM; 261260059; -.
EPD; P30622; -.
PaxDb; P30622; -.
PeptideAtlas; P30622; -.
PRIDE; P30622; -.
Ensembl; ENST00000302528; ENSP00000303585; ENSG00000130779. [P30622-1]
Ensembl; ENST00000358808; ENSP00000351665; ENSG00000130779. [P30622-1]
Ensembl; ENST00000537178; ENSP00000445531; ENSG00000130779. [P30622-2]
Ensembl; ENST00000540338; ENSP00000439093; ENSG00000130779. [P30622-3]
Ensembl; ENST00000620786; ENSP00000479322; ENSG00000130779. [P30622-3]
GeneID; 6249; -.
KEGG; hsa:6249; -.
UCSC; uc001ucg.2; human. [P30622-3]
CTD; 6249; -.
DisGeNET; 6249; -.
EuPathDB; HostDB:ENSG00000130779.19; -.
GeneCards; CLIP1; -.
HGNC; HGNC:10461; CLIP1.
HPA; CAB004399; -.
HPA; HPA026678; -.
MalaCards; CLIP1; -.
MIM; 179838; gene.
neXtProt; NX_P30622; -.
OpenTargets; ENSG00000130779; -.
Orphanet; 88616; Autosomal recessive non-syndromic intellectual disability.
PharmGKB; PA162382349; -.
eggNOG; KOG4568; Eukaryota.
eggNOG; COG5244; LUCA.
GeneTree; ENSGT00760000119173; -.
HOGENOM; HOG000092755; -.
HOVERGEN; HBG007123; -.
InParanoid; P30622; -.
KO; K10421; -.
OMA; EAKFRER; -.
OrthoDB; EOG091G0J1Y; -.
PhylomeDB; P30622; -.
TreeFam; TF326096; -.
Reactome; R-HSA-141444; Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal.
Reactome; R-HSA-2467813; Separation of Sister Chromatids.
Reactome; R-HSA-2500257; Resolution of Sister Chromatid Cohesion.
Reactome; R-HSA-5626467; RHO GTPases activate IQGAPs.
Reactome; R-HSA-5663220; RHO GTPases Activate Formins.
Reactome; R-HSA-68877; Mitotic Prometaphase.
SIGNOR; P30622; -.
ChiTaRS; CLIP1; human.
EvolutionaryTrace; P30622; -.
GeneWiki; CLIP1; -.
GenomeRNAi; 6249; -.
PRO; PR:P30622; -.
Proteomes; UP000005640; Chromosome 12.
Bgee; ENSG00000130779; -.
CleanEx; HS_CLIP1; -.
ExpressionAtlas; P30622; baseline and differential.
Genevisible; P30622; HS.
GO; GO:0005813; C:centrosome; IDA:UniProtKB.
GO; GO:0005881; C:cytoplasmic microtubule; IEA:Ensembl.
GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005768; C:endosome; TAS:ProtInc.
GO; GO:0005882; C:intermediate filament; TAS:ProtInc.
GO; GO:0000776; C:kinetochore; TAS:UniProtKB.
GO; GO:0005874; C:microtubule; IMP:Alzheimers_University_of_Toronto.
GO; GO:0015630; C:microtubule cytoskeleton; IMP:UniProtKB.
GO; GO:0035371; C:microtubule plus-end; IEA:Ensembl.
GO; GO:0005635; C:nuclear envelope; IEA:Ensembl.
GO; GO:0001726; C:ruffle; IEA:UniProtKB-SubCell.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0046872; F:metal ion binding; NAS:UniProtKB.
GO; GO:0008017; F:microtubule binding; IDA:UniProtKB.
GO; GO:0051010; F:microtubule plus-end binding; IDA:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; TAS:UniProtKB.
GO; GO:0015631; F:tubulin binding; IDA:UniProtKB.
GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
GO; GO:0001578; P:microtubule bundle formation; IMP:UniProtKB.
GO; GO:0000278; P:mitotic cell cycle; TAS:UniProtKB.
GO; GO:0031116; P:positive regulation of microtubule polymerization; IMP:UniProtKB.
GO; GO:0044861; P:protein transport into plasma membrane raft; IEA:Ensembl.
GO; GO:0007062; P:sister chromatid cohesion; TAS:Reactome.
Gene3D; 2.30.30.190; -; 2.
InterPro; IPR036859; CAP-Gly_dom_sf.
InterPro; IPR000938; CAP-Gly_domain.
InterPro; IPR032108; CLIP1_ZNF.
Pfam; PF01302; CAP_GLY; 2.
Pfam; PF16641; CLIP1_ZNF; 2.
SMART; SM01052; CAP_GLY; 2.
SUPFAM; SSF74924; SSF74924; 2.
PROSITE; PS00845; CAP_GLY_1; 2.
PROSITE; PS50245; CAP_GLY_2; 2.
1: Evidence at protein level;
3D-structure; Alternative splicing; Cell projection; Coiled coil;
Complete proteome; Cytoplasm; Cytoplasmic vesicle; Cytoskeleton;
Membrane; Metal-binding; Microtubule; Phosphoprotein; Polymorphism;
Reference proteome; Repeat; Transport; Zinc; Zinc-finger.
CHAIN 1 1438 CAP-Gly domain-containing linker protein
1.
/FTId=PRO_0000083527.
DOMAIN 78 120 CAP-Gly 1. {ECO:0000255|PROSITE-
ProRule:PRU00045}.
DOMAIN 232 274 CAP-Gly 2. {ECO:0000255|PROSITE-
ProRule:PRU00045}.
ZN_FING 1417 1434 CCHC-type. {ECO:0000269|PubMed:17563362,
ECO:0000269|PubMed:17828275}.
REGION 97 101 Important for tubulin binding.
{ECO:0000269|PubMed:17889670}.
COILED 350 1353 {ECO:0000255}.
COMPBIAS 143 204 Ser-rich.
COMPBIAS 304 331 Ser-rich.
MOD_RES 48 48 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231}.
MOD_RES 50 50 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 140 140 Phosphothreonine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 143 143 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 147 147 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 182 182 Phosphothreonine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 195 195 Phosphoserine.
{ECO:0000244|PubMed:16964243,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:23186163}.
MOD_RES 197 197 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 200 200 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 204 204 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 310 310 Phosphoserine.
{ECO:0000250|UniProtKB:Q9JK25}.
MOD_RES 312 312 Phosphoserine; by PKA.
{ECO:0000250|UniProtKB:Q9JK25}.
MOD_RES 315 315 Phosphoserine.
{ECO:0000250|UniProtKB:Q922J3}.
MOD_RES 348 348 Phosphoserine.
{ECO:0000250|UniProtKB:Q9JK25}.
MOD_RES 1236 1236 Phosphoserine.
{ECO:0000250|UniProtKB:Q9JK25}.
MOD_RES 1310 1310 Phosphothreonine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 1364 1364 Phosphoserine.
{ECO:0000244|PubMed:20068231}.
VAR_SEQ 457 502 Missing (in isoform 3).
{ECO:0000303|PubMed:1356075,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_000765.
VAR_SEQ 457 467 Missing (in isoform 2).
{ECO:0000303|PubMed:1600942}.
/FTId=VSP_038201.
VARIANT 162 162 S -> P (in dbSNP:rs7963597).
/FTId=VAR_059206.
VARIANT 780 780 R -> W (in dbSNP:rs3741447).
/FTId=VAR_048672.
VARIANT 941 941 S -> P (in dbSNP:rs17883517).
{ECO:0000269|PubMed:15489334}.
/FTId=VAR_048673.
VARIANT 1080 1080 D -> E (in dbSNP:rs1129167).
{ECO:0000269|PubMed:1356075,
ECO:0000269|PubMed:15489334}.
/FTId=VAR_020398.
VARIANT 1213 1213 M -> I (in a breast cancer sample;
somatic mutation).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_036446.
VARIANT 1224 1224 A -> S (in dbSNP:rs17881033).
/FTId=VAR_048674.
MUTAGEN 98 99 KN->EE: Abolishes interaction with
tubulin. Abolishes localization at the
microtubule plus end.
{ECO:0000269|PubMed:17889670}.
CONFLICT 193 193 S -> G (in Ref. 3; AAI14214).
{ECO:0000305}.
CONFLICT 324 324 S -> P (in Ref. 3; AAI14214).
{ECO:0000305}.
CONFLICT 651 651 T -> A (in Ref. 3; AAI14214).
{ECO:0000305}.
CONFLICT 682 682 D -> N (in Ref. 3; AAI14214).
{ECO:0000305}.
CONFLICT 766 766 L -> P (in Ref. 3; AAI14214).
{ECO:0000305}.
CONFLICT 1432 1432 C -> R (in Ref. 3; AAI14214).
{ECO:0000305}.
STRAND 37 39 {ECO:0000244|PDB:2CP5}.
STRAND 63 66 {ECO:0000244|PDB:3RDV}.
TURN 67 69 {ECO:0000244|PDB:3RDV}.
STRAND 70 78 {ECO:0000244|PDB:3RDV}.
STRAND 81 85 {ECO:0000244|PDB:3RDV}.
STRAND 87 95 {ECO:0000244|PDB:3RDV}.
STRAND 97 103 {ECO:0000244|PDB:3RDV}.
STRAND 106 108 {ECO:0000244|PDB:3RDV}.
TURN 113 115 {ECO:0000244|PDB:2QK0}.
STRAND 116 119 {ECO:0000244|PDB:3RDV}.
HELIX 121 123 {ECO:0000244|PDB:3RDV}.
STRAND 124 127 {ECO:0000244|PDB:2E3I}.
STRAND 193 196 {ECO:0000244|PDB:2CP6}.
STRAND 217 220 {ECO:0000244|PDB:2E3H}.
TURN 221 223 {ECO:0000244|PDB:2E3H}.
STRAND 224 233 {ECO:0000244|PDB:2E3H}.
STRAND 235 249 {ECO:0000244|PDB:2E3H}.
STRAND 252 257 {ECO:0000244|PDB:2E3H}.
STRAND 260 262 {ECO:0000244|PDB:2E3H}.
TURN 267 269 {ECO:0000244|PDB:2CP6}.
STRAND 270 274 {ECO:0000244|PDB:2E3H}.
HELIX 275 277 {ECO:0000244|PDB:2E3H}.
STRAND 278 280 {ECO:0000244|PDB:2E3H}.
STRAND 295 298 {ECO:0000244|PDB:2CP6}.
TURN 1420 1423 {ECO:0000244|PDB:2HQH}.
STRAND 1424 1427 {ECO:0000244|PDB:2HQH}.
HELIX 1429 1431 {ECO:0000244|PDB:2HQH}.
SEQUENCE 1438 AA; 162246 MW; A7F125F7A96DBDDB CRC64;
MSMLKPSGLK APTKILKPGS TALKTPTAVV APVEKTISSE KASSTPSSET QEEFVDDFRV
GERVWVNGNK PGFIQFLGET QFAPGQWAGI VLDEPIGKND GSVAGVRYFQ CEPLKGIFTR
PSKLTRKVQA EDEANGLQTT PASRATSPLC TSTASMVSSS PSTPSNIPQK PSQPAAKEPS
ATPPISNLTK TASESISNLS EAGSIKKGER ELKIGDRVLV GGTKAGVVRF LGETDFAKGE
WCGVELDEPL GKNDGAVAGT RYFQCQPKYG LFAPVHKVTK IGFPSTTPAK AKANAVRRVM
ATTSASLKRS PSASSLSSMS SVASSVSSRP SRTGLLTETS SRYARKISGT TALQEALKEK
QQHIEQLLAE RDLERAEVAK ATSHVGEIEQ ELALARDGHD QHVLELEAKM DQLRTMVEAA
DREKVELLNQ LEEEKRKVED LQFRVEEESI TKGDLEQKSQ ISEDPENTQT KLEHARIKEL
EQSLLFEKTK ADKLQRELED TRVATVSEKS RIMELEKDLA LRVQEVAELR RRLESNKPAG
DVDMSLSLLQ EISSLQEKLE VTRTDHQREI TSLKEHFGAR EETHQKEIKA LYTATEKLSK
ENESLKSKLE HANKENSDVI ALWKSKLETA IASHQQAMEE LKVSFSKGLG TETAEFAELK
TQIEKMRLDY QHEIENLQNQ QDSERAAHAK EMEALRAKLM KVIKEKENSL EAIRSKLDKA
EDQHLVEMED TLNKLQEAEI KVKELEVLQA KCNEQTKVID NFTSQLKATE EKLLDLDALR
KASSEGKSEM KKLRQQLEAA EKQIKHLEIE KNAESSKASS ITRELQGREL KLTNLQENLS
EVSQVKETLE KELQILKEKF AEASEEAVSV QRSMQETVNK LHQKEEQFNM LSSDLEKLRE
NLADMEAKFR EKDEREEQLI KAKEKLENDI AEIMKMSGDN SSQLTKMNDE LRLKERDVEE
LQLKLTKANE NASFLQKSIE DMTVKAEQSQ QEAAKKHEEE KKELERKLSD LEKKMETSHN
QCQELKARYE RATSETKTKH EEILQNLQKT LLDTEDKLKG AREENSGLLQ ELEELRKQAD
KAKAAQTAED AMQIMEQMTK EKTETLASLE DTKQTNAKLQ NELDTLKENN LKNVEELNKS
KELLTVENQK MEEFRKEIET LKQAAAQKSQ QLSALQEENV KLAEELGRSR DEVTSHQKLE
EERSVLNNQL LEMKKRESKF IKDADEEKAS LQKSISITSA LLTEKDAELE KLRNEVTVLR
GENASAKSLH SVVQTLESDK VKLELKVKNL ELQLKENKRQ LSSSSGNTDT QADEDERAQE
SQIDFLNSVI VDLQRKNQDL KMKVEMMSEA ALNGNGDDLN NYDSDDQEKQ SKKKPRLFCD
ICDCFDLHDT EDCPTQAQMS EDPPHSTHHG SRGEERPYCE ICEMFGHWAT NCNDDETF


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