CLIP1_HUMAN
ID CLIP1_HUMAN Reviewed; 1438 AA.
AC P30622; A0AVD3; Q17RS4; Q29RG0;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 13-OCT-2009, sequence version 2.
DT 03-AUG-2022, entry version 212.
DE RecName: Full=CAP-Gly domain-containing linker protein 1;
DE AltName: Full=Cytoplasmic linker protein 1;
DE AltName: Full=Cytoplasmic linker protein 170 alpha-2;
DE Short=CLIP-170;
DE AltName: Full=Reed-Sternberg intermediate filament-associated protein;
DE AltName: Full=Restin;
GN Name=CLIP1; Synonyms=CYLN1, RSN;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND TISSUE SPECIFICITY.
RC TISSUE=Peripheral blood monocyte;
RX PubMed=1600942; DOI=10.1002/j.1460-2075.1992.tb05269.x;
RA Bilbe G., Delabie J., Brueggen J., Richener H., Asselbergs F.A.M.,
RA Cerletti N., Sorg C., Odink K., Tarcsay L., Wiesendanger W.,
RA de Wolf-Peeters C., Shipman R.;
RT "Restin: a novel intermediate filament-associated protein highly expressed
RT in the Reed-Sternberg cells of Hodgkin's disease.";
RL EMBO J. 11:2103-2113(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), AND VARIANT GLU-1080.
RX PubMed=1356075; DOI=10.1016/0092-8674(92)90240-d;
RA Pierre P., Scheel J., Rickard J.E., Kreis T.E.;
RT "CLIP-170 links endocytic vesicles to microtubules.";
RL Cell 70:887-900(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3), AND VARIANTS
RP PRO-941 AND GLU-1080.
RC TISSUE=Colon;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=12433698; DOI=10.1182/blood.v100.12.4139;
RA Sahin U., Neumann F., Tureci O., Schmits R., Perez F., Pfreundschuh M.;
RT "Hodgkin and Reed-Sternberg cell-associated autoantigen CLIP-170/restin is
RT a marker for dendritic cells and is involved in the trafficking of
RT macropinosomes to the cytoskeleton, supporting a function-based concept of
RT Hodgkin and Reed-Sternberg cells.";
RL Blood 100:4139-4145(2002).
RN [5]
RP INTERACTION WITH MTOR, AND PHOSPHORYLATION BY MTOR.
RX PubMed=12231510; DOI=10.1093/embo-reports/kvf197;
RA Choi J.H., Bertram P.G., Drenan R., Carvalho J., Zhou H.H., Zheng X.F.;
RT "The FKBP12-rapamycin-associated protein (FRAP) is a CLIP-170 kinase.";
RL EMBO Rep. 3:988-994(2002).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-200 AND SER-204, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-195, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-48; THR-140; SER-143;
RP SER-147; THR-182; SER-197; SER-200 AND SER-204, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-195; SER-200 AND SER-204, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [11]
RP INTERACTION WITH DCTN1.
RX PubMed=20679239; DOI=10.1073/pnas.1006615107;
RA Li H., Liu X.S., Yang X., Song B., Wang Y., Liu X.;
RT "Polo-like kinase 1 phosphorylation of p150Glued facilitates nuclear
RT envelope breakdown during prophase.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:14633-14638(2010).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-48; THR-140; SER-143;
RP SER-200; SER-204 AND SER-1364, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-50; THR-140; SER-143;
RP THR-182; SER-195; SER-200 AND SER-204, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-200 AND THR-1310, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [16]
RP STRUCTURE BY NMR OF 1-340.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the 1st and 2nd CAP-Gly domain in human CLIP-
RT 170/Restin.";
RL Submitted (NOV-2005) to the PDB data bank.
RN [17]
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 57-128, FUNCTION, SUBUNIT,
RP SUBCELLULAR LOCATION, MUTAGENESIS OF 98-LYS-ASN-99, AND INTERACTION WITH
RP TUBULIN.
RX PubMed=17889670; DOI=10.1016/j.molcel.2007.07.023;
RA Slep K.C., Vale R.D.;
RT "Structural basis of microtubule plus end tracking by XMAP215, CLIP-170,
RT and EB1.";
RL Mol. Cell 27:976-991(2007).
RN [18]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 1388-1427 IN COMPLEX WITH DCTN1.
RX PubMed=17828277; DOI=10.1038/nsmb1291;
RA Weisbrich A., Honnappa S., Jaussi R., Okhrimenko O., Frey D., Jelesarov I.,
RA Akhmanova A., Steinmetz M.O.;
RT "Structure-function relationship of CAP-Gly domains.";
RL Nat. Struct. Mol. Biol. 14:959-967(2007).
RN [19]
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 1416-1438 IN COMPLEX WITH DCTN1
RP AND ZINC, INTERACTION WITH DCTN1, AND ZINC-FINGER.
RX PubMed=17828275; DOI=10.1038/nsmb1299;
RA Hayashi I., Plevin M.J., Ikura M.;
RT "CLIP170 autoinhibition mimics intermolecular interactions with p150Glued
RT or EB1.";
RL Nat. Struct. Mol. Biol. 14:980-981(2007).
RN [20]
RP X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) OF 211-300, STRUCTURE BY NMR OF
RP 203-300 IN COMPLEX WITH TUBA1B, INTERACTION WITH TUBULIN; TUBA1B; MAPRE1
RP AND MAPRE3, FUNCTION, AND ZINC-FINGER DOMAIN.
RX PubMed=17563362; DOI=10.1073/pnas.0703876104;
RA Mishima M., Maesaki R., Kasa M., Watanabe T., Fukata M., Kaibuchi K.,
RA Hakoshima T.;
RT "Structural basis for tubulin recognition by cytoplasmic linker protein 170
RT and its autoinhibition.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:10346-10351(2007).
RN [21]
RP X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 56-127 IN COMPLEX WITH SLAIN2,
RP SUBCELLULAR LOCATION, AND INTERACTION WITH SLAIN2.
RX PubMed=21646404; DOI=10.1083/jcb.201012179;
RA van der Vaart B., Manatschal C., Grigoriev I., Olieric V., Gouveia S.M.,
RA Bjelic S., Demmers J., Vorobjev I., Hoogenraad C.C., Steinmetz M.O.,
RA Akhmanova A.;
RT "SLAIN2 links microtubule plus end-tracking proteins and controls
RT microtubule growth in interphase.";
RL J. Cell Biol. 193:1083-1099(2011).
RN [22]
RP VARIANT [LARGE SCALE ANALYSIS] ILE-1213.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: Binds to the plus end of microtubules and regulates the
CC dynamics of the microtubule cytoskeleton. Promotes microtubule growth
CC and microtubule bundling. Links cytoplasmic vesicles to microtubules
CC and thereby plays an important role in intracellular vesicle
CC trafficking. Plays a role macropinocytosis and endosome trafficking.
CC {ECO:0000269|PubMed:12433698, ECO:0000269|PubMed:17563362,
CC ECO:0000269|PubMed:17889670}.
CC -!- SUBUNIT: Interacts with MTOR; phosphorylates and regulates CLIP1
CC (PubMed:12231510). Interacts (via CAP-Gly domains) with tubulin
CC (PubMed:17563362, PubMed:17889670). Interacts with SLAIN2
CC (PubMed:21646404). Interacts (via zinc finger) with DCTN1
CC (PubMed:17828275, PubMed:20679239). Interacts with TUBA1B, MAPRE1 and
CC MAPRE3 (PubMed:17563362). Binds preferentially to tyrosinated
CC microtubules, and only marginally to detyrosinated microtubules (By
CC similarity). {ECO:0000250|UniProtKB:Q922J3,
CC ECO:0000269|PubMed:12231510, ECO:0000269|PubMed:17563362,
CC ECO:0000269|PubMed:17828275, ECO:0000269|PubMed:17828277,
CC ECO:0000269|PubMed:17889670, ECO:0000269|PubMed:20679239,
CC ECO:0000269|PubMed:21646404}.
CC -!- INTERACTION:
CC P30622; Q15691: MAPRE1; NbExp=2; IntAct=EBI-2683569, EBI-1004115;
CC P30622; Q04864-2: REL; NbExp=3; IntAct=EBI-2683569, EBI-10829018;
CC P30622; P68366: TUBA4A; NbExp=3; IntAct=EBI-2683569, EBI-351772;
CC P30622-1; P30622-1: CLIP1; NbExp=12; IntAct=EBI-9640673, EBI-9640673;
CC P30622-1; Q14203: DCTN1; NbExp=7; IntAct=EBI-9640673, EBI-724352;
CC P30622-1; Q15691: MAPRE1; NbExp=2; IntAct=EBI-9640673, EBI-1004115;
CC P30622-2; Q15691: MAPRE1; NbExp=4; IntAct=EBI-6479976, EBI-1004115;
CC P30622-2; Q71U36: TUBA1A; NbExp=3; IntAct=EBI-6479976, EBI-302552;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:17889670, ECO:0000269|PubMed:21646404}. Cytoplasmic
CC vesicle membrane {ECO:0000269|PubMed:12433698}; Peripheral membrane
CC protein; Cytoplasmic side. Cell projection, ruffle
CC {ECO:0000269|PubMed:12433698}. Note=Localizes to microtubule plus ends
CC (PubMed:21646404, PubMed:17889670). Localizes preferentially to the
CC ends of tyrosinated microtubules (By similarity). Accumulates in plasma
CC membrane regions with ruffling and protrusions. Associates with the
CC membranes of intermediate macropinocytic vesicles (PubMed:12433698).
CC {ECO:0000250|UniProtKB:Q922J3, ECO:0000269|PubMed:12433698,
CC ECO:0000269|PubMed:17889670, ECO:0000269|PubMed:21646404}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=P30622-3; Sequence=Displayed;
CC Name=2; Synonyms=Long;
CC IsoId=P30622-1; Sequence=VSP_038201;
CC Name=3; Synonyms=Short;
CC IsoId=P30622-2; Sequence=VSP_000765;
CC -!- TISSUE SPECIFICITY: Detected in dendritic cells (at protein level).
CC Highly expressed in the Reed-Sternberg cells of Hodgkin disease.
CC {ECO:0000269|PubMed:12433698, ECO:0000269|PubMed:1600942}.
CC -!- DOMAIN: Intramolecular interaction between the zinc finger domain and
CC the CAP-Gly domains may inhibit interaction with tubulin.
CC {ECO:0000269|PubMed:17563362}.
CC -!- PTM: Phosphorylated. Phosphorylation induces conformational changes by
CC increasing the affinity of the N-terminus for C-terminus, resulting in
CC inhibition of its function thus decreasing its binding to microtubules
CC and DCTN1. Exhibits a folded, autoinhibited conformation when
CC phosphorylated and an open conformation when dephosphorylated with
CC increased binding affinity to microtubules and DCTN1. Phosphorylation
CC regulates its recruitment to tyrosinated microtubules and the
CC recruitment of vesicular cargo to microtubules in neurons (By
CC similarity). Phosphorylation by MTOR may positively regulate CLIP1
CC association with microtubules (PubMed:12231510).
CC {ECO:0000250|UniProtKB:Q9JK25, ECO:0000269|PubMed:12231510}.
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DR EMBL; X64838; CAA46050.1; -; mRNA.
DR EMBL; M97501; AAA35693.1; -; mRNA.
DR EMBL; BC114213; AAI14214.1; -; mRNA.
DR EMBL; BC117209; AAI17210.1; -; mRNA.
DR EMBL; BC126305; AAI26306.1; -; mRNA.
DR CCDS; CCDS58285.1; -. [P30622-3]
DR CCDS; CCDS9232.1; -. [P30622-1]
DR CCDS; CCDS9233.1; -. [P30622-2]
DR PIR; A43336; A43336.
DR PIR; S22695; S22695.
DR RefSeq; NP_001234926.1; NM_001247997.1. [P30622-3]
DR RefSeq; NP_002947.1; NM_002956.2. [P30622-1]
DR RefSeq; NP_937883.1; NM_198240.1. [P30622-2]
DR RefSeq; XP_016875275.1; XM_017019786.1. [P30622-1]
DR RefSeq; XP_016875279.1; XM_017019790.1. [P30622-2]
DR PDB; 2CP5; NMR; -; A=1-128.
DR PDB; 2CP6; NMR; -; A=181-339.
DR PDB; 2E3H; X-ray; 1.45 A; A=211-300.
DR PDB; 2E3I; X-ray; 2.00 A; A=56-141.
DR PDB; 2E4H; NMR; -; A=203-300.
DR PDB; 2HQH; X-ray; 1.80 A; E/F/G/H=1416-1438.
DR PDB; 2QK0; X-ray; 2.00 A; A=57-128.
DR PDB; 3E2U; X-ray; 2.60 A; E/F/G/H=1399-1438.
DR PDB; 3RDV; X-ray; 1.75 A; A/B/C/D=56-127.
DR PDBsum; 2CP5; -.
DR PDBsum; 2CP6; -.
DR PDBsum; 2E3H; -.
DR PDBsum; 2E3I; -.
DR PDBsum; 2E4H; -.
DR PDBsum; 2HQH; -.
DR PDBsum; 2QK0; -.
DR PDBsum; 3E2U; -.
DR PDBsum; 3RDV; -.
DR AlphaFoldDB; P30622; -.
DR SMR; P30622; -.
DR BioGRID; 112163; 102.
DR CORUM; P30622; -.
DR DIP; DIP-42826N; -.
DR ELM; P30622; -.
DR IntAct; P30622; 36.
DR MINT; P30622; -.
DR STRING; 9606.ENSP00000479322; -.
DR GlyConnect; 643; 6 N-Linked glycans (3 sites).
DR GlyGen; P30622; 6 sites, 11 N-linked glycans (3 sites), 2 O-linked glycans (3 sites).
DR iPTMnet; P30622; -.
DR MetOSite; P30622; -.
DR PhosphoSitePlus; P30622; -.
DR BioMuta; CLIP1; -.
DR DMDM; 261260059; -.
DR EPD; P30622; -.
DR jPOST; P30622; -.
DR MassIVE; P30622; -.
DR MaxQB; P30622; -.
DR PaxDb; P30622; -.
DR PeptideAtlas; P30622; -.
DR PRIDE; P30622; -.
DR ProteomicsDB; 54727; -. [P30622-3]
DR ProteomicsDB; 54728; -. [P30622-1]
DR ProteomicsDB; 54729; -. [P30622-2]
DR Antibodypedia; 3829; 320 antibodies from 41 providers.
DR DNASU; 6249; -.
DR Ensembl; ENST00000302528.11; ENSP00000303585.7; ENSG00000130779.22. [P30622-1]
DR Ensembl; ENST00000358808.6; ENSP00000351665.2; ENSG00000130779.22. [P30622-1]
DR Ensembl; ENST00000537178.5; ENSP00000445531.1; ENSG00000130779.22. [P30622-2]
DR Ensembl; ENST00000620786.5; ENSP00000479322.1; ENSG00000130779.22. [P30622-3]
DR GeneID; 6249; -.
DR KEGG; hsa:6249; -.
DR MANE-Select; ENST00000620786.5; ENSP00000479322.1; NM_001247997.2; NP_001234926.1.
DR UCSC; uc001ucg.2; human. [P30622-3]
DR CTD; 6249; -.
DR DisGeNET; 6249; -.
DR GeneCards; CLIP1; -.
DR HGNC; HGNC:10461; CLIP1.
DR HPA; ENSG00000130779; Tissue enhanced (tongue).
DR MalaCards; CLIP1; -.
DR MIM; 179838; gene.
DR neXtProt; NX_P30622; -.
DR OpenTargets; ENSG00000130779; -.
DR Orphanet; 88616; Autosomal recessive non-syndromic intellectual disability.
DR PharmGKB; PA162382349; -.
DR VEuPathDB; HostDB:ENSG00000130779; -.
DR eggNOG; KOG4568; Eukaryota.
DR GeneTree; ENSGT00940000155122; -.
DR InParanoid; P30622; -.
DR OMA; HQANEAQ; -.
DR OrthoDB; 1110101at2759; -.
DR PhylomeDB; P30622; -.
DR TreeFam; TF326096; -.
DR PathwayCommons; P30622; -.
DR Reactome; R-HSA-141444; Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal.
DR Reactome; R-HSA-2467813; Separation of Sister Chromatids.
DR Reactome; R-HSA-2500257; Resolution of Sister Chromatid Cohesion.
DR Reactome; R-HSA-5626467; RHO GTPases activate IQGAPs.
DR Reactome; R-HSA-5663220; RHO GTPases Activate Formins.
DR Reactome; R-HSA-68877; Mitotic Prometaphase.
DR Reactome; R-HSA-9648025; EML4 and NUDC in mitotic spindle formation.
DR SignaLink; P30622; -.
DR SIGNOR; P30622; -.
DR BioGRID-ORCS; 6249; 9 hits in 1084 CRISPR screens.
DR ChiTaRS; CLIP1; human.
DR EvolutionaryTrace; P30622; -.
DR GeneWiki; CLIP1; -.
DR GenomeRNAi; 6249; -.
DR Pharos; P30622; Tbio.
DR PRO; PR:P30622; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; P30622; protein.
DR Bgee; ENSG00000130779; Expressed in biceps brachii and 210 other tissues.
DR ExpressionAtlas; P30622; baseline and differential.
DR Genevisible; P30622; HS.
DR GO; GO:0005813; C:centrosome; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005882; C:intermediate filament; TAS:ProtInc.
DR GO; GO:0000776; C:kinetochore; TAS:UniProtKB.
DR GO; GO:0005874; C:microtubule; IMP:Alzheimers_University_of_Toronto.
DR GO; GO:0015630; C:microtubule cytoskeleton; IMP:UniProtKB.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0001726; C:ruffle; IEA:UniProtKB-SubCell.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0008017; F:microtubule binding; IDA:UniProtKB.
DR GO; GO:0051010; F:microtubule plus-end binding; IDA:UniProtKB.
DR GO; GO:0015631; F:tubulin binding; IDA:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
DR GO; GO:0031122; P:cytoplasmic microtubule organization; IBA:GO_Central.
DR GO; GO:0001578; P:microtubule bundle formation; IMP:UniProtKB.
DR GO; GO:0000278; P:mitotic cell cycle; TAS:UniProtKB.
DR GO; GO:0031116; P:positive regulation of microtubule polymerization; IMP:UniProtKB.
DR Gene3D; 2.30.30.190; -; 2.
DR InterPro; IPR036859; CAP-Gly_dom_sf.
DR InterPro; IPR000938; CAP-Gly_domain.
DR InterPro; IPR032108; CLIP1_ZNF.
DR Pfam; PF01302; CAP_GLY; 2.
DR Pfam; PF16641; CLIP1_ZNF; 2.
DR SMART; SM01052; CAP_GLY; 2.
DR SUPFAM; SSF74924; SSF74924; 2.
DR PROSITE; PS00845; CAP_GLY_1; 2.
DR PROSITE; PS50245; CAP_GLY_2; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell projection; Coiled coil;
KW Cytoplasm; Cytoplasmic vesicle; Cytoskeleton; Membrane; Metal-binding;
KW Microtubule; Phosphoprotein; Reference proteome; Repeat; Transport; Zinc;
KW Zinc-finger.
FT CHAIN 1..1438
FT /note="CAP-Gly domain-containing linker protein 1"
FT /id="PRO_0000083527"
FT DOMAIN 78..120
FT /note="CAP-Gly 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00045"
FT DOMAIN 232..274
FT /note="CAP-Gly 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00045"
FT ZN_FING 1417..1434
FT /note="CCHC-type"
FT /evidence="ECO:0000269|PubMed:17563362,
FT ECO:0000269|PubMed:17828275"
FT REGION 97..101
FT /note="Important for tubulin binding"
FT /evidence="ECO:0000269|PubMed:17889670"
FT REGION 129..188
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 302..340
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 987..1006
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1298..1319
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1395..1414
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 350..1353
FT /evidence="ECO:0000255"
FT COMPBIAS 132..188
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 990..1006
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 48
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 50
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 140
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 143
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 147
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 182
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 195
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163"
FT MOD_RES 197
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 200
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 204
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 310
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9JK25"
FT MOD_RES 312
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000250|UniProtKB:Q9JK25"
FT MOD_RES 315
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q922J3"
FT MOD_RES 348
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9JK25"
FT MOD_RES 1236
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9JK25"
FT MOD_RES 1310
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 1364
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT VAR_SEQ 457..502
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:1356075,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_000765"
FT VAR_SEQ 457..467
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:1600942"
FT /id="VSP_038201"
FT VARIANT 162
FT /note="S -> P (in dbSNP:rs7963597)"
FT /id="VAR_059206"
FT VARIANT 780
FT /note="R -> W (in dbSNP:rs3741447)"
FT /id="VAR_048672"
FT VARIANT 941
FT /note="S -> P (in dbSNP:rs17883517)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_048673"
FT VARIANT 1080
FT /note="D -> E (in dbSNP:rs1129167)"
FT /evidence="ECO:0000269|PubMed:1356075,
FT ECO:0000269|PubMed:15489334"
FT /id="VAR_020398"
FT VARIANT 1213
FT /note="M -> I (in a breast cancer sample; somatic mutation;
FT dbSNP:rs1183319975)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036446"
FT VARIANT 1224
FT /note="A -> S (in dbSNP:rs17881033)"
FT /id="VAR_048674"
FT MUTAGEN 98..99
FT /note="KN->EE: Abolishes interaction with tubulin.
FT Abolishes localization at the microtubule plus end."
FT /evidence="ECO:0000269|PubMed:17889670"
FT CONFLICT 193
FT /note="S -> G (in Ref. 3; AAI14214)"
FT /evidence="ECO:0000305"
FT CONFLICT 324
FT /note="S -> P (in Ref. 3; AAI14214)"
FT /evidence="ECO:0000305"
FT CONFLICT 651
FT /note="T -> A (in Ref. 3; AAI14214)"
FT /evidence="ECO:0000305"
FT CONFLICT 682
FT /note="D -> N (in Ref. 3; AAI14214)"
FT /evidence="ECO:0000305"
FT CONFLICT 766
FT /note="L -> P (in Ref. 3; AAI14214)"
FT /evidence="ECO:0000305"
FT CONFLICT 1432
FT /note="C -> R (in Ref. 3; AAI14214)"
FT /evidence="ECO:0000305"
FT STRAND 37..39
FT /evidence="ECO:0007829|PDB:2CP5"
FT STRAND 63..66
FT /evidence="ECO:0007829|PDB:3RDV"
FT TURN 67..69
FT /evidence="ECO:0007829|PDB:3RDV"
FT STRAND 70..78
FT /evidence="ECO:0007829|PDB:3RDV"
FT STRAND 81..85
FT /evidence="ECO:0007829|PDB:3RDV"
FT STRAND 87..95
FT /evidence="ECO:0007829|PDB:3RDV"
FT STRAND 97..103
FT /evidence="ECO:0007829|PDB:3RDV"
FT STRAND 106..108
FT /evidence="ECO:0007829|PDB:3RDV"
FT TURN 113..115
FT /evidence="ECO:0007829|PDB:2QK0"
FT STRAND 116..119
FT /evidence="ECO:0007829|PDB:3RDV"
FT HELIX 121..123
FT /evidence="ECO:0007829|PDB:3RDV"
FT STRAND 124..127
FT /evidence="ECO:0007829|PDB:2E3I"
FT STRAND 193..196
FT /evidence="ECO:0007829|PDB:2CP6"
FT STRAND 217..220
FT /evidence="ECO:0007829|PDB:2E3H"
FT TURN 221..223
FT /evidence="ECO:0007829|PDB:2E3H"
FT STRAND 224..233
FT /evidence="ECO:0007829|PDB:2E3H"
FT STRAND 235..249
FT /evidence="ECO:0007829|PDB:2E3H"
FT STRAND 252..257
FT /evidence="ECO:0007829|PDB:2E3H"
FT STRAND 260..262
FT /evidence="ECO:0007829|PDB:2E3H"
FT TURN 267..269
FT /evidence="ECO:0007829|PDB:2CP6"
FT STRAND 270..274
FT /evidence="ECO:0007829|PDB:2E3H"
FT HELIX 275..277
FT /evidence="ECO:0007829|PDB:2E3H"
FT STRAND 278..280
FT /evidence="ECO:0007829|PDB:2E3H"
FT STRAND 295..298
FT /evidence="ECO:0007829|PDB:2CP6"
FT TURN 1420..1423
FT /evidence="ECO:0007829|PDB:2HQH"
FT STRAND 1424..1427
FT /evidence="ECO:0007829|PDB:2HQH"
FT HELIX 1429..1431
FT /evidence="ECO:0007829|PDB:2HQH"
SQ 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
