ID F5H6A0_HUMAN Unreviewed; 802 AA.
AC F5H6A0;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 2.
DT 27-MAR-2024, entry version 78.
DE SubName: Full=CAP-Gly domain containing linker protein 1 {ECO:0000313|Ensembl:ENSP00000437786.2};
DE Flags: Fragment;
GN Name=CLIP1 {ECO:0000313|Ensembl:ENSP00000437786.2};
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 {ECO:0000313|Ensembl:ENSP00000437786.2, ECO:0000313|Proteomes:UP000005640};
RN [1] {ECO:0007829|PubMed:17081983}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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 [2] {ECO:0007829|PubMed:16964243}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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 [3] {ECO:0000313|Ensembl:ENSP00000437786.2, ECO:0000313|Proteomes:UP000005640}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RG Baylor College of Medicine Human Genome Sequencing Center Sequence Production Team;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA Song X.Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA Nguyen B.V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.,
RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA Gibbs R.A., null.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [4] {ECO:0007829|PubMed:18669648}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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 [5] {ECO:0007829|PubMed:19413330}
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 [6] {ECO:0007829|PubMed:19690332}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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 [7] {ECO:0007829|PubMed:20068231}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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 [8] {ECO:0007829|PubMed:21269460}
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., Burckstummer 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 [9] {ECO:0007829|PubMed:23186163}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=23186163;
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 [10] {ECO:0007829|PubMed:24275569}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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 [11] {ECO:0000313|Ensembl:ENSP00000437786.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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DR EMBL; AC048338; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC079406; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC093016; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC127002; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; F5H6A0; -.
DR SMR; F5H6A0; -.
DR MassIVE; F5H6A0; -.
DR MaxQB; F5H6A0; -.
DR PeptideAtlas; F5H6A0; -.
DR ProteomicsDB; 27124; -.
DR Antibodypedia; 3829; 366 antibodies from 41 providers.
DR Ensembl; ENST00000540304.6; ENSP00000437786.2; ENSG00000130779.22.
DR UCSC; uc058umk.1; human.
DR HGNC; HGNC:10461; CLIP1.
DR VEuPathDB; HostDB:ENSG00000130779; -.
DR GeneTree; ENSGT00940000155122; -.
DR HOGENOM; CLU_001753_0_0_1; -.
DR ChiTaRS; CLIP1; human.
DR Proteomes; UP000005640; Chromosome 12.
DR Bgee; ENSG00000130779; Expressed in biceps brachii and 212 other cell types or tissues.
DR ExpressionAtlas; F5H6A0; baseline and differential.
DR Gene3D; 2.30.30.190; CAP Gly-rich-like domain; 2.
DR Gene3D; 1.20.5.1160; Vasodilator-stimulated phosphoprotein; 1.
DR InterPro; IPR036859; CAP-Gly_dom_sf.
DR InterPro; IPR000938; CAP-Gly_domain.
DR PANTHER; PTHR18916:SF44; CAP-GLY DOMAIN-CONTAINING LINKER PROTEIN 1; 1.
DR PANTHER; PTHR18916; DYNACTIN 1-RELATED MICROTUBULE-BINDING; 1.
DR Pfam; PF01302; CAP_GLY; 2.
DR SMART; SM01052; CAP_GLY; 2.
DR SUPFAM; SSF74924; Cap-Gly domain; 2.
DR PROSITE; PS00845; CAP_GLY_1; 2.
DR PROSITE; PS50245; CAP_GLY_2; 2.
PE 1: Evidence at protein level;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Proteomics identification {ECO:0007829|EPD:F5H6A0,
KW ECO:0007829|MaxQB:F5H6A0};
KW Reference proteome {ECO:0000313|Proteomes:UP000005640}.
FT DOMAIN 78..120
FT /note="CAP-Gly"
FT /evidence="ECO:0000259|PROSITE:PS50245"
FT DOMAIN 232..274
FT /note="CAP-Gly"
FT /evidence="ECO:0000259|PROSITE:PS50245"
FT REGION 129..188
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 302..328
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 781..802
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 337..455
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 132..188
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 802
FT /evidence="ECO:0000313|Ensembl:ENSP00000437786.2"
SQ SEQUENCE 802 AA; 89479 MW; 883FA20DF4420BA2 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 SRTGLHVLEL EAKMDQLRTM VEAADREKVE
LLNQLEEEKR KVEDLQFRVE EESITKGDLE TQTKLEHARI KELEQSLLFE KTKADKLQRE
LEDTRVATVS EKSRIMELEK DLALRVQEVA ELRRRLESNK PAGDVDMSLS LLQEISSLQE
KLEVTRTDHQ REITSLKEHF GAREETHQKE IKALYTATEK LSKENESLKS KLEHANKENS
DVIALWKSKL ETAIASHQQA MEELKVSFSK GLGTETAEFA ELKTQIEKMR LDYQHEIENL
QNQQDSERAA HAKEMEALRA KLMKVIKEKE NSLEAIRSKL DKAEDQHLVE MEDTLNKLQE
AEIKASSITR ELQGRELKLT NLQENLSEVS QVKETLEKEL QILKEKFAEA SEEAVSVQRS
MQETVNKLHQ KEEQFNMLSS DLEKLRENLA DMEAKFREKD EREEQLIKAK EKLENDIAEI
MKMSGDNSSQ LTKMNDELRL KE
//
