Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P30622

- CLIP1_HUMAN

UniProt

P30622 - CLIP1_HUMAN

Protein

CAP-Gly domain-containing linker protein 1

Gene

CLIP1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 151 (01 Oct 2014)
      Sequence version 2 (13 Oct 2009)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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.3 Publications

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri1417 – 143418CCHC-typeAdd
    BLAST

    GO - Molecular functioni

    1. metal ion binding Source: UniProtKB
    2. microtubule binding Source: UniProtKB
    3. microtubule plus-end binding Source: UniProtKB
    4. nucleic acid binding Source: InterPro
    5. protein binding Source: UniProtKB
    6. protein homodimerization activity Source: UniProtKB
    7. tubulin binding Source: UniProtKB
    8. zinc ion binding Source: UniProtKB

    GO - Biological processi

    1. microtubule bundle formation Source: UniProtKB
    2. mitotic cell cycle Source: Reactome
    3. mitotic nuclear division Source: UniProtKB
    4. positive regulation of microtubule polymerization Source: UniProtKB
    5. transport Source: UniProtKB-KW

    Keywords - Biological processi

    Transport

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_150425. Resolution of Sister Chromatid Cohesion.
    REACT_150471. Separation of Sister Chromatids.
    REACT_682. Mitotic Prometaphase.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    CAP-Gly domain-containing linker protein 1
    Alternative name(s):
    Cytoplasmic linker protein 1
    Cytoplasmic linker protein 170 alpha-2
    Short name:
    CLIP-170
    Reed-Sternberg intermediate filament-associated protein
    Restin
    Gene namesi
    Name:CLIP1
    Synonyms:CYLN1, RSN
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 12

    Organism-specific databases

    HGNCiHGNC:10461. CLIP1.

    Subcellular locationi

    Cytoplasm. Cytoplasmcytoskeleton. Cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side. Cell projectionruffle
    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.

    GO - Cellular componenti

    1. centrosome Source: UniProtKB
    2. cytoplasmic microtubule Source: Ensembl
    3. cytoplasmic vesicle membrane Source: UniProtKB-SubCell
    4. cytosol Source: Reactome
    5. endosome Source: ProtInc
    6. intermediate filament Source: ProtInc
    7. kinetochore Source: UniProtKB
    8. microtubule Source: UniProtKB
    9. microtubule cytoskeleton Source: UniProtKB
    10. microtubule plus-end Source: Ensembl
    11. ruffle Source: UniProtKB-SubCell

    Keywords - Cellular componenti

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

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi98 – 992KN → EE: Abolishes interaction with tubulin. Abolishes localization at the microtubule plus end. 1 Publication

    Organism-specific databases

    PharmGKBiPA162382349.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 14381438CAP-Gly domain-containing linker protein 1PRO_0000083527Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei48 – 481Phosphoserine3 Publications
    Modified residuei140 – 1401Phosphothreonine3 Publications
    Modified residuei143 – 1431Phosphoserine3 Publications
    Modified residuei147 – 1471Phosphoserine2 Publications
    Modified residuei182 – 1821Phosphothreonine2 Publications
    Modified residuei195 – 1951Phosphoserine3 Publications
    Modified residuei197 – 1971Phosphoserine2 Publications
    Modified residuei200 – 2001Phosphoserine5 Publications
    Modified residuei204 – 2041Phosphoserine5 Publications
    Modified residuei1364 – 13641Phosphoserine2 Publications

    Post-translational modificationi

    Phosphorylated. Phosphorylation by MTOR may positively regulate CLIP1 association with microtubules.6 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP30622.
    PaxDbiP30622.
    PRIDEiP30622.

    PTM databases

    PhosphoSiteiP30622.

    Expressioni

    Tissue specificityi

    Detected in dendritic cells (at protein level). Highly expressed in the Reed-Sternberg cells of Hodgkin disease.2 Publications

    Gene expression databases

    ArrayExpressiP30622.
    BgeeiP30622.
    CleanExiHS_CLIP1.
    GenevestigatoriP30622.

    Organism-specific databases

    HPAiCAB004399.
    HPA026678.

    Interactioni

    Subunit structurei

    Interacts with MTOR; phosphorylates and regulates CLIP1. Interacts (via CAP-Gly domains) with tubulin. Interacts with SLAIN2. Interacts (via zinc finger) with DCTN1. Interacts with MAPRE1 and MAPRE3.6 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    TUBA4AP683663EBI-2683569,EBI-351772

    Protein-protein interaction databases

    BioGridi112163. 16 interactions.
    DIPiDIP-42826N.
    IntActiP30622. 13 interactions.
    MINTiMINT-1781312.
    STRINGi9606.ENSP00000351665.

    Structurei

    Secondary structure

    1
    1438
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi37 – 393
    Beta strandi63 – 664
    Turni67 – 693
    Beta strandi70 – 789
    Beta strandi81 – 855
    Beta strandi87 – 959
    Beta strandi97 – 1037
    Beta strandi106 – 1083
    Turni113 – 1153
    Beta strandi116 – 1194
    Helixi121 – 1233
    Beta strandi124 – 1274
    Beta strandi193 – 1964
    Beta strandi217 – 2204
    Turni221 – 2233
    Beta strandi224 – 23310
    Beta strandi235 – 24915
    Beta strandi252 – 2576
    Beta strandi260 – 2623
    Turni267 – 2693
    Beta strandi270 – 2745
    Helixi275 – 2773
    Beta strandi278 – 2803
    Beta strandi295 – 2984
    Turni1420 – 14234
    Beta strandi1424 – 14274
    Helixi1429 – 14313

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2CP5NMR-A1-128[»]
    2CP6NMR-A181-339[»]
    2E3HX-ray1.45A211-300[»]
    2E3IX-ray2.00A56-141[»]
    2E4HNMR-A203-300[»]
    2HQHX-ray1.80E/F/G/H1416-1438[»]
    2QK0X-ray2.00A57-128[»]
    3E2UX-ray2.60E/F/G/H1399-1438[»]
    3RDVX-ray1.75A/B/C/D56-127[»]
    ProteinModelPortaliP30622.
    SMRiP30622. Positions 4-130, 181-340.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP30622.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini78 – 12043CAP-Gly 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini232 – 27443CAP-Gly 2PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni97 – 1015Important for tubulin binding

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili350 – 13531004Sequence AnalysisAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi143 – 20462Ser-richAdd
    BLAST
    Compositional biasi304 – 33128Ser-richAdd
    BLAST

    Domaini

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

    Sequence similaritiesi

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

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri1417 – 143418CCHC-typeAdd
    BLAST

    Keywords - Domaini

    Coiled coil, Repeat, Zinc-finger

    Phylogenomic databases

    eggNOGiCOG5244.
    HOGENOMiHOG000092755.
    HOVERGENiHBG007123.
    KOiK10421.
    OMAiHSQCQDL.
    PhylomeDBiP30622.
    TreeFamiTF326096.

    Family and domain databases

    Gene3Di2.30.30.190. 2 hits.
    InterProiIPR000938. CAP-Gly_domain.
    IPR001878. Znf_CCHC.
    [Graphical view]
    PfamiPF01302. CAP_GLY. 2 hits.
    [Graphical view]
    SMARTiSM01052. CAP_GLY. 2 hits.
    SM00343. ZnF_C2HC. 1 hit.
    [Graphical view]
    SUPFAMiSSF74924. SSF74924. 2 hits.
    PROSITEiPS00845. CAP_GLY_1. 2 hits.
    PS50245. CAP_GLY_2. 2 hits.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P30622-3) [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

    MSMLKPSGLK APTKILKPGS TALKTPTAVV APVEKTISSE KASSTPSSET     50
    QEEFVDDFRV GERVWVNGNK PGFIQFLGET QFAPGQWAGI VLDEPIGKND 100
    GSVAGVRYFQ CEPLKGIFTR PSKLTRKVQA EDEANGLQTT PASRATSPLC 150
    TSTASMVSSS PSTPSNIPQK PSQPAAKEPS ATPPISNLTK TASESISNLS 200
    EAGSIKKGER ELKIGDRVLV GGTKAGVVRF LGETDFAKGE WCGVELDEPL 250
    GKNDGAVAGT RYFQCQPKYG LFAPVHKVTK IGFPSTTPAK AKANAVRRVM 300
    ATTSASLKRS PSASSLSSMS SVASSVSSRP SRTGLLTETS SRYARKISGT 350
    TALQEALKEK QQHIEQLLAE RDLERAEVAK ATSHVGEIEQ ELALARDGHD 400
    QHVLELEAKM DQLRTMVEAA DREKVELLNQ LEEEKRKVED LQFRVEEESI 450
    TKGDLEQKSQ ISEDPENTQT KLEHARIKEL EQSLLFEKTK ADKLQRELED 500
    TRVATVSEKS RIMELEKDLA LRVQEVAELR RRLESNKPAG DVDMSLSLLQ 550
    EISSLQEKLE VTRTDHQREI TSLKEHFGAR EETHQKEIKA LYTATEKLSK 600
    ENESLKSKLE HANKENSDVI ALWKSKLETA IASHQQAMEE LKVSFSKGLG 650
    TETAEFAELK TQIEKMRLDY QHEIENLQNQ QDSERAAHAK EMEALRAKLM 700
    KVIKEKENSL EAIRSKLDKA EDQHLVEMED TLNKLQEAEI KVKELEVLQA 750
    KCNEQTKVID NFTSQLKATE EKLLDLDALR KASSEGKSEM KKLRQQLEAA 800
    EKQIKHLEIE KNAESSKASS ITRELQGREL KLTNLQENLS EVSQVKETLE 850
    KELQILKEKF AEASEEAVSV QRSMQETVNK LHQKEEQFNM LSSDLEKLRE 900
    NLADMEAKFR EKDEREEQLI KAKEKLENDI AEIMKMSGDN SSQLTKMNDE 950
    LRLKERDVEE LQLKLTKANE NASFLQKSIE DMTVKAEQSQ QEAAKKHEEE 1000
    KKELERKLSD LEKKMETSHN QCQELKARYE RATSETKTKH EEILQNLQKT 1050
    LLDTEDKLKG AREENSGLLQ ELEELRKQAD KAKAAQTAED AMQIMEQMTK 1100
    EKTETLASLE DTKQTNAKLQ NELDTLKENN LKNVEELNKS KELLTVENQK 1150
    MEEFRKEIET LKQAAAQKSQ QLSALQEENV KLAEELGRSR DEVTSHQKLE 1200
    EERSVLNNQL LEMKKRESKF IKDADEEKAS LQKSISITSA LLTEKDAELE 1250
    KLRNEVTVLR GENASAKSLH SVVQTLESDK VKLELKVKNL ELQLKENKRQ 1300
    LSSSSGNTDT QADEDERAQE SQIDFLNSVI VDLQRKNQDL KMKVEMMSEA 1350
    ALNGNGDDLN NYDSDDQEKQ SKKKPRLFCD ICDCFDLHDT EDCPTQAQMS 1400
    EDPPHSTHHG SRGEERPYCE ICEMFGHWAT NCNDDETF 1438
    Length:1,438
    Mass (Da):162,246
    Last modified:October 13, 2009 - v2
    Checksum:iA7F125F7A96DBDDB
    GO
    Isoform 2 (identifier: P30622-1) [UniParc]FASTAAdd to Basket

    Also known as: Long

    The sequence of this isoform differs from the canonical sequence as follows:
         457-467: Missing.

    Show »
    Length:1,427
    Mass (Da):160,990
    Checksum:i0A4F166DD94254E8
    GO
    Isoform 3 (identifier: P30622-2) [UniParc]FASTAAdd to Basket

    Also known as: Short

    The sequence of this isoform differs from the canonical sequence as follows:
         457-502: Missing.

    Show »
    Length:1,392
    Mass (Da):156,781
    Checksum:i959DF99064762A10
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti193 – 1931S → G in AAI14214. (PubMed:15489334)Curated
    Sequence conflicti324 – 3241S → P in AAI14214. (PubMed:15489334)Curated
    Sequence conflicti651 – 6511T → A in AAI14214. (PubMed:15489334)Curated
    Sequence conflicti682 – 6821D → N in AAI14214. (PubMed:15489334)Curated
    Sequence conflicti766 – 7661L → P in AAI14214. (PubMed:15489334)Curated
    Sequence conflicti1432 – 14321C → R in AAI14214. (PubMed:15489334)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti162 – 1621S → P.
    Corresponds to variant rs7963597 [ dbSNP | Ensembl ].
    VAR_059206
    Natural varianti780 – 7801R → W.
    Corresponds to variant rs3741447 [ dbSNP | Ensembl ].
    VAR_048672
    Natural varianti941 – 9411S → P.1 Publication
    Corresponds to variant rs17883517 [ dbSNP | Ensembl ].
    VAR_048673
    Natural varianti1080 – 10801D → E.2 Publications
    Corresponds to variant rs1129167 [ dbSNP | Ensembl ].
    VAR_020398
    Natural varianti1213 – 12131M → I in a breast cancer sample; somatic mutation. 1 Publication
    VAR_036446
    Natural varianti1224 – 12241A → S.
    Corresponds to variant rs17881033 [ dbSNP | Ensembl ].
    VAR_048674

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei457 – 50246Missing in isoform 3. 2 PublicationsVSP_000765Add
    BLAST
    Alternative sequencei457 – 46711Missing in isoform 2. 1 PublicationVSP_038201Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X64838 mRNA. Translation: CAA46050.1.
    M97501 mRNA. Translation: AAA35693.1.
    BC114213 mRNA. Translation: AAI14214.1.
    BC117209 mRNA. Translation: AAI17210.1.
    BC126305 mRNA. Translation: AAI26306.1.
    CCDSiCCDS58285.1. [P30622-3]
    CCDS9232.1. [P30622-1]
    CCDS9233.1. [P30622-2]
    PIRiA43336.
    S22695.
    RefSeqiNP_001234926.1. NM_001247997.1. [P30622-3]
    NP_002947.1. NM_002956.2. [P30622-1]
    NP_937883.1. NM_198240.1. [P30622-2]
    UniGeneiHs.524809.

    Genome annotation databases

    EnsembliENST00000302528; ENSP00000303585; ENSG00000130779. [P30622-1]
    ENST00000358808; ENSP00000351665; ENSG00000130779. [P30622-1]
    ENST00000537178; ENSP00000445531; ENSG00000130779. [P30622-2]
    ENST00000540338; ENSP00000439093; ENSG00000130779. [P30622-3]
    GeneIDi6249.
    KEGGihsa:6249.
    UCSCiuc001ucg.2. human. [P30622-3]
    uc001uch.1. human. [P30622-1]
    uc001uci.1. human. [P30622-2]

    Polymorphism databases

    DMDMi261260059.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X64838 mRNA. Translation: CAA46050.1 .
    M97501 mRNA. Translation: AAA35693.1 .
    BC114213 mRNA. Translation: AAI14214.1 .
    BC117209 mRNA. Translation: AAI17210.1 .
    BC126305 mRNA. Translation: AAI26306.1 .
    CCDSi CCDS58285.1. [P30622-3 ]
    CCDS9232.1. [P30622-1 ]
    CCDS9233.1. [P30622-2 ]
    PIRi A43336.
    S22695.
    RefSeqi NP_001234926.1. NM_001247997.1. [P30622-3 ]
    NP_002947.1. NM_002956.2. [P30622-1 ]
    NP_937883.1. NM_198240.1. [P30622-2 ]
    UniGenei Hs.524809.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2CP5 NMR - A 1-128 [» ]
    2CP6 NMR - A 181-339 [» ]
    2E3H X-ray 1.45 A 211-300 [» ]
    2E3I X-ray 2.00 A 56-141 [» ]
    2E4H NMR - A 203-300 [» ]
    2HQH X-ray 1.80 E/F/G/H 1416-1438 [» ]
    2QK0 X-ray 2.00 A 57-128 [» ]
    3E2U X-ray 2.60 E/F/G/H 1399-1438 [» ]
    3RDV X-ray 1.75 A/B/C/D 56-127 [» ]
    ProteinModelPortali P30622.
    SMRi P30622. Positions 4-130, 181-340.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 112163. 16 interactions.
    DIPi DIP-42826N.
    IntActi P30622. 13 interactions.
    MINTi MINT-1781312.
    STRINGi 9606.ENSP00000351665.

    PTM databases

    PhosphoSitei P30622.

    Polymorphism databases

    DMDMi 261260059.

    Proteomic databases

    MaxQBi P30622.
    PaxDbi P30622.
    PRIDEi P30622.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000302528 ; ENSP00000303585 ; ENSG00000130779 . [P30622-1 ]
    ENST00000358808 ; ENSP00000351665 ; ENSG00000130779 . [P30622-1 ]
    ENST00000537178 ; ENSP00000445531 ; ENSG00000130779 . [P30622-2 ]
    ENST00000540338 ; ENSP00000439093 ; ENSG00000130779 . [P30622-3 ]
    GeneIDi 6249.
    KEGGi hsa:6249.
    UCSCi uc001ucg.2. human. [P30622-3 ]
    uc001uch.1. human. [P30622-1 ]
    uc001uci.1. human. [P30622-2 ]

    Organism-specific databases

    CTDi 6249.
    GeneCardsi GC12M122755.
    HGNCi HGNC:10461. CLIP1.
    HPAi CAB004399.
    HPA026678.
    MIMi 179838. gene.
    neXtProti NX_P30622.
    PharmGKBi PA162382349.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5244.
    HOGENOMi HOG000092755.
    HOVERGENi HBG007123.
    KOi K10421.
    OMAi HSQCQDL.
    PhylomeDBi P30622.
    TreeFami TF326096.

    Enzyme and pathway databases

    Reactomei REACT_150425. Resolution of Sister Chromatid Cohesion.
    REACT_150471. Separation of Sister Chromatids.
    REACT_682. Mitotic Prometaphase.

    Miscellaneous databases

    ChiTaRSi CLIP1. human.
    EvolutionaryTracei P30622.
    GeneWikii CLIP1.
    GenomeRNAii 6249.
    NextBioi 24265.
    PROi P30622.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P30622.
    Bgeei P30622.
    CleanExi HS_CLIP1.
    Genevestigatori P30622.

    Family and domain databases

    Gene3Di 2.30.30.190. 2 hits.
    InterProi IPR000938. CAP-Gly_domain.
    IPR001878. Znf_CCHC.
    [Graphical view ]
    Pfami PF01302. CAP_GLY. 2 hits.
    [Graphical view ]
    SMARTi SM01052. CAP_GLY. 2 hits.
    SM00343. ZnF_C2HC. 1 hit.
    [Graphical view ]
    SUPFAMi SSF74924. SSF74924. 2 hits.
    PROSITEi PS00845. CAP_GLY_1. 2 hits.
    PS50245. CAP_GLY_2. 2 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Restin: a novel intermediate filament-associated protein highly expressed in the Reed-Sternberg cells of Hodgkin's disease."
      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.
      EMBO J. 11:2103-2113(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), TISSUE SPECIFICITY.
      Tissue: Peripheral blood monocyte.
    2. "CLIP-170 links endocytic vesicles to microtubules."
      Pierre P., Scheel J., Rickard J.E., Kreis T.E.
      Cell 70:887-900(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), VARIANT GLU-1080.
    3. "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] (ISOFORMS 1 AND 3), VARIANTS PRO-941 AND GLU-1080.
      Tissue: Colon.
    4. "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."
      Sahin U., Neumann F., Tureci O., Schmits R., Perez F., Pfreundschuh M.
      Blood 100:4139-4145(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    5. "The FKBP12-rapamycin-associated protein (FRAP) is a CLIP-170 kinase."
      Choi J.H., Bertram P.G., Drenan R., Carvalho J., Zhou H.H., Zheng X.F.
      EMBO Rep. 3:988-994(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH MTOR, PHOSPHORYLATION BY MTOR.
    6. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-200 AND SER-204, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    7. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
      Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
      Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-195, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    8. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-48; THR-140; SER-143; SER-147; THR-182; SER-197; SER-200 AND SER-204, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    9. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    10. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-195; SER-200 AND SER-204, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    11. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      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.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-48; THR-140; SER-143; SER-200; SER-204 AND SER-1364, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. "Solution structure of the 1st and 2nd CAP-Gly domain in human CLIP-170/Restin."
      RIKEN structural genomics initiative (RSGI)
      Submitted (NOV-2005) to the PDB data bank
      Cited for: STRUCTURE BY NMR OF 1-340.
    14. "Structural basis of microtubule plus end tracking by XMAP215, CLIP-170, and EB1."
      Slep K.C., Vale R.D.
      Mol. Cell 27:976-991(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 57-128, FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, MUTAGENESIS OF 98-LYS-ASN-99, INTERACTION WITH TUBULIN.
    15. Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 1388-1427 IN COMPLEX WITH DCTN1.
    16. "CLIP170 autoinhibition mimics intermolecular interactions with p150Glued or EB1."
      Hayashi I., Plevin M.J., Ikura M.
      Nat. Struct. Mol. Biol. 14:980-981(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 1416-1438 IN COMPLEX WITH DCTN1 AND ZINC, INTERACTION WITH DCTN1, ZINC-FINGER.
    17. "Structural basis for tubulin recognition by cytoplasmic linker protein 170 and its autoinhibition."
      Mishima M., Maesaki R., Kasa M., Watanabe T., Fukata M., Kaibuchi K., Hakoshima T.
      Proc. Natl. Acad. Sci. U.S.A. 104:10346-10351(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: 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, ZINC-FINGER DOMAIN.
    18. "SLAIN2 links microtubule plus end-tracking proteins and controls microtubule growth in interphase."
      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.
      J. Cell Biol. 193:1083-1099(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 56-127 IN COMPLEX WITH SLAIN2, SUBCELLULAR LOCATION.
    19. Cited for: VARIANT [LARGE SCALE ANALYSIS] ILE-1213.

    Entry informationi

    Entry nameiCLIP1_HUMAN
    AccessioniPrimary (citable) accession number: P30622
    Secondary accession number(s): A0AVD3, Q17RS4, Q29RG0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1993
    Last sequence update: October 13, 2009
    Last modified: October 1, 2014
    This is version 151 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 12
      Human chromosome 12: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3