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P30622

- CLIP1_HUMAN

UniProt

P30622 - CLIP1_HUMAN

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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

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 homodimerization activity Source: UniProtKB
  6. tubulin binding Source: UniProtKB
  7. 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
Complete GO annotation...

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. cell projection Source: UniProtKB-KW
  2. centrosome Source: UniProtKB
  3. cytoplasmic vesicle Source: UniProtKB-KW
  4. cytosol Source: Reactome
  5. endosome Source: ProtInc
  6. intermediate filament Source: ProtInc
  7. kinetochore Source: UniProtKB
  8. membrane Source: UniProtKB-KW
  9. microtubule Source: UniProtKB
  10. microtubule cytoskeleton Source: UniProtKB
Complete GO annotation...

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

Orphaneti88616. Autosomal recessive non-syndromic intellectual disability.
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 – 481Phosphoserine2 Publications
Modified residuei140 – 1401Phosphothreonine2 Publications
Modified residuei143 – 1431Phosphoserine2 Publications
Modified residuei147 – 1471Phosphoserine1 Publication
Modified residuei182 – 1821Phosphothreonine1 Publication
Modified residuei195 – 1951Phosphoserine2 Publications
Modified residuei197 – 1971Phosphoserine1 Publication
Modified residuei200 – 2001Phosphoserine4 Publications
Modified residuei204 – 2041Phosphoserine4 Publications
Modified residuei1364 – 13641Phosphoserine1 Publication

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

BgeeiP30622.
CleanExiHS_CLIP1.
ExpressionAtlasiP30622. baseline and differential.
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. 17 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 – 393Combined sources
Beta strandi63 – 664Combined sources
Turni67 – 693Combined sources
Beta strandi70 – 789Combined sources
Beta strandi81 – 855Combined sources
Beta strandi87 – 959Combined sources
Beta strandi97 – 1037Combined sources
Beta strandi106 – 1083Combined sources
Turni113 – 1153Combined sources
Beta strandi116 – 1194Combined sources
Helixi121 – 1233Combined sources
Beta strandi124 – 1274Combined sources
Beta strandi193 – 1964Combined sources
Beta strandi217 – 2204Combined sources
Turni221 – 2233Combined sources
Beta strandi224 – 23310Combined sources
Beta strandi235 – 24915Combined sources
Beta strandi252 – 2576Combined sources
Beta strandi260 – 2623Combined sources
Turni267 – 2693Combined sources
Beta strandi270 – 2745Combined sources
Helixi275 – 2773Combined sources
Beta strandi278 – 2803Combined sources
Beta strandi295 – 2984Combined sources
Turni1420 – 14234Combined sources
Beta strandi1424 – 14274Combined sources
Helixi1429 – 14313Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
GeneTreeiENSGT00760000119173.
HOGENOMiHOG000092755.
HOVERGENiHBG007123.
InParanoidiP30622.
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

        10         20         30         40         50
MSMLKPSGLK APTKILKPGS TALKTPTAVV APVEKTISSE KASSTPSSET
60 70 80 90 100
QEEFVDDFRV GERVWVNGNK PGFIQFLGET QFAPGQWAGI VLDEPIGKND
110 120 130 140 150
GSVAGVRYFQ CEPLKGIFTR PSKLTRKVQA EDEANGLQTT PASRATSPLC
160 170 180 190 200
TSTASMVSSS PSTPSNIPQK PSQPAAKEPS ATPPISNLTK TASESISNLS
210 220 230 240 250
EAGSIKKGER ELKIGDRVLV GGTKAGVVRF LGETDFAKGE WCGVELDEPL
260 270 280 290 300
GKNDGAVAGT RYFQCQPKYG LFAPVHKVTK IGFPSTTPAK AKANAVRRVM
310 320 330 340 350
ATTSASLKRS PSASSLSSMS SVASSVSSRP SRTGLLTETS SRYARKISGT
360 370 380 390 400
TALQEALKEK QQHIEQLLAE RDLERAEVAK ATSHVGEIEQ ELALARDGHD
410 420 430 440 450
QHVLELEAKM DQLRTMVEAA DREKVELLNQ LEEEKRKVED LQFRVEEESI
460 470 480 490 500
TKGDLEQKSQ ISEDPENTQT KLEHARIKEL EQSLLFEKTK ADKLQRELED
510 520 530 540 550
TRVATVSEKS RIMELEKDLA LRVQEVAELR RRLESNKPAG DVDMSLSLLQ
560 570 580 590 600
EISSLQEKLE VTRTDHQREI TSLKEHFGAR EETHQKEIKA LYTATEKLSK
610 620 630 640 650
ENESLKSKLE HANKENSDVI ALWKSKLETA IASHQQAMEE LKVSFSKGLG
660 670 680 690 700
TETAEFAELK TQIEKMRLDY QHEIENLQNQ QDSERAAHAK EMEALRAKLM
710 720 730 740 750
KVIKEKENSL EAIRSKLDKA EDQHLVEMED TLNKLQEAEI KVKELEVLQA
760 770 780 790 800
KCNEQTKVID NFTSQLKATE EKLLDLDALR KASSEGKSEM KKLRQQLEAA
810 820 830 840 850
EKQIKHLEIE KNAESSKASS ITRELQGREL KLTNLQENLS EVSQVKETLE
860 870 880 890 900
KELQILKEKF AEASEEAVSV QRSMQETVNK LHQKEEQFNM LSSDLEKLRE
910 920 930 940 950
NLADMEAKFR EKDEREEQLI KAKEKLENDI AEIMKMSGDN SSQLTKMNDE
960 970 980 990 1000
LRLKERDVEE LQLKLTKANE NASFLQKSIE DMTVKAEQSQ QEAAKKHEEE
1010 1020 1030 1040 1050
KKELERKLSD LEKKMETSHN QCQELKARYE RATSETKTKH EEILQNLQKT
1060 1070 1080 1090 1100
LLDTEDKLKG AREENSGLLQ ELEELRKQAD KAKAAQTAED AMQIMEQMTK
1110 1120 1130 1140 1150
EKTETLASLE DTKQTNAKLQ NELDTLKENN LKNVEELNKS KELLTVENQK
1160 1170 1180 1190 1200
MEEFRKEIET LKQAAAQKSQ QLSALQEENV KLAEELGRSR DEVTSHQKLE
1210 1220 1230 1240 1250
EERSVLNNQL LEMKKRESKF IKDADEEKAS LQKSISITSA LLTEKDAELE
1260 1270 1280 1290 1300
KLRNEVTVLR GENASAKSLH SVVQTLESDK VKLELKVKNL ELQLKENKRQ
1310 1320 1330 1340 1350
LSSSSGNTDT QADEDERAQE SQIDFLNSVI VDLQRKNQDL KMKVEMMSEA
1360 1370 1380 1390 1400
ALNGNGDDLN NYDSDDQEKQ SKKKPRLFCD ICDCFDLHDT EDCPTQAQMS
1410 1420 1430
EDPPHSTHHG SRGEERPYCE ICEMFGHWAT NCNDDETF
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:
EMBLi
GenBanki
DDBJi
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]
ENST00000620786; ENSP00000479322; 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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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. 17 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 ]
ENST00000620786 ; ENSP00000479322 ; 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.
Orphaneti 88616. Autosomal recessive non-syndromic intellectual disability.
PharmGKBi PA162382349.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5244.
GeneTreei ENSGT00760000119173.
HOGENOMi HOG000092755.
HOVERGENi HBG007123.
InParanoidi P30622.
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

Bgeei P30622.
CleanExi HS_CLIP1.
ExpressionAtlasi P30622. baseline and differential.
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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 153 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

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