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P30622 (CLIP1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 146. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:CLIP1
Synonyms:CYLN1, RSN
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1438 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

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. Ref.4 Ref.14 Ref.17

Subunit structure

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. Ref.5 Ref.14 Ref.16 Ref.17

Subcellular location

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. Ref.4 Ref.14 Ref.18

Tissue specificity

Detected in dendritic cells (at protein level). Highly expressed in the Reed-Sternberg cells of Hodgkin disease. Ref.1 Ref.4

Domain

Intramolecular interaction between the zinc finger domain and the CAP-Gly domains may inhibit interaction with tubulin. Ref.17

Post-translational modification

Phosphorylated. Phosphorylation by MTOR may positively regulate CLIP1 association with microtubules. Ref.5

Sequence similarities

Contains 2 CAP-Gly domains.

Contains 1 CCHC-type zinc finger.

Ontologies

Keywords
   Biological processTransport
   Cellular componentCell projection
Cytoplasm
Cytoplasmic vesicle
Cytoskeleton
Membrane
Microtubule
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainCoiled coil
Repeat
Zinc-finger
   LigandMetal-binding
Zinc
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processmicrotubule bundle formation

Inferred from mutant phenotype Ref.14. Source: UniProtKB

mitosis

Traceable author statement PubMed 15928712. Source: UniProtKB

mitotic cell cycle

Traceable author statement. Source: Reactome

positive regulation of microtubule polymerization

Inferred from mutant phenotype PubMed 15262990Ref.14. Source: UniProtKB

transport

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcentrosome

Inferred from direct assay PubMed 21399614. Source: UniProtKB

cytoplasmic microtubule

Inferred from electronic annotation. Source: Ensembl

cytoplasmic vesicle membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

cytosol

Traceable author statement. Source: Reactome

endosome

Traceable author statement Ref.2. Source: ProtInc

intermediate filament

Traceable author statement Ref.1. Source: ProtInc

kinetochore

Traceable author statement PubMed 15928712. Source: UniProtKB

microtubule

Inferred from sequence or structural similarity. Source: UniProtKB

microtubule cytoskeleton

Inferred from mutant phenotype Ref.14. Source: UniProtKB

microtubule plus-end

Inferred from electronic annotation. Source: Ensembl

ruffle

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionmetal ion binding

Non-traceable author statement PubMed 15928712. Source: UniProtKB

microtubule binding

Inferred from direct assay Ref.14. Source: UniProtKB

microtubule plus-end binding

Inferred from direct assay Ref.4. Source: UniProtKB

nucleic acid binding

Inferred from electronic annotation. Source: InterPro

protein homodimerization activity

Traceable author statement PubMed 15928712. Source: UniProtKB

tubulin binding

Inferred from direct assay Ref.14. Source: UniProtKB

zinc ion binding

Inferred from direct assay Ref.16. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

TUBA4AP683663EBI-2683569,EBI-351772

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P30622-3)

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.
Isoform 2 (identifier: P30622-1)

Also known as: Long;

The sequence of this isoform differs from the canonical sequence as follows:
     457-467: Missing.
Isoform 3 (identifier: P30622-2)

Also known as: Short;

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 14381438CAP-Gly domain-containing linker protein 1
PRO_0000083527

Regions

Domain78 – 12043CAP-Gly 1
Domain232 – 27443CAP-Gly 2
Zinc finger1417 – 143418CCHC-type
Region97 – 1015Important for tubulin binding
Coiled coil350 – 13531004 Potential
Compositional bias143 – 20462Ser-rich
Compositional bias304 – 33128Ser-rich

Amino acid modifications

Modified residue481Phosphoserine Ref.8 Ref.11
Modified residue1401Phosphothreonine Ref.8 Ref.11
Modified residue1431Phosphoserine Ref.8 Ref.11
Modified residue1471Phosphoserine Ref.8
Modified residue1821Phosphothreonine Ref.8
Modified residue1951Phosphoserine Ref.7 Ref.10
Modified residue1971Phosphoserine Ref.8
Modified residue2001Phosphoserine Ref.6 Ref.8 Ref.10 Ref.11
Modified residue2041Phosphoserine Ref.6 Ref.8 Ref.10 Ref.11
Modified residue13641Phosphoserine Ref.11

Natural variations

Alternative sequence457 – 50246Missing in isoform 3.
VSP_000765
Alternative sequence457 – 46711Missing in isoform 2.
VSP_038201
Natural variant1621S → P.
Corresponds to variant rs7963597 [ dbSNP | Ensembl ].
VAR_059206
Natural variant7801R → W.
Corresponds to variant rs3741447 [ dbSNP | Ensembl ].
VAR_048672
Natural variant9411S → P. Ref.3
Corresponds to variant rs17883517 [ dbSNP | Ensembl ].
VAR_048673
Natural variant10801D → E. Ref.2 Ref.3
Corresponds to variant rs1129167 [ dbSNP | Ensembl ].
VAR_020398
Natural variant12131M → I in a breast cancer sample; somatic mutation. Ref.19
VAR_036446
Natural variant12241A → S.
Corresponds to variant rs17881033 [ dbSNP | Ensembl ].
VAR_048674

Experimental info

Mutagenesis98 – 992KN → EE: Abolishes interaction with tubulin. Abolishes localization at the microtubule plus end. Ref.14
Sequence conflict1931S → G in AAI14214. Ref.3
Sequence conflict3241S → P in AAI14214. Ref.3
Sequence conflict6511T → A in AAI14214. Ref.3
Sequence conflict6821D → N in AAI14214. Ref.3
Sequence conflict7661L → P in AAI14214. Ref.3
Sequence conflict14321C → R in AAI14214. Ref.3

Secondary structure

............................................. 1438
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified October 13, 2009. Version 2.
Checksum: A7F125F7A96DBDDB

FASTA1,438162,246
        10         20         30         40         50         60 
MSMLKPSGLK APTKILKPGS TALKTPTAVV APVEKTISSE KASSTPSSET QEEFVDDFRV 

        70         80         90        100        110        120 
GERVWVNGNK PGFIQFLGET QFAPGQWAGI VLDEPIGKND GSVAGVRYFQ CEPLKGIFTR 

       130        140        150        160        170        180 
PSKLTRKVQA EDEANGLQTT PASRATSPLC TSTASMVSSS PSTPSNIPQK PSQPAAKEPS 

       190        200        210        220        230        240 
ATPPISNLTK TASESISNLS EAGSIKKGER ELKIGDRVLV GGTKAGVVRF LGETDFAKGE 

       250        260        270        280        290        300 
WCGVELDEPL GKNDGAVAGT RYFQCQPKYG LFAPVHKVTK IGFPSTTPAK AKANAVRRVM 

       310        320        330        340        350        360 
ATTSASLKRS PSASSLSSMS SVASSVSSRP SRTGLLTETS SRYARKISGT TALQEALKEK 

       370        380        390        400        410        420 
QQHIEQLLAE RDLERAEVAK ATSHVGEIEQ ELALARDGHD QHVLELEAKM DQLRTMVEAA 

       430        440        450        460        470        480 
DREKVELLNQ LEEEKRKVED LQFRVEEESI TKGDLEQKSQ ISEDPENTQT KLEHARIKEL 

       490        500        510        520        530        540 
EQSLLFEKTK ADKLQRELED TRVATVSEKS RIMELEKDLA LRVQEVAELR RRLESNKPAG 

       550        560        570        580        590        600 
DVDMSLSLLQ EISSLQEKLE VTRTDHQREI TSLKEHFGAR EETHQKEIKA LYTATEKLSK 

       610        620        630        640        650        660 
ENESLKSKLE HANKENSDVI ALWKSKLETA IASHQQAMEE LKVSFSKGLG TETAEFAELK 

       670        680        690        700        710        720 
TQIEKMRLDY QHEIENLQNQ QDSERAAHAK EMEALRAKLM KVIKEKENSL EAIRSKLDKA 

       730        740        750        760        770        780 
EDQHLVEMED TLNKLQEAEI KVKELEVLQA KCNEQTKVID NFTSQLKATE EKLLDLDALR 

       790        800        810        820        830        840 
KASSEGKSEM KKLRQQLEAA EKQIKHLEIE KNAESSKASS ITRELQGREL KLTNLQENLS 

       850        860        870        880        890        900 
EVSQVKETLE KELQILKEKF AEASEEAVSV QRSMQETVNK LHQKEEQFNM LSSDLEKLRE 

       910        920        930        940        950        960 
NLADMEAKFR EKDEREEQLI KAKEKLENDI AEIMKMSGDN SSQLTKMNDE LRLKERDVEE 

       970        980        990       1000       1010       1020 
LQLKLTKANE NASFLQKSIE DMTVKAEQSQ QEAAKKHEEE KKELERKLSD LEKKMETSHN 

      1030       1040       1050       1060       1070       1080 
QCQELKARYE RATSETKTKH EEILQNLQKT LLDTEDKLKG AREENSGLLQ ELEELRKQAD 

      1090       1100       1110       1120       1130       1140 
KAKAAQTAED AMQIMEQMTK EKTETLASLE DTKQTNAKLQ NELDTLKENN LKNVEELNKS 

      1150       1160       1170       1180       1190       1200 
KELLTVENQK MEEFRKEIET LKQAAAQKSQ QLSALQEENV KLAEELGRSR DEVTSHQKLE 

      1210       1220       1230       1240       1250       1260 
EERSVLNNQL LEMKKRESKF IKDADEEKAS LQKSISITSA LLTEKDAELE KLRNEVTVLR 

      1270       1280       1290       1300       1310       1320 
GENASAKSLH SVVQTLESDK VKLELKVKNL ELQLKENKRQ LSSSSGNTDT QADEDERAQE 

      1330       1340       1350       1360       1370       1380 
SQIDFLNSVI VDLQRKNQDL KMKVEMMSEA ALNGNGDDLN NYDSDDQEKQ SKKKPRLFCD 

      1390       1400       1410       1420       1430 
ICDCFDLHDT EDCPTQAQMS EDPPHSTHHG SRGEERPYCE ICEMFGHWAT NCNDDETF 

« Hide

Isoform 2 (Long) [UniParc].

Checksum: 0A4F166DD94254E8
Show »

FASTA1,427160,990
Isoform 3 (Short) [UniParc].

Checksum: 959DF99064762A10
Show »

FASTA1,392156,781

References

« Hide 'large scale' references
[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]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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]"Structure-function relationship of CAP-Gly domains."
Weisbrich A., Honnappa S., Jaussi R., Okhrimenko O., Frey D., Jelesarov I., Akhmanova A., Steinmetz M.O.
Nat. Struct. Mol. Biol. 14:959-967(2007) [PubMed] [Europe PMC] [Abstract]
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]"The consensus coding sequences of human breast and colorectal cancers."
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. expand/collapse author list , 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.
Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] ILE-1213.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRA43336.
S22695.
RefSeqNP_001234926.1. NM_001247997.1.
NP_002947.1. NM_002956.2.
NP_937883.1. NM_198240.1.
UniGeneHs.524809.

3D structure databases

PDBe
RCSB PDB
PDBj
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[»]
ProteinModelPortalP30622.
SMRP30622. Positions 4-130, 181-340.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112163. 17 interactions.
DIPDIP-42826N.
IntActP30622. 12 interactions.
MINTMINT-1781312.
STRING9606.ENSP00000351665.

PTM databases

PhosphoSiteP30622.

Polymorphism databases

DMDM261260059.

Proteomic databases

PaxDbP30622.
PRIDEP30622.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000302528; ENSP00000303585; ENSG00000130779. [P30622-1]
ENST00000358808; ENSP00000351665; ENSG00000130779. [P30622-1]
ENST00000537178; ENSP00000445531; ENSG00000130779. [P30622-2]
ENST00000540338; ENSP00000439093; ENSG00000130779. [P30622-3]
GeneID6249.
KEGGhsa:6249.
UCSCuc001ucg.2. human. [P30622-3]
uc001uch.1. human. [P30622-1]
uc001uci.1. human. [P30622-2]

Organism-specific databases

CTD6249.
GeneCardsGC12M122755.
HGNCHGNC:10461. CLIP1.
HPACAB004399.
HPA026678.
MIM179838. gene.
neXtProtNX_P30622.
PharmGKBPA162382349.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5244.
HOGENOMHOG000092755.
HOVERGENHBG007123.
KOK10421.
OMAQFNALST.
PhylomeDBP30622.
TreeFamTF326096.

Enzyme and pathway databases

ReactomeREACT_115566. Cell Cycle.
REACT_21300. Mitotic M-M/G1 phases.

Gene expression databases

ArrayExpressP30622.
BgeeP30622.
CleanExHS_CLIP1.
GenevestigatorP30622.

Family and domain databases

Gene3D2.30.30.190. 2 hits.
InterProIPR000938. CAP-Gly_domain.
IPR028396. CLIP-170.
IPR001878. Znf_CCHC.
[Graphical view]
PANTHERPTHR18916:SF9. PTHR18916:SF9. 1 hit.
PfamPF01302. CAP_GLY. 2 hits.
[Graphical view]
SMARTSM01052. CAP_GLY. 2 hits.
SM00343. ZnF_C2HC. 1 hit.
[Graphical view]
SUPFAMSSF74924. SSF74924. 2 hits.
PROSITEPS00845. CAP_GLY_1. 2 hits.
PS50245. CAP_GLY_2. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSCLIP1. human.
EvolutionaryTraceP30622.
GeneWikiCLIP1.
GenomeRNAi6249.
NextBio24265.
PROP30622.
SOURCESearch...

Entry information

Entry nameCLIP1_HUMAN
AccessionPrimary (citable) accession number: P30622
Secondary accession number(s): A0AVD3, Q17RS4, Q29RG0
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: October 13, 2009
Last modified: April 16, 2014
This is version 146 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 12

Human chromosome 12: entries, gene names and cross-references to MIM