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Protein

CAP-Gly domain-containing linker protein 1

Gene

CLIP1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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)DescriptionActionsGraphical viewLength
Zinc fingeri1417 – 1434CCHC-type2 PublicationsAdd BLAST18

GO - Molecular functioni

  • metal ion binding Source: UniProtKB
  • microtubule binding Source: UniProtKB
  • microtubule plus-end binding Source: UniProtKB
  • protein homodimerization activity Source: UniProtKB
  • tubulin binding Source: UniProtKB
  • zinc ion binding Source: UniProtKB

GO - Biological processi

  • microtubule bundle formation Source: UniProtKB
  • mitotic nuclear division Source: UniProtKB
  • positive regulation of dendrite development Source: Ensembl
  • positive regulation of microtubule polymerization Source: UniProtKB
  • protein transport into plasma membrane raft Source: Ensembl
  • sister chromatid cohesion Source: Reactome
Complete GO annotation...

Keywords - Biological processi

Transport

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BioCyciZFISH:ENSG00000104918-MONOMER.
ReactomeiR-HSA-2467813. Separation of Sister Chromatids.
R-HSA-2500257. Resolution of Sister Chromatid Cohesion.
R-HSA-5626467. RHO GTPases activate IQGAPs.
R-HSA-5663220. RHO GTPases Activate Formins.
R-HSA-68877. Mitotic Prometaphase.
SIGNORiP30622.

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
Proteomesi
  • UP000005640 Componenti: Chromosome 12

Organism-specific databases

HGNCiHGNC:10461. CLIP1.

Subcellular locationi

GO - Cellular componenti

  • centrosome Source: UniProtKB
  • cytoplasm Source: HPA
  • cytoplasmic microtubule Source: Ensembl
  • cytoplasmic vesicle membrane Source: UniProtKB-SubCell
  • cytosol Source: Reactome
  • endosome Source: ProtInc
  • intermediate filament Source: ProtInc
  • kinetochore Source: UniProtKB
  • microtubule Source: UniProtKB
  • microtubule cytoskeleton Source: UniProtKB
  • microtubule end Source: HPA
  • microtubule plus-end Source: Ensembl
  • nuclear envelope Source: Ensembl
  • ruffle Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

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

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi98 – 99KN → EE: Abolishes interaction with tubulin. Abolishes localization at the microtubule plus end. 1 Publication2

Organism-specific databases

DisGeNETi6249.
MalaCardsiCLIP1.
OpenTargetsiENSG00000130779.
Orphaneti88616. Autosomal recessive non-syndromic intellectual disability.
PharmGKBiPA162382349.

Polymorphism and mutation databases

BioMutaiCLIP1.
DMDMi261260059.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000835271 – 1438CAP-Gly domain-containing linker protein 1Add BLAST1438

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei48PhosphoserineCombined sources1
Modified residuei50PhosphothreonineCombined sources1
Modified residuei140PhosphothreonineCombined sources1
Modified residuei143PhosphoserineCombined sources1
Modified residuei147PhosphoserineCombined sources1
Modified residuei182PhosphothreonineCombined sources1
Modified residuei195PhosphoserineCombined sources1
Modified residuei197PhosphoserineCombined sources1
Modified residuei200PhosphoserineCombined sources1
Modified residuei204PhosphoserineCombined sources1
Modified residuei310PhosphoserineBy similarity1
Modified residuei312Phosphoserine; by PKABy similarity1
Modified residuei315PhosphoserineBy similarity1
Modified residuei348PhosphoserineBy similarity1
Modified residuei1310PhosphothreonineCombined sources1
Modified residuei1364PhosphoserineCombined sources1

Post-translational modificationi

Phosphorylated. Phosphorylation induces conformational changes by increasing the affinity of the N-terminus for C-terminus, resulting in inhibition of its function thus decreasing its binding to microtubules and DCTN1. Exhibits a folded, autoinhibited conformation when phosphorylated and an open conformation when dephosphorylated with increased binding affinity to microtubules and DCTN1. Phosphorylation regulates its recruitment to tyrosinated microtubules and the recruitment of vesicular cargo to microtubules in neurons (By similarity). Phosphorylation by MTOR may positively regulate CLIP1 association with microtubules (PubMed:12231510).By similarity1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiP30622.
PaxDbiP30622.
PeptideAtlasiP30622.
PRIDEiP30622.

PTM databases

iPTMnetiP30622.
PhosphoSitePlusiP30622.
UniCarbKBiP30622.

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

BgeeiENSG00000130779.
CleanExiHS_CLIP1.
ExpressionAtlasiP30622. baseline and differential.
GenevisibleiP30622. HS.

Organism-specific databases

HPAiCAB004399.
HPA026678.

Interactioni

Subunit structurei

Interacts with MTOR; phosphorylates and regulates CLIP1 (PubMed:12231510). Interacts (via CAP-Gly domains) with tubulin (PubMed:17563362, PubMed:17889670). Interacts with SLAIN2 (PubMed:21646404). Interacts (via zinc finger) with DCTN1 (PubMed:17828275, PubMed:20679239). Interacts with TUBA1B, MAPRE1 and MAPRE3 (PubMed:17563362). Binds preferentially to tyrosinated microtubules, and only marginally to detyrosinated microtubules (By similarity).By similarity7 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
MAPRE1Q156912EBI-2683569,EBI-1004115
TUBA4AP683663EBI-2683569,EBI-351772

GO - Molecular functioni

  • microtubule binding Source: UniProtKB
  • microtubule plus-end binding Source: UniProtKB
  • protein homodimerization activity Source: UniProtKB
  • tubulin binding Source: UniProtKB

Protein-protein interaction databases

BioGridi112163. 31 interactors.
DIPiDIP-42826N.
IntActiP30622. 18 interactors.
MINTiMINT-1781312.
STRINGi9606.ENSP00000303585.

Structurei

Secondary structure

11438
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi37 – 39Combined sources3
Beta strandi63 – 66Combined sources4
Turni67 – 69Combined sources3
Beta strandi70 – 78Combined sources9
Beta strandi81 – 85Combined sources5
Beta strandi87 – 95Combined sources9
Beta strandi97 – 103Combined sources7
Beta strandi106 – 108Combined sources3
Turni113 – 115Combined sources3
Beta strandi116 – 119Combined sources4
Helixi121 – 123Combined sources3
Beta strandi124 – 127Combined sources4
Beta strandi193 – 196Combined sources4
Beta strandi217 – 220Combined sources4
Turni221 – 223Combined sources3
Beta strandi224 – 233Combined sources10
Beta strandi235 – 249Combined sources15
Beta strandi252 – 257Combined sources6
Beta strandi260 – 262Combined sources3
Turni267 – 269Combined sources3
Beta strandi270 – 274Combined sources5
Helixi275 – 277Combined sources3
Beta strandi278 – 280Combined sources3
Beta strandi295 – 298Combined sources4
Turni1420 – 1423Combined sources4
Beta strandi1424 – 1427Combined sources4
Helixi1429 – 1431Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP30622.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini78 – 120CAP-Gly 1PROSITE-ProRule annotationAdd BLAST43
Domaini232 – 274CAP-Gly 2PROSITE-ProRule annotationAdd BLAST43

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni97 – 101Important for tubulin binding1 Publication5

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili350 – 1353Sequence analysisAdd BLAST1004

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi143 – 204Ser-richAdd BLAST62
Compositional biasi304 – 331Ser-richAdd BLAST28

Domaini

Intramolecular interaction between the zinc finger domain and the CAP-Gly domains may inhibit interaction with tubulin.1 Publication

Sequence similaritiesi

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

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri1417 – 1434CCHC-type2 PublicationsAdd BLAST18

Keywords - Domaini

Coiled coil, Repeat, Zinc-finger

Phylogenomic databases

eggNOGiKOG4568. Eukaryota.
COG5244. LUCA.
GeneTreeiENSGT00760000119173.
HOGENOMiHOG000092755.
HOVERGENiHBG007123.
InParanoidiP30622.
KOiK10421.
OMAiSEGKSEM.
OrthoDBiEOG091G0J1Y.
PhylomeDBiP30622.
TreeFamiTF326096.

Family and domain databases

Gene3Di2.30.30.190. 2 hits.
InterProiIPR000938. CAP-Gly_domain.
IPR032108. CLIP1_ZNF.
[Graphical view]
PfamiPF01302. CAP_GLY. 2 hits.
PF16641. CLIP1_ZNF. 2 hits.
[Graphical view]
SMARTiSM01052. CAP_GLY. 2 hits.
[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. AlignAdd to basket

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)DescriptionActionsGraphical viewLength
Sequence conflicti193S → G in AAI14214 (PubMed:15489334).Curated1
Sequence conflicti324S → P in AAI14214 (PubMed:15489334).Curated1
Sequence conflicti651T → A in AAI14214 (PubMed:15489334).Curated1
Sequence conflicti682D → N in AAI14214 (PubMed:15489334).Curated1
Sequence conflicti766L → P in AAI14214 (PubMed:15489334).Curated1
Sequence conflicti1432C → R in AAI14214 (PubMed:15489334).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_059206162S → P.Corresponds to variant rs7963597dbSNPEnsembl.1
Natural variantiVAR_048672780R → W.Corresponds to variant rs3741447dbSNPEnsembl.1
Natural variantiVAR_048673941S → P.1 PublicationCorresponds to variant rs17883517dbSNPEnsembl.1
Natural variantiVAR_0203981080D → E.2 PublicationsCorresponds to variant rs1129167dbSNPEnsembl.1
Natural variantiVAR_0364461213M → I in a breast cancer sample; somatic mutation. 1 Publication1
Natural variantiVAR_0486741224A → S.Corresponds to variant rs17881033dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_000765457 – 502Missing in isoform 3. 2 PublicationsAdd BLAST46
Alternative sequenceiVSP_038201457 – 467Missing in isoform 2. 1 PublicationAdd BLAST11

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]
XP_016875275.1. XM_017019786.1. [P30622-1]
XP_016875279.1. XM_017019790.1. [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]

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.
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]
XP_016875275.1. XM_017019786.1. [P30622-1]
XP_016875279.1. XM_017019790.1. [P30622-2]
UniGeneiHs.524809.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112163. 31 interactors.
DIPiDIP-42826N.
IntActiP30622. 18 interactors.
MINTiMINT-1781312.
STRINGi9606.ENSP00000303585.

PTM databases

iPTMnetiP30622.
PhosphoSitePlusiP30622.
UniCarbKBiP30622.

Polymorphism and mutation databases

BioMutaiCLIP1.
DMDMi261260059.

Proteomic databases

EPDiP30622.
PaxDbiP30622.
PeptideAtlasiP30622.
PRIDEiP30622.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

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]

Organism-specific databases

CTDi6249.
DisGeNETi6249.
GeneCardsiCLIP1.
HGNCiHGNC:10461. CLIP1.
HPAiCAB004399.
HPA026678.
MalaCardsiCLIP1.
MIMi179838. gene.
neXtProtiNX_P30622.
OpenTargetsiENSG00000130779.
Orphaneti88616. Autosomal recessive non-syndromic intellectual disability.
PharmGKBiPA162382349.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG4568. Eukaryota.
COG5244. LUCA.
GeneTreeiENSGT00760000119173.
HOGENOMiHOG000092755.
HOVERGENiHBG007123.
InParanoidiP30622.
KOiK10421.
OMAiSEGKSEM.
OrthoDBiEOG091G0J1Y.
PhylomeDBiP30622.
TreeFamiTF326096.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000104918-MONOMER.
ReactomeiR-HSA-2467813. Separation of Sister Chromatids.
R-HSA-2500257. Resolution of Sister Chromatid Cohesion.
R-HSA-5626467. RHO GTPases activate IQGAPs.
R-HSA-5663220. RHO GTPases Activate Formins.
R-HSA-68877. Mitotic Prometaphase.
SIGNORiP30622.

Miscellaneous databases

ChiTaRSiCLIP1. human.
EvolutionaryTraceiP30622.
GeneWikiiCLIP1.
GenomeRNAii6249.
PROiP30622.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000130779.
CleanExiHS_CLIP1.
ExpressionAtlasiP30622. baseline and differential.
GenevisibleiP30622. HS.

Family and domain databases

Gene3Di2.30.30.190. 2 hits.
InterProiIPR000938. CAP-Gly_domain.
IPR032108. CLIP1_ZNF.
[Graphical view]
PfamiPF01302. CAP_GLY. 2 hits.
PF16641. CLIP1_ZNF. 2 hits.
[Graphical view]
SMARTiSM01052. CAP_GLY. 2 hits.
[Graphical view]
SUPFAMiSSF74924. SSF74924. 2 hits.
PROSITEiPS00845. CAP_GLY_1. 2 hits.
PS50245. CAP_GLY_2. 2 hits.
[Graphical view]
ProtoNetiSearch...

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 30, 2016
This is version 174 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.