P30622 (CLIP1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	CLIP1
Synonyms:	CYLN1, RSN

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	1438 AA.
Sequence status	Complete.
Protein existence	Evidence 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.13 Ref.16
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.13 Ref.15 Ref.16
Subcellular location	Cytoplasm. Cytoplasm › cytoskeleton. Cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side. Cell projection › ruffle. 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.13 Ref.17
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.16
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 process	Transport
Cellular component	Cell projection Cytoplasm Cytoplasmic vesicle Cytoskeleton Membrane Microtubule
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Coiled coil Repeat Zinc-finger
Ligand	Metal-binding Zinc
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	microtubule bundle formation Inferred from mutant phenotype Ref.13. Source: UniProtKB mitotic prometaphase Traceable author statement. Source: Reactome positive regulation of microtubule polymerization Inferred from mutant phenotype PubMed 15262990Ref.13. Source: UniProtKB transport Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	centrosome Inferred from direct assay PubMed 21399614. Source: UniProtKB cytoplasmic microtubule Inferred from electronic annotation. Source: Compara 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 plus end Inferred from electronic annotation. Source: Compara ruffle Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	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 zinc ion binding Inferred from direct assay Ref.15. Source: UniProtKB
Complete GO annotation...

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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1438

1438

CAP-Gly domain-containing linker protein 1

PRO_0000083527

Regions

Domain

78 – 120

43

CAP-Gly 1

Domain

232 – 274

43

CAP-Gly 2

Zinc finger

1417 – 1434

18

CCHC-type

Region

97 – 101

5

Important for tubulin binding

Coiled coil

350 – 1353

1004

Potential

Compositional bias

143 – 204

62

Ser-rich

Compositional bias

304 – 331

28

Ser-rich

Amino acid modifications

Modified residue

48

1

Phosphoserine Ref.8 Ref.10

Modified residue

140

1

Phosphothreonine Ref.8 Ref.10

Modified residue

143

1

Phosphoserine Ref.8 Ref.10

Modified residue

147

1

Phosphoserine Ref.8

Modified residue

182

1

Phosphothreonine Ref.8

Modified residue

195

1

Phosphoserine Ref.7 Ref.9

Modified residue

197

1

Phosphoserine Ref.8

Modified residue

200

1

Phosphoserine Ref.6 Ref.8 Ref.9 Ref.10

Modified residue

204

1

Phosphoserine Ref.6 Ref.8 Ref.9 Ref.10

Modified residue

937

1

Phosphoserine By similarity

Modified residue

1364

1

Phosphoserine Ref.10

Natural variations

Alternative sequence

457 – 502

46

Missing in isoform 3.

VSP_000765

Alternative sequence

457 – 467

11

Missing in isoform 2.

VSP_038201

Natural variant

162

1

S → P.
Corresponds to variant rs7963597 [ dbSNP | Ensembl ].

VAR_059206

Natural variant

780

1

R → W.
Corresponds to variant rs3741447 [ dbSNP | Ensembl ].

VAR_048672

Natural variant

941

1

S → P. Ref.3
Corresponds to variant rs17883517 [ dbSNP | Ensembl ].

VAR_048673

Natural variant

1080

1

D → E. Ref.2 Ref.3
Corresponds to variant rs1129167 [ dbSNP | Ensembl ].

VAR_020398

Natural variant

1213

1

M → I in a breast cancer sample; somatic mutation. Ref.18

VAR_036446

Natural variant

1224

1

A → S.
Corresponds to variant rs17881033 [ dbSNP | Ensembl ].

VAR_048674

Experimental info

Mutagenesis

98 – 99

2

KN → EE: Abolishes interaction with tubulin. Abolishes localization at the microtubule plus end. Ref.13

Sequence conflict

193

1

S → G in AAI14214. Ref.3

Sequence conflict

324

1

S → P in AAI14214. Ref.3

Sequence conflict

651

1

T → A in AAI14214. Ref.3

Sequence conflict

682

1

D → N in AAI14214. Ref.3

Sequence conflict

766

1

L → P in AAI14214. Ref.3

Sequence conflict

1432

1

C → R in AAI14214. Ref.3

Secondary structure

1

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1438

Helix Strand Turn

Details...

Beta strand

37 – 39

3

Beta strand

63 – 66

4

Turn

67 – 69

3

Beta strand

70 – 78

9

Beta strand

81 – 85

5

Beta strand

87 – 95

9

Beta strand

97 – 103

7

Beta strand

106 – 108

3

Turn

113 – 115

3

Beta strand

116 – 119

4

Helix

121 – 123

3

Beta strand

124 – 127

4

Beta strand

193 – 196

4

Beta strand

217 – 220

4

Turn

221 – 223

3

Beta strand

224 – 233

10

Beta strand

235 – 249

15

Beta strand

252 – 257

6

Beta strand

260 – 262

3

Turn

267 – 269

3

Beta strand

270 – 274

5

Helix

275 – 277

3

Beta strand

278 – 280

3

Beta strand

295 – 298

4

Turn

1420 – 1423

4

Beta strand

1424 – 1427

4

Helix

1429 – 1431

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified October 13, 2009. Version 2. Checksum: A7F125F7A96DBDDB	FASTA	1,438	162,246
	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
	Isoform 2 (Long) [UniParc]. Checksum: 0A4F166DD94254E8	FASTA	1,427	160,990
	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 TKGDLETQTK LEHARIKELE QSLLFEKTKA 490 500 510 520 530 540 DKLQRELEDT RVATVSEKSR IMELEKDLAL RVQEVAELRR RLESNKPAGD VDMSLSLLQE 550 560 570 580 590 600 ISSLQEKLEV TRTDHQREIT SLKEHFGARE ETHQKEIKAL YTATEKLSKE NESLKSKLEH 610 620 630 640 650 660 ANKENSDVIA LWKSKLETAI ASHQQAMEEL KVSFSKGLGT ETAEFAELKT QIEKMRLDYQ 670 680 690 700 710 720 HEIENLQNQQ DSERAAHAKE MEALRAKLMK VIKEKENSLE AIRSKLDKAE DQHLVEMEDT 730 740 750 760 770 780 LNKLQEAEIK VKELEVLQAK CNEQTKVIDN FTSQLKATEE KLLDLDALRK ASSEGKSEMK 790 800 810 820 830 840 KLRQQLEAAE KQIKHLEIEK NAESSKASSI TRELQGRELK LTNLQENLSE VSQVKETLEK 850 860 870 880 890 900 ELQILKEKFA EASEEAVSVQ RSMQETVNKL HQKEEQFNML SSDLEKLREN LADMEAKFRE 910 920 930 940 950 960 KDEREEQLIK AKEKLENDIA EIMKMSGDNS SQLTKMNDEL RLKERDVEEL QLKLTKANEN 970 980 990 1000 1010 1020 ASFLQKSIED MTVKAEQSQQ EAAKKHEEEK KELERKLSDL EKKMETSHNQ CQELKARYER 1030 1040 1050 1060 1070 1080 ATSETKTKHE EILQNLQKTL LDTEDKLKGA REENSGLLQE LEELRKQADK AKAAQTAEDA 1090 1100 1110 1120 1130 1140 MQIMEQMTKE KTETLASLED TKQTNAKLQN ELDTLKENNL KNVEELNKSK ELLTVENQKM 1150 1160 1170 1180 1190 1200 EEFRKEIETL KQAAAQKSQQ LSALQEENVK LAEELGRSRD EVTSHQKLEE ERSVLNNQLL 1210 1220 1230 1240 1250 1260 EMKKRESKFI KDADEEKASL QKSISITSAL LTEKDAELEK LRNEVTVLRG ENASAKSLHS 1270 1280 1290 1300 1310 1320 VVQTLESDKV KLELKVKNLE LQLKENKRQL SSSSGNTDTQ ADEDERAQES QIDFLNSVIV 1330 1340 1350 1360 1370 1380 DLQRKNQDLK MKVEMMSEAA LNGNGDDLNN YDSDDQEKQS KKKPRLFCDI CDCFDLHDTE 1390 1400 1410 1420 DCPTQAQMSE DPPHSTHHGS RGEERPYCEI CEMFGHWATN CNDDETF
	Isoform 3 (Short) [UniParc]. Checksum: 959DF99064762A10	FASTA	1,392	156,781
	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 TKGDLEVATV SEKSRIMELE KDLALRVQEV 490 500 510 520 530 540 AELRRRLESN KPAGDVDMSL SLLQEISSLQ EKLEVTRTDH QREITSLKEH FGAREETHQK 550 560 570 580 590 600 EIKALYTATE KLSKENESLK SKLEHANKEN SDVIALWKSK LETAIASHQQ AMEELKVSFS 610 620 630 640 650 660 KGLGTETAEF AELKTQIEKM RLDYQHEIEN LQNQQDSERA AHAKEMEALR AKLMKVIKEK 670 680 690 700 710 720 ENSLEAIRSK LDKAEDQHLV EMEDTLNKLQ EAEIKVKELE VLQAKCNEQT KVIDNFTSQL 730 740 750 760 770 780 KATEEKLLDL DALRKASSEG KSEMKKLRQQ LEAAEKQIKH LEIEKNAESS KASSITRELQ 790 800 810 820 830 840 GRELKLTNLQ ENLSEVSQVK ETLEKELQIL KEKFAEASEE AVSVQRSMQE TVNKLHQKEE 850 860 870 880 890 900 QFNMLSSDLE KLRENLADME AKFREKDERE EQLIKAKEKL ENDIAEIMKM SGDNSSQLTK 910 920 930 940 950 960 MNDELRLKER DVEELQLKLT KANENASFLQ KSIEDMTVKA EQSQQEAAKK HEEEKKELER 970 980 990 1000 1010 1020 KLSDLEKKME TSHNQCQELK ARYERATSET KTKHEEILQN LQKTLLDTED KLKGAREENS 1030 1040 1050 1060 1070 1080 GLLQELEELR KQADKAKAAQ TAEDAMQIME QMTKEKTETL ASLEDTKQTN AKLQNELDTL 1090 1100 1110 1120 1130 1140 KENNLKNVEE LNKSKELLTV ENQKMEEFRK EIETLKQAAA QKSQQLSALQ EENVKLAEEL 1150 1160 1170 1180 1190 1200 GRSRDEVTSH QKLEEERSVL NNQLLEMKKR ESKFIKDADE EKASLQKSIS ITSALLTEKD 1210 1220 1230 1240 1250 1260 AELEKLRNEV TVLRGENASA KSLHSVVQTL ESDKVKLELK VKNLELQLKE NKRQLSSSSG 1270 1280 1290 1300 1310 1320 NTDTQADEDE RAQESQIDFL NSVIVDLQRK NQDLKMKVEM MSEAALNGNG DDLNNYDSDD 1330 1340 1350 1360 1370 1380 QEKQSKKKPR LFCDICDCFD LHDTEDCPTQ AQMSEDPPHS THHGSRGEER PYCEICEMFG 1390 HWATNCNDDE TF

References

	« Hide 'large scale' referencesShow '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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[9]	"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, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[10]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[11]	"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].
[12]	"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.
[13]	"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.
[14]	"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.
[15]	"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.
[16]	"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.
[17]	"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.
[18]	"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. , 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.

IPI

IPI00013455.
IPI00027172.
IPI00217113.

PIR

A43336.
S22695.

RefSeq

NP_001234926.1. NM_001247997.1.
NP_002947.1. NM_002956.2.
NP_937883.1. NM_198240.1.

UniGene

Hs.524809.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

P30622.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-42826N.

IntAct

P30622. 5 interactions.

MINT

MINT-1781312.

STRING

9606.ENSP00000351665.

PTM databases

PhosphoSite

P30622.

Polymorphism databases

DMDM

261260059.

Proteomic databases

PaxDb

P30622.

PRIDE

P30622.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000302528; ENSP00000303585; ENSG00000130779.
ENST00000358808; ENSP00000351665; ENSG00000130779.
ENST00000537178; ENSP00000445531; ENSG00000130779.
ENST00000540338; ENSP00000439093; ENSG00000130779.

GeneID

6249.

KEGG

hsa:6249.

UCSC

uc001ucg.2. human.
uc001uch.1. human.
uc001uci.1. human.

Organism-specific databases

CTD

6249.

GeneCards

GC12M122755.

HGNC

HGNC:10461. CLIP1.

HPA

CAB004399.
HPA026678.

MIM

179838. gene.

neXtProt

NX_P30622.

PharmGKB

PA162382349.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG5244.

HOGENOM

HOG000092755.

HOVERGEN

HBG007123.

KO

K10421.

OMA

MEMSHNQ.

OrthoDB

EOG42Z4PQ.

Enzyme and pathway databases

Pathway_Interaction_DB

lis1pathway. Lissencephaly gene (LIS1) in neuronal migration and development.

Reactome

REACT_115566. Cell Cycle.
REACT_21300. Mitotic M-M/G1 phases.

Gene expression databases

ArrayExpress

P30622.

Bgee

P30622.

CleanEx

HS_CLIP1.

Genevestigator

P30622.

GermOnline

ENSG00000130779. Homo sapiens.

Family and domain databases

Gene3D

2.30.30.190. 2 hits.

InterPro

IPR000938. CAP-Gly_domain.
IPR001878. Znf_CCHC.
[Graphical view]

Pfam

PF01302. CAP_GLY. 2 hits.
[Graphical view]

SMART

SM01052. CAP_GLY. 2 hits.
SM00343. ZnF_C2HC. 1 hit.
[Graphical view]

SUPFAM

SSF74924. CAP-Gly_domain. 2 hits.

PROSITE

PS00845. CAP_GLY_1. 2 hits.
PS50245. CAP_GLY_2. 2 hits.
PS50158. ZF_CCHC. False negative.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

CLIP1. human.

EvolutionaryTrace

P30622.

GenomeRNAi

6249.

NextBio

24265.

SOURCE

Search...

Entry information

Entry name

CLIP1_HUMAN

Accession

Primary (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:	May 1, 2013
This is version 136 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.