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)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	1438 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Seems to be a intermediate filament associated protein that links endocytic vesicles to microtubules.
Subunit structure	Interacts with MTOR; phosphorylates and regulates CLIP1. Ref.4
Subcellular location	Cytoplasm. Cytoplasm › cytoskeleton. Note: Associated with the cytoskeleton. Localizes to the tips of microtubules By similarity.
Tissue specificity	Highly expressed in the Reed-Sternberg cells of Hodgkin disease. Ref.1
Post-translational modification	Phosphorylated. Phosphorylation by MTOR may positively regulate CLIP1 association with microtubules. Ref.4 Ref.5 Ref.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14
Sequence similarities	Contains 2 CAP-Gly domains.

Ontologies

Keywords
Cellular component	Cytoplasm Cytoskeleton Microtubule
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Coiled coil Repeat
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	mitotic prometaphase Traceable author statement. Source: Reactome positive regulation of microtubule polymerization Inferred from mutant phenotype. Source: UniProtKB
Cellular component	centrosome Inferred from direct assay. Source: UniProtKB cytosol Traceable author statement. Source: Reactome endosome Traceable author statement. Source: ProtInc intermediate filament Traceable author statement. Source: ProtInc kinetochore Traceable author statement. Source: UniProtKB
Molecular function	nucleic acid binding Inferred from electronic annotation. Source: InterPro protein homodimerization activity Traceable author statement. Source: UniProtKB zinc ion binding Inferred from electronic annotation. Source: InterPro
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

Coiled coil

350 – 1353

1004

Potential

Motif

1419 – 1432

14

CCHC-box

Compositional bias

143 – 204

62

Ser-rich

Compositional bias

304 – 331

28

Ser-rich

Amino acid modifications

Modified residue

45

1

Phosphothreonine Ref.12

Modified residue

48

1

Phosphoserine Ref.12

Modified residue

140

1

Phosphothreonine Ref.12

Modified residue

143

1

Phosphoserine Ref.12

Modified residue

147

1

Phosphoserine Ref.12

Modified residue

182

1

Phosphothreonine Ref.8 Ref.9 Ref.10 Ref.12 Ref.13

Modified residue

193

1

Phosphoserine Ref.13

Modified residue

195

1

Phosphoserine Ref.8 Ref.11 Ref.13 Ref.14

Modified residue

197

1

Phosphoserine Ref.12

Modified residue

200

1

Phosphoserine Ref.6 Ref.7 Ref.11 Ref.12 Ref.13 Ref.14

Modified residue

204

1

Phosphoserine Ref.5 Ref.7 Ref.12 Ref.13 Ref.14

Modified residue

833

1

Phosphothreonine Ref.11

Modified residue

937

1

Phosphoserine By similarity

Modified residue

1364

1

Phosphoserine Ref.13

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.17

VAR_036446

Natural variant

1224

1

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

VAR_048674

Experimental info

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

63 – 66

4

Turn

67 – 69

3

Beta strand

70 – 79

10

Beta strand

81 – 95

15

Beta strand

97 – 103

7

Beta strand

106 – 109

4

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

Beta strand

270 – 274

5

Helix

275 – 277

3

Beta strand

278 – 280

3

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: 1600942] [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: 1356075] [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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3), VARIANTS PRO-941 AND GLU-1080. Tissue: Colon.
[4]	"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: 12231510] [Abstract] Cited for: INTERACTION WITH MTOR, PHOSPHORYLATION BY MTOR.
[5]	"Large-scale characterization of HeLa cell nuclear phosphoproteins." Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004) [PubMed: 15302935] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-204, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[6]	"Global phosphoproteome of HT-29 human colon adenocarcinoma cells." Kim J.-E., Tannenbaum S.R., White F.M. J. Proteome Res. 4:1339-1346(2005) [PubMed: 16083285] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-200, MASS SPECTROMETRY. Tissue: Colon adenocarcinoma.
[7]	"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: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-200 AND SER-204, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[8]	"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: 16964243] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-182 AND SER-195, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[9]	"Phosphoproteome analysis of the human mitotic spindle." Nousiainen M., Sillje H.H.W., Sauer G., Nigg E.A., Koerner R. Proc. Natl. Acad. Sci. U.S.A. 103:5391-5396(2006) [PubMed: 16565220] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-182, MASS SPECTROMETRY. Tissue: Cervix adenocarcinoma.
[10]	"Evaluation of the low-specificity protease elastase for large-scale phosphoproteome analysis." Wang B., Malik R., Nigg E.A., Korner R. Anal. Chem. 80:9526-9533(2008) [PubMed: 19007248] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-182, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[11]	"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column." Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y. Anal. Sci. 24:161-166(2008) [PubMed: 18187866] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-195; SER-200 AND THR-833, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[12]	"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: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-45; SER-48; THR-140; SER-143; SER-147; THR-182; SER-197; SER-200 AND SER-204, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[13]	"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: 19413330] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-182; SER-193; SER-195; SER-200; SER-204 AND SER-1364, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[14]	"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: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-195; SER-200 AND SER-204, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[15]	"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.
[16]	"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: 17828277] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 1388-1427.
[17]	"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: 16959974] [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.

SMR

P30622. Positions 4-130, 181-340.

ModBase

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Protein-protein interaction databases

DIP

DIP-42826N.

IntAct

P30622. 2 interactions.

MINT

MINT-1781312.

STRING

P30622.

PTM databases

PhosphoSite

P30622.

Polymorphism databases

DMDM

261260059.

Proteomic databases

PRIDE

P30622.

Protocols and materials databases

StructuralBiologyKnowledgebase

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Genome annotation databases

Ensembl

ENST00000302528; ENSP00000303585; ENSG00000130779.
ENST00000358808; ENSP00000351665; ENSG00000130779.
ENST00000361654; ENSP00000355314; ENSG00000130779.

GeneID

6249.

KEGG

hsa:6249.

NMPDR

fig|9606.3.peg.8431.

UCSC

uc001uch.1. human.
uc001uci.1. human.

Organism-specific databases

CTD

6249.

GeneCards

GC12M122755.

H-InvDB

HIX0026332.

HGNC

HGNC:10461. CLIP1.

HPA

CAB004399.
HPA026678.

MIM

179838. gene.

neXtProt

NX_P30622.

GenAtlas

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Phylogenomic databases

GeneTree

ENSGT00550000074375.

HOVERGEN

HBG007123.

OMA

GNTDTQA.

OrthoDB

EOG42Z4PQ.

PhylomeDB

P30622.

Enzyme and pathway databases

Pathway_Interaction_DB

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

Reactome

REACT_152. Cell Cycle, Mitotic.
REACT_383. DNA Replication.

Gene expression databases

ArrayExpress

P30622.

Bgee

P30622.

CleanEx

HS_CLIP1.

Genevestigator

P30622.

GermOnline

ENSG00000130779. Homo sapiens.

Family and domain databases

InterPro

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

Gene3D

G3DSA:2.30.30.190. CAP-Gly_domain. 2 hits.

KO

K10421.

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.
[Graphical view]

ProtoNet

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Other

NextBio

24265.

SOURCE

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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:	January 25, 2012
This is version 122 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.