P48059 (LIMS1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
LIM and senescent cell antigen-like-containing domain protein 1

Alternative name(s):
Particularly interesting new Cys-His protein 1
Short name=PINCH-1
Renal carcinoma antigen NY-REN-48

Gene names

Name:	LIMS1
Synonyms:	PINCH, PINCH1

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	325 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Adapter protein in a cytoplasmic complex linking beta-integrins to the actin cytoskeleton, bridges the complex to cell surface receptor tyrosine kinases and growth factor receptors. Involved in the regulation of cell survival, cell proliferation and cell differentiation.
Subunit structure	Interacts (via LIM zinc-binding 5) with TGFB1I1 By similarity. Interacts with integrin-linked protein kinase 1 (ILK) via the first LIM domain, and in competition with LIMS2. Part of the heterotrimeric IPP complex composed of integrin-linked kinase (ILK), LIMS1 or LIMS2, and PARVA. Interacts with SH3/SH2 adapter NCK2, thereby linking the complex to cell surface receptors. Ref.7 Ref.9
Subcellular location	Cell junction › focal adhesion. Cell membrane; Peripheral membrane protein; Cytoplasmic side Ref.9 Ref.15.
Tissue specificity	Expressed in most tissues except in the brain.
Sequence similarities	Contains 5 LIM zinc-binding domains.

Ontologies

Keywords
Cellular component	Cell junction Cell membrane Membrane
Coding sequence diversity	Alternative splicing
Domain	LIM domain Repeat
Ligand	Metal-binding Zinc
PTM	Acetylation
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	cell aging Traceable author statement Ref.1. Source: ProtInc cell junction assembly Traceable author statement. Source: Reactome cellular response to transforming growth factor beta stimulus Inferred from expression pattern PubMed 21390327. Source: UniProtKB negative regulation of transcription, DNA-dependent Inferred from direct assay PubMed 21390327. Source: UniProtKB
Cellular_component	cytosol Traceable author statement. Source: Reactome focal adhesion Inferred from direct assay PubMed 21390327. Source: UniProtKB perinuclear region of cytoplasm Inferred from direct assay PubMed 21390327. Source: UniProtKB plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	zinc ion binding Inferred from direct assay Ref.14. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
Hoxa1	P09022	3	EBI-306928,EBI-3957603	From a different organism.
ILK	Q13418	3	EBI-306928,EBI-747644

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P48059-1)

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: P48059-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MLGVAAGMTHSNM

Note: No experimental confirmation available.

Isoform 3 (identifier: P48059-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MAFSGRARPCIIPENEEIPRAALNTVHEANGTEDERAVSKLQRRHSDVKVYKEFCDFYAKFNM

Isoform 4 (identifier: P48059-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MTCNM

Isoform 5 (identifier: P48059-5)

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MTALQLKELSHSGLYRRRRDRPDSLRVNGLPEEELSNM

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.6

Chain

2 – 325

324

LIM and senescent cell antigen-like-containing domain protein 1

PRO_0000075888

Regions

Domain

10 – 62

53

LIM zinc-binding 1

Domain

71 – 121

51

LIM zinc-binding 2

Domain

135 – 184

50

LIM zinc-binding 3

Domain

193 – 243

51

LIM zinc-binding 4

Domain

252 – 303

52

LIM zinc-binding 5

Amino acid modifications

Modified residue

2

1

N-acetylalanine Ref.6

Natural variations

Alternative sequence

1

1

M → MLGVAAGMTHSNM in isoform 2.

VSP_042672

Alternative sequence

1

1

M → MAFSGRARPCIIPENEEIPR AALNTVHEANGTEDERAVSK LQRRHSDVKVYKEFCDFYAK FNM in isoform 3.

VSP_043210

Alternative sequence

1

1

M → MTCNM in isoform 4.

VSP_043211

Alternative sequence

1

1

M → MTALQLKELSHSGLYRRRRD RPDSLRVNGLPEEELSNM in isoform 5.

VSP_043212

Experimental info

Mutagenesis

42

1

F → A: Loss of interaction with ILK and loss of localization to focal adhesion. Ref.14 Ref.15

Mutagenesis

56

1

R → A: Alters interaction with ILK. Ref.15

Mutagenesis

61

1

H → D: Alters interaction with ILK. Ref.14

Mutagenesis

62

1

D → A: Alters interaction with ILK. Ref.14

Mutagenesis

66

1

L → D: Alters interaction with ILK. Ref.14

Sequence conflict

78

1

I → T in AAH05341. Ref.5

Sequence conflict

262

1

D → G in AAH05341. Ref.5

Secondary structure

1

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325

Helix Strand Turn

Details...

Turn

11 – 13

3

Beta strand

22 – 26

5

Beta strand

29 – 32

4

Turn

33 – 35

3

Turn

39 – 41

3

Helix

46 – 48

3

Beta strand

51 – 53

3

Beta strand

56 – 58

3

Helix

60 – 66

7

Beta strand

72 – 74

3

Beta strand

83 – 85

3

Beta strand

88 – 90

3

Turn

92 – 94

3

Beta strand

98 – 100

3

Beta strand

105 – 107

3

Beta strand

110 – 112

3

Beta strand

115 – 117

3

Helix

119 – 126

8

Turn

136 – 138

3

Beta strand

150 – 152

3

Turn

156 – 158

3

Beta strand

162 – 164

3

Beta strand

173 – 175

3

Beta strand

178 – 180

3

Helix

182 – 186

5

Turn

194 – 197

4

Beta strand

210 – 213

4

Turn

214 – 216

3

Turn

220 – 222

3

Beta strand

227 – 229

3

Beta strand

232 – 234

3

Beta strand

237 – 239

3

Helix

241 – 247

7

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified January 23, 2007. Version 4. Checksum: E665FEB11D849CAE	FASTA	325	37,251
	10 20 30 40 50 60 MANALASATC ERCKGGFAPA EKIVNSNGEL YHEQCFVCAQ CFQQFPEGLF YEFEGRKYCE 70 80 90 100 110 120 HDFQMLFAPC CHQCGEFIIG RVIKAMNNSW HPECFRCDLC QEVLADIGFV KNAGRHLCRP 130 140 150 160 170 180 CHNREKARGL GKYICQKCHA IIDEQPLIFK NDPYHPDHFN CANCGKELTA DARELKGELY 190 200 210 220 230 240 CLPCHDKMGV PICGACRRPI EGRVVNAMGK QWHVEHFVCA KCEKPFLGHR HYERKGLAYC 250 260 270 280 290 300 ETHYNQLFGD VCFHCNRVIE GDVVSALNKA WCVNCFACST CNTKLTLKNK FVEFDMKPVC 310 320 KKCYEKFPLE LKKRLKKLAE TLGRK
	Isoform 2 [UniParc]. Checksum: 8577792E1A56418B	FASTA	337	38,422
	10 20 30 40 50 60 MLGVAAGMTH SNMANALASA TCERCKGGFA PAEKIVNSNG ELYHEQCFVC AQCFQQFPEG 70 80 90 100 110 120 LFYEFEGRKY CEHDFQMLFA PCCHQCGEFI IGRVIKAMNN SWHPECFRCD LCQEVLADIG 130 140 150 160 170 180 FVKNAGRHLC RPCHNREKAR GLGKYICQKC HAIIDEQPLI FKNDPYHPDH FNCANCGKEL 190 200 210 220 230 240 TADARELKGE LYCLPCHDKM GVPICGACRR PIEGRVVNAM GKQWHVEHFV CAKCEKPFLG 250 260 270 280 290 300 HRHYERKGLA YCETHYNQLF GDVCFHCNRV IEGDVVSALN KAWCVNCFAC STCNTKLTLK 310 320 330 NKFVEFDMKP VCKKCYEKFP LELKKRLKKL AETLGRK
	Isoform 3 [UniParc]. Checksum: 3AB2EDB2203CEBFF	FASTA	387	44,390
	10 20 30 40 50 60 MAFSGRARPC IIPENEEIPR AALNTVHEAN GTEDERAVSK LQRRHSDVKV YKEFCDFYAK 70 80 90 100 110 120 FNMANALASA TCERCKGGFA PAEKIVNSNG ELYHEQCFVC AQCFQQFPEG LFYEFEGRKY 130 140 150 160 170 180 CEHDFQMLFA PCCHQCGEFI IGRVIKAMNN SWHPECFRCD LCQEVLADIG FVKNAGRHLC 190 200 210 220 230 240 RPCHNREKAR GLGKYICQKC HAIIDEQPLI FKNDPYHPDH FNCANCGKEL TADARELKGE 250 260 270 280 290 300 LYCLPCHDKM GVPICGACRR PIEGRVVNAM GKQWHVEHFV CAKCEKPFLG HRHYERKGLA 310 320 330 340 350 360 YCETHYNQLF GDVCFHCNRV IEGDVVSALN KAWCVNCFAC STCNTKLTLK NKFVEFDMKP 370 380 VCKKCYEKFP LELKKRLKKL AETLGRK
	Isoform 4 [UniParc]. Checksum: A69518B2E12F39A5	FASTA	329	37,701
	10 20 30 40 50 60 MTCNMANALA SATCERCKGG FAPAEKIVNS NGELYHEQCF VCAQCFQQFP EGLFYEFEGR 70 80 90 100 110 120 KYCEHDFQML FAPCCHQCGE FIIGRVIKAM NNSWHPECFR CDLCQEVLAD IGFVKNAGRH 130 140 150 160 170 180 LCRPCHNREK ARGLGKYICQ KCHAIIDEQP LIFKNDPYHP DHFNCANCGK ELTADARELK 190 200 210 220 230 240 GELYCLPCHD KMGVPICGAC RRPIEGRVVN AMGKQWHVEH FVCAKCEKPF LGHRHYERKG 250 260 270 280 290 300 LAYCETHYNQ LFGDVCFHCN RVIEGDVVSA LNKAWCVNCF ACSTCNTKLT LKNKFVEFDM 310 320 KPVCKKCYEK FPLELKKRLK KLAETLGRK
	Isoform 5 [UniParc]. Checksum: B2123BE2DDC4736C	FASTA	362	41,571
	10 20 30 40 50 60 MTALQLKELS HSGLYRRRRD RPDSLRVNGL PEEELSNMAN ALASATCERC KGGFAPAEKI 70 80 90 100 110 120 VNSNGELYHE QCFVCAQCFQ QFPEGLFYEF EGRKYCEHDF QMLFAPCCHQ CGEFIIGRVI 130 140 150 160 170 180 KAMNNSWHPE CFRCDLCQEV LADIGFVKNA GRHLCRPCHN REKARGLGKY ICQKCHAIID 190 200 210 220 230 240 EQPLIFKNDP YHPDHFNCAN CGKELTADAR ELKGELYCLP CHDKMGVPIC GACRRPIEGR 250 260 270 280 290 300 VVNAMGKQWH VEHFVCAKCE KPFLGHRHYE RKGLAYCETH YNQLFGDVCF HCNRVIEGDV 310 320 330 340 350 360 VSALNKAWCV NCFACSTCNT KLTLKNKFVE FDMKPVCKKC YEKFPLELKK RLKKLAETLG RK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"A new LIM protein containing an autoepitope homologous to 'senescent cell antigen'." Rearden A. Biochem. Biophys. Res. Commun. 201:1124-1131(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Tissue: Fetal liver.
[2]	Rearden A. Submitted (MAR-2001) to the EMBL/GenBank/DDBJ databases Cited for: SEQUENCE REVISION TO C-TERMINUS.
[3]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2; 3 AND 5). Tissue: Testis, Tongue and Trachea.
[4]	"Generation and annotation of the DNA sequences of human chromosomes 2 and 4." Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K. Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	"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] (ISOFORM 1). Tissue: Bone marrow.
[6]	"Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides." Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J. Nat. Biotechnol. 21:566-569(2003) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-12, ACETYLATION AT ALA-2. Tissue: Platelet.
[7]	"Nck-2, a novel Src homology2/3-containing adaptor protein that interacts with the LIM-only protein PINCH and components of growth factor receptor kinase-signaling pathways." Tu Y., Li F., Wu C. Mol. Biol. Cell 9:3367-3382(1998) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH NCK2.
[8]	"Antigens recognized by autologous antibody in patients with renal-cell carcinoma." Scanlan M.J., Gordan J.D., Williamson B., Stockert E., Bander N.H., Jongeneel C.V., Gure A.O., Jaeger D., Jaeger E., Knuth A., Chen Y.-T., Old L.J. Int. J. Cancer 83:456-464(1999) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION AS A RENAL CANCER ANTIGEN. Tissue: Renal cell carcinoma.
[9]	"The LIM-only protein PINCH directly interacts with integrin-linked kinase and is recruited to integrin-rich sites in spreading cells." Tu Y., Li F., Goicoechea S., Wu C. Mol. Cell. Biol. 19:2425-2434(1999) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH ILK AND NCK2, SUBCELLULAR LOCATION.
[10]	"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].
[11]	"Solution structure of the focal adhesion adaptor PINCH LIM1 domain and characterization of its interaction with the integrin-linked kinase ankyrin repeat domain." Velyvis A., Yang Y., Wu C., Qin J. J. Biol. Chem. 276:4932-4939(2001) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF 1-70.
[12]	"Structural and functional insights into PINCH LIM4 domain-mediated integrin signaling." Velyvis A., Vaynberg J., Yang Y., Vinogradova O., Zhang Y., Wu C., Qin J. Nat. Struct. Biol. 10:558-564(2003) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF 188-251.
[13]	"Solution structure of the second and third LIM domain of particularly interesting new Cys-His protein (PINCH)." RIKEN structural genomics initiative (RSGI) Submitted (JUN-2006) to the PDB data bank Cited for: STRUCTURE BY NMR OF 71-190.
[14]	"The structural basis of integrin-linked kinase-PINCH interactions." Chiswell B.P., Zhang R., Murphy J.W., Boggon T.J., Calderwood D.A. Proc. Natl. Acad. Sci. U.S.A. 105:20677-20682(2008) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 6-68 IN COMPLEX WITH ILK, MUTAGENESIS OF PHE-42; HIS-61; ASP-62 AND LEU-66.
[15]	"Structural basis of focal adhesion localization of LIM-only adaptor PINCH by integrin-linked kinase." Yang Y., Wang X., Hawkins C.A., Chen K., Vaynberg J., Mao X., Tu Y., Zuo X., Wang J., Wang Y.-X., Wu C., Tjandra N., Qin J. J. Biol. Chem. 284:5836-5844(2009) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF 1-70 IN COMPLEX WITH ILK, MUTAGENESIS OF PHE-42 AND ARG-56, SUBCELLULAR LOCATION.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U09284 mRNA. Translation: AAA20086.2.
AK296992 mRNA. Translation: BAH12469.1.
AK302411 mRNA. Translation: BAH13699.1.
AK304260 mRNA. Translation: BAH14143.1.
AK314217 mRNA. Translation: BAG36891.1.
AC010095 Genomic DNA. Translation: AAY14983.1.
AC012487 Genomic DNA. No translation available.
BC005341 mRNA. Translation: AAH05341.1.

IPI

IPI00788612.
IPI00917739.

PIR

JC2324.

RefSeq

NP_001180411.1. NM_001193482.1.
NP_001180412.1. NM_001193483.2.
NP_001180413.1. NM_001193484.1.
NP_001180414.1. NM_001193485.2.
NP_001180417.1. NM_001193488.1.
NP_004978.2. NM_004987.5.

UniGene

Hs.597715.
Hs.613268.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1G47	NMR	-	A	1-70	[»]
1NYP	NMR	-	A	188-251	[»]
1U5S	NMR	-	B	188-251	[»]
2COR	NMR	-	A	125-190	[»]
2D8X	NMR	-	A	71-126	[»]
2KBX	NMR	-	B	1-70	[»]
3F6Q	X-ray	1.60	B	6-68	[»]

ProteinModelPortal

P48059.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-40671N.

IntAct

P48059. 24 interactions.

MINT

MINT-5004275.

STRING

9606.ENSP00000331775.

PTM databases

PhosphoSite

P48059.

Polymorphism databases

DMDM

18266876.

2D gel databases

OGP

P48059.

Proteomic databases

PaxDb

P48059.

PRIDE

P48059.

Protocols and materials databases

DNASU

3987.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000332345; ENSP00000331775; ENSG00000169756.
ENST00000338045; ENSP00000337598; ENSG00000169756.
ENST00000393310; ENSP00000376987; ENSG00000169756.
ENST00000409441; ENSP00000387264; ENSG00000169756.
ENST00000410093; ENSP00000386926; ENSG00000169756.
ENST00000542845; ENSP00000446121; ENSG00000169756.
ENST00000544547; ENSP00000437912; ENSG00000169756.

GeneID

3987.

KEGG

hsa:3987.

UCSC

uc002teg.3. human.

Organism-specific databases

CTD

3987.

GeneCards

GC02P109150.

HGNC

HGNC:6616. LIMS1.

MIM

602567. gene.

neXtProt

NX_P48059.

PharmGKB

PA30389.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG263350.

HOGENOM

HOG000253950.

HOVERGEN

HBG000053.

InParanoid

P48059.

OMA

QNRALCH.

OrthoDB

EOG4NP73S.

Enzyme and pathway databases

Reactome

REACT_111155. Cell-Cell communication.

Gene expression databases

ArrayExpress

P48059.

Bgee

P48059.

CleanEx

HS_LIMS1.

Genevestigator

P48059.

GermOnline

ENSG00000169756. Homo sapiens.

Family and domain databases

Gene3D

2.10.110.10. 5 hits.

InterPro

IPR017351. PINCH.
IPR001781. Znf_LIM.
[Graphical view]

Pfam

PF00412. LIM. 5 hits.
[Graphical view]

PIRSF

PIRSF038003. PINCH. 1 hit.

SMART

SM00132. LIM. 5 hits.
[Graphical view]

PROSITE

PS00478. LIM_DOMAIN_1. 4 hits.
PS50023. LIM_DOMAIN_2. 5 hits.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

LIMS1. human.

EvolutionaryTrace

P48059.

GenomeRNAi

3987.

NextBio

15640.

SOURCE

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Entry information

Entry name

LIMS1_HUMAN

Accession

Primary (citable) accession number: P48059
Secondary accession number(s): B2RAJ4 , B7Z483, B7Z7R3, B7Z907, Q53TE0, Q9BS44

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1996
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 137 of the entry and version 4 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.