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P48059

- LIMS1_HUMAN

UniProt

P48059 - LIMS1_HUMAN

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Protein

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

Gene
LIMS1, PINCH, PINCH1
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.

GO - Molecular functioni

  1. protein binding Source: UniProtKB
  2. zinc ion binding Source: UniProtKB

GO - Biological processi

  1. cell aging Source: ProtInc
  2. cell junction assembly Source: Reactome
  3. cellular response to transforming growth factor beta stimulus Source: UniProtKB
  4. negative regulation of transcription, DNA-templated Source: UniProtKB
Complete GO annotation...

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_20580. Regulation of cytoskeletal remodeling and cell spreading by IPP complex components.
REACT_20649. Cell-extracellular matrix interactions.

Names & Taxonomyi

Protein namesi
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 namesi
Name:LIMS1
Synonyms:PINCH, PINCH1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 2

Organism-specific databases

HGNCiHGNC:6616. LIMS1.

Subcellular locationi

Cell junctionfocal adhesion. Cell membrane; Peripheral membrane protein; Cytoplasmic side 2 Publications

GO - Cellular componenti

  1. cytosol Source: Reactome
  2. focal adhesion Source: UniProtKB
  3. perinuclear region of cytoplasm Source: UniProtKB
  4. plasma membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi42 – 421F → A: Loss of interaction with ILK and loss of localization to focal adhesion. 2 Publications
Mutagenesisi56 – 561R → A: Alters interaction with ILK. 1 Publication
Mutagenesisi61 – 611H → D: Alters interaction with ILK. 1 Publication
Mutagenesisi62 – 621D → A: Alters interaction with ILK. 1 Publication
Mutagenesisi66 – 661L → D: Alters interaction with ILK. 1 Publication

Organism-specific databases

PharmGKBiPA30389.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 325324LIM and senescent cell antigen-like-containing domain protein 1PRO_0000075888Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiP48059.
PaxDbiP48059.
PRIDEiP48059.

2D gel databases

OGPiP48059.

PTM databases

PhosphoSiteiP48059.

Expressioni

Tissue specificityi

Expressed in most tissues except in the brain.

Gene expression databases

ArrayExpressiP48059.
BgeeiP48059.
CleanExiHS_LIMS1.
GenevestigatoriP48059.

Interactioni

Subunit structurei

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.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Hoxa1P090223EBI-306928,EBI-3957603From a different organism.
ILKQ134185EBI-306928,EBI-747644
IlkO552223EBI-306928,EBI-6690138From a different organism.
NCK2O436392EBI-306928,EBI-713635

Protein-protein interaction databases

BioGridi110175. 16 interactions.
DIPiDIP-40671N.
IntActiP48059. 29 interactions.
MINTiMINT-5004275.
STRINGi9606.ENSP00000331775.

Structurei

Secondary structure

1
325
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni11 – 133
Beta strandi22 – 265
Beta strandi29 – 324
Turni33 – 353
Turni39 – 413
Helixi46 – 483
Beta strandi51 – 533
Beta strandi56 – 583
Helixi60 – 667
Beta strandi72 – 743
Beta strandi83 – 853
Beta strandi88 – 903
Turni92 – 943
Beta strandi98 – 1003
Beta strandi105 – 1073
Beta strandi110 – 1123
Beta strandi115 – 1173
Helixi119 – 1268
Turni136 – 1383
Beta strandi150 – 1523
Turni156 – 1583
Beta strandi162 – 1643
Beta strandi173 – 1753
Beta strandi178 – 1803
Helixi182 – 1865
Turni194 – 1974
Beta strandi210 – 2134
Turni214 – 2163
Turni220 – 2223
Beta strandi227 – 2293
Beta strandi232 – 2343
Beta strandi237 – 2393
Helixi241 – 2477

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1G47NMR-A1-70[»]
1NYPNMR-A188-251[»]
1U5SNMR-B188-251[»]
2CORNMR-A125-190[»]
2D8XNMR-A71-127[»]
2KBXNMR-B1-70[»]
3F6QX-ray1.60B6-68[»]
4HI8X-ray1.20B6-68[»]
4HI9X-ray1.20B6-68[»]
ProteinModelPortaliP48059.
SMRiP48059. Positions 6-305.

Miscellaneous databases

EvolutionaryTraceiP48059.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini10 – 6253LIM zinc-binding 1Add
BLAST
Domaini71 – 12151LIM zinc-binding 2Add
BLAST
Domaini135 – 18450LIM zinc-binding 3Add
BLAST
Domaini193 – 24351LIM zinc-binding 4Add
BLAST
Domaini252 – 30352LIM zinc-binding 5Add
BLAST

Sequence similaritiesi

Keywords - Domaini

LIM domain, Repeat

Phylogenomic databases

eggNOGiNOG263350.
HOGENOMiHOG000253950.
HOVERGENiHBG000053.
InParanoidiP48059.
OMAiNQNRALC.
PhylomeDBiP48059.
TreeFamiTF314113.

Family and domain databases

Gene3Di2.10.110.10. 5 hits.
InterProiIPR017351. PINCH.
IPR001781. Znf_LIM.
[Graphical view]
PANTHERiPTHR24210. PTHR24210. 1 hit.
PfamiPF00412. LIM. 5 hits.
[Graphical view]
PIRSFiPIRSF038003. PINCH. 1 hit.
SMARTiSM00132. LIM. 5 hits.
[Graphical view]
PROSITEiPS00478. LIM_DOMAIN_1. 4 hits.
PS50023. LIM_DOMAIN_2. 5 hits.
[Graphical view]

Sequences (5)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 5 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P48059-1) [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

MANALASATC ERCKGGFAPA EKIVNSNGEL YHEQCFVCAQ CFQQFPEGLF    50
YEFEGRKYCE HDFQMLFAPC CHQCGEFIIG RVIKAMNNSW HPECFRCDLC 100
QEVLADIGFV KNAGRHLCRP CHNREKARGL GKYICQKCHA IIDEQPLIFK 150
NDPYHPDHFN CANCGKELTA DARELKGELY CLPCHDKMGV PICGACRRPI 200
EGRVVNAMGK QWHVEHFVCA KCEKPFLGHR HYERKGLAYC ETHYNQLFGD 250
VCFHCNRVIE GDVVSALNKA WCVNCFACST CNTKLTLKNK FVEFDMKPVC 300
KKCYEKFPLE LKKRLKKLAE TLGRK 325
Length:325
Mass (Da):37,251
Last modified:January 23, 2007 - v4
Checksum:iE665FEB11D849CAE
GO
Isoform 2 (identifier: P48059-2) [UniParc]FASTAAdd to Basket

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

Note: No experimental confirmation available.

Show »
Length:337
Mass (Da):38,422
Checksum:i8577792E1A56418B
GO
Isoform 3 (identifier: P48059-3) [UniParc]FASTAAdd to Basket

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

Show »
Length:387
Mass (Da):44,390
Checksum:i3AB2EDB2203CEBFF
GO
Isoform 4 (identifier: P48059-4) [UniParc]FASTAAdd to Basket

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

Show »
Length:329
Mass (Da):37,701
Checksum:iA69518B2E12F39A5
GO
Isoform 5 (identifier: P48059-5) [UniParc]FASTAAdd to Basket

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

Show »
Length:362
Mass (Da):41,571
Checksum:iB2123BE2DDC4736C
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 11M → MLGVAAGMTHSNM in isoform 2. VSP_042672
Alternative sequencei1 – 11M → MAFSGRARPCIIPENEEIPR AALNTVHEANGTEDERAVSK LQRRHSDVKVYKEFCDFYAK FNM in isoform 3. VSP_043210
Alternative sequencei1 – 11M → MTCNM in isoform 4. VSP_043211
Alternative sequencei1 – 11M → MTALQLKELSHSGLYRRRRD RPDSLRVNGLPEEELSNM in isoform 5. VSP_043212

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti78 – 781I → T in AAH05341. 1 Publication
Sequence conflicti262 – 2621D → G in AAH05341. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS2078.1. [P48059-1]
CCDS54382.1. [P48059-2]
CCDS54383.1. [P48059-4]
CCDS54384.1. [P48059-5]
CCDS54385.1. [P48059-3]
PIRiJC2324.
RefSeqiNP_001180411.1. NM_001193482.1. [P48059-4]
NP_001180412.1. NM_001193483.2. [P48059-2]
NP_001180413.1. NM_001193484.1. [P48059-5]
NP_001180414.1. NM_001193485.2. [P48059-3]
NP_001180417.1. NM_001193488.1. [P48059-1]
NP_004978.2. NM_004987.5. [P48059-1]
UniGeneiHs.597715.
Hs.613268.

Genome annotation databases

EnsembliENST00000332345; ENSP00000331775; ENSG00000169756. [P48059-1]
ENST00000338045; ENSP00000337598; ENSG00000169756. [P48059-1]
ENST00000393310; ENSP00000376987; ENSG00000169756. [P48059-1]
ENST00000409441; ENSP00000387264; ENSG00000169756. [P48059-5]
ENST00000410093; ENSP00000386926; ENSG00000169756. [P48059-4]
ENST00000542845; ENSP00000446121; ENSG00000169756. [P48059-3]
ENST00000544547; ENSP00000437912; ENSG00000169756. [P48059-2]
GeneIDi3987.
KEGGihsa:3987.
UCSCiuc002teg.3. human. [P48059-1]
uc002tei.3. human. [P48059-4]
uc002tej.3. human. [P48059-5]
uc002tek.4. human. [P48059-3]
uc002tel.3. human. [P48059-2]

Polymorphism databases

DMDMi18266876.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS2078.1. [P48059-1 ]
CCDS54382.1. [P48059-2 ]
CCDS54383.1. [P48059-4 ]
CCDS54384.1. [P48059-5 ]
CCDS54385.1. [P48059-3 ]
PIRi JC2324.
RefSeqi NP_001180411.1. NM_001193482.1. [P48059-4 ]
NP_001180412.1. NM_001193483.2. [P48059-2 ]
NP_001180413.1. NM_001193484.1. [P48059-5 ]
NP_001180414.1. NM_001193485.2. [P48059-3 ]
NP_001180417.1. NM_001193488.1. [P48059-1 ]
NP_004978.2. NM_004987.5. [P48059-1 ]
UniGenei Hs.597715.
Hs.613268.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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 71-127 [» ]
2KBX NMR - B 1-70 [» ]
3F6Q X-ray 1.60 B 6-68 [» ]
4HI8 X-ray 1.20 B 6-68 [» ]
4HI9 X-ray 1.20 B 6-68 [» ]
ProteinModelPortali P48059.
SMRi P48059. Positions 6-305.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 110175. 16 interactions.
DIPi DIP-40671N.
IntActi P48059. 29 interactions.
MINTi MINT-5004275.
STRINGi 9606.ENSP00000331775.

PTM databases

PhosphoSitei P48059.

Polymorphism databases

DMDMi 18266876.

2D gel databases

OGPi P48059.

Proteomic databases

MaxQBi P48059.
PaxDbi P48059.
PRIDEi P48059.

Protocols and materials databases

DNASUi 3987.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000332345 ; ENSP00000331775 ; ENSG00000169756 . [P48059-1 ]
ENST00000338045 ; ENSP00000337598 ; ENSG00000169756 . [P48059-1 ]
ENST00000393310 ; ENSP00000376987 ; ENSG00000169756 . [P48059-1 ]
ENST00000409441 ; ENSP00000387264 ; ENSG00000169756 . [P48059-5 ]
ENST00000410093 ; ENSP00000386926 ; ENSG00000169756 . [P48059-4 ]
ENST00000542845 ; ENSP00000446121 ; ENSG00000169756 . [P48059-3 ]
ENST00000544547 ; ENSP00000437912 ; ENSG00000169756 . [P48059-2 ]
GeneIDi 3987.
KEGGi hsa:3987.
UCSCi uc002teg.3. human. [P48059-1 ]
uc002tei.3. human. [P48059-4 ]
uc002tej.3. human. [P48059-5 ]
uc002tek.4. human. [P48059-3 ]
uc002tel.3. human. [P48059-2 ]

Organism-specific databases

CTDi 3987.
GeneCardsi GC02P109150.
HGNCi HGNC:6616. LIMS1.
MIMi 602567. gene.
neXtProti NX_P48059.
PharmGKBi PA30389.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG263350.
HOGENOMi HOG000253950.
HOVERGENi HBG000053.
InParanoidi P48059.
OMAi NQNRALC.
PhylomeDBi P48059.
TreeFami TF314113.

Enzyme and pathway databases

Reactomei REACT_20580. Regulation of cytoskeletal remodeling and cell spreading by IPP complex components.
REACT_20649. Cell-extracellular matrix interactions.

Miscellaneous databases

ChiTaRSi LIMS1. human.
EvolutionaryTracei P48059.
GeneWikii LIMS1.
GenomeRNAii 3987.
NextBioi 15640.
PROi P48059.
SOURCEi Search...

Gene expression databases

ArrayExpressi P48059.
Bgeei P48059.
CleanExi HS_LIMS1.
Genevestigatori P48059.

Family and domain databases

Gene3Di 2.10.110.10. 5 hits.
InterProi IPR017351. PINCH.
IPR001781. Znf_LIM.
[Graphical view ]
PANTHERi PTHR24210. PTHR24210. 1 hit.
Pfami PF00412. LIM. 5 hits.
[Graphical view ]
PIRSFi PIRSF038003. PINCH. 1 hit.
SMARTi SM00132. LIM. 5 hits.
[Graphical view ]
PROSITEi PS00478. LIM_DOMAIN_1. 4 hits.
PS50023. LIM_DOMAIN_2. 5 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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. 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. 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.

Entry informationi

Entry nameiLIMS1_HUMAN
AccessioniPrimary (citable) accession number: P48059
Secondary accession number(s): B2RAJ4
, B7Z483, B7Z7R3, B7Z907, Q53TE0, Q9BS44
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: January 23, 2007
Last modified: September 3, 2014
This is version 150 of the entry and version 4 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, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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