Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

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

Gene

Lims1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: 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

GO - Biological processi

  • cell-cell junction organization Source: MGI
  • cell-matrix adhesion Source: MGI
  • chordate embryonic development Source: MGI
  • establishment of protein localization Source: MGI
  • establishment or maintenance of cell polarity Source: MGI
  • negative regulation of apoptotic process Source: MGI
  • negative regulation of epithelial cell proliferation Source: MGI
  • negative regulation of hepatocyte proliferation Source: MGI
  • negative regulation of neural precursor cell proliferation Source: MGI
  • negative regulation of transcription, DNA-templated Source: MGI
  • positive regulation of cell-substrate adhesion Source: MGI
  • positive regulation of focal adhesion assembly Source: MGI
  • positive regulation of gene expression Source: MGI
  • positive regulation of GTPase activity Source: MGI
  • positive regulation of integrin-mediated signaling pathway Source: MGI
  • positive regulation of substrate adhesion-dependent cell spreading Source: MGI
  • single organismal cell-cell adhesion Source: MGI
Complete GO annotation...

Keywords - Ligandi

Metal-binding, Zinc

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
Gene namesi
Name:Lims1
Synonyms:Pinch1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Unplaced

Organism-specific databases

MGIiMGI:1195263. Lims1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 325324LIM and senescent cell antigen-like-containing domain protein 1PRO_0000266009Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

EPDiQ99JW4.
MaxQBiQ99JW4.
PaxDbiQ99JW4.
PRIDEiQ99JW4.

PTM databases

PhosphoSiteiQ99JW4.

Expressioni

Gene expression databases

BgeeiQ99JW4.
CleanExiMM_LIMS1.

Interactioni

Subunit structurei

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 (By similarity). Interacts (via LIM zinc-binding 5) with TGFB1I1.By similarity1 Publication

GO - Molecular functioni

Protein-protein interaction databases

BioGridi225940. 7 interactions.
DIPiDIP-59289N.
IntActiQ99JW4. 2 interactions.
STRINGi10090.ENSMUSP00000020077.

Structurei

3D structure databases

ProteinModelPortaliQ99JW4.
SMRiQ99JW4. Positions 6-68, 71-305.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

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

Sequence similaritiesi

Contains 5 LIM zinc-binding domains.PROSITE-ProRule annotation

Keywords - Domaini

LIM domain, Repeat

Phylogenomic databases

eggNOGiKOG2272. Eukaryota.
ENOG410XP46. LUCA.
HOVERGENiHBG000053.
InParanoidiQ99JW4.
OrthoDBiEOG7GBFX3.
PhylomeDBiQ99JW4.
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]

Sequencei

Sequence statusi: Complete.

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

Q99JW4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MANALASATC ERCKGGFAPA EKIVNSNGEL YHEQCFVCAQ CFQQFPEGLF
60 70 80 90 100
YEFEGRKYCE HDFQMLFAPC CHQCGEFIIG RVIKAMNNSW HPECFRCDLC
110 120 130 140 150
QEVLADIGFV KNAGRHLCRP CHNREKARGL GKYICQKCHA IIDEQPLIFK
160 170 180 190 200
NDPYHPDHFN CANCGKELTA DARELKGELY CLPCHDKMGV PICGACRRPI
210 220 230 240 250
EGRVVNAMGK QWHVEHFVCA KCEKPFLGHR HYERKGLAYC ETHYNQLFGD
260 270 280 290 300
VCFHCNRVIE GDVVSALNKA WCVSCFACST CNTKLTLKNK FVEFDMKPVC
310 320
KKCYEKFPLE LKKRLKKLSE TLGRK
Length:325
Mass (Da):37,240
Last modified:January 23, 2007 - v3
Checksum:iE665FEA59B5FFDFE
GO

Sequence cautioni

The sequence AAH05621.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence BAB29637.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence BAC38699.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence BAC40663.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence BAE30227.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence BAE30814.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence BAE31411.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence BAE31922.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti59 – 591C → S in BAE30227 (PubMed:16141072).Curated
Sequence conflicti123 – 1231N → D in BAB29637 (PubMed:16141072).Curated
Sequence conflicti148 – 1481I → T in BAB29637 (PubMed:16141072).Curated
Sequence conflicti170 – 1701A → V in BAC40663 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK014954 mRNA. Translation: BAB29637.1. Different initiation.
AK082932 mRNA. Translation: BAC38699.1. Different initiation.
AK088939 mRNA. Translation: BAC40663.1. Different initiation.
AK151235 mRNA. Translation: BAE30227.1. Different initiation.
AK151938 mRNA. Translation: BAE30814.1. Different initiation.
AK152679 mRNA. Translation: BAE31411.1. Different initiation.
AK153346 mRNA. Translation: BAE31922.1. Different initiation.
BC005621 mRNA. Translation: AAH05621.1. Different initiation.
RefSeqiNP_080424.2. NM_026148.3.
XP_006513136.1. XM_006513073.2.
UniGeneiMm.402697.
Mm.482932.
Mm.57734.

Genome annotation databases

GeneIDi110829.
KEGGimmu:110829.
UCSCiuc011xeb.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK014954 mRNA. Translation: BAB29637.1. Different initiation.
AK082932 mRNA. Translation: BAC38699.1. Different initiation.
AK088939 mRNA. Translation: BAC40663.1. Different initiation.
AK151235 mRNA. Translation: BAE30227.1. Different initiation.
AK151938 mRNA. Translation: BAE30814.1. Different initiation.
AK152679 mRNA. Translation: BAE31411.1. Different initiation.
AK153346 mRNA. Translation: BAE31922.1. Different initiation.
BC005621 mRNA. Translation: AAH05621.1. Different initiation.
RefSeqiNP_080424.2. NM_026148.3.
XP_006513136.1. XM_006513073.2.
UniGeneiMm.402697.
Mm.482932.
Mm.57734.

3D structure databases

ProteinModelPortaliQ99JW4.
SMRiQ99JW4. Positions 6-68, 71-305.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi225940. 7 interactions.
DIPiDIP-59289N.
IntActiQ99JW4. 2 interactions.
STRINGi10090.ENSMUSP00000020077.

PTM databases

PhosphoSiteiQ99JW4.

Proteomic databases

EPDiQ99JW4.
MaxQBiQ99JW4.
PaxDbiQ99JW4.
PRIDEiQ99JW4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi110829.
KEGGimmu:110829.
UCSCiuc011xeb.1. mouse.

Organism-specific databases

CTDi3987.
MGIiMGI:1195263. Lims1.

Phylogenomic databases

eggNOGiKOG2272. Eukaryota.
ENOG410XP46. LUCA.
HOVERGENiHBG000053.
InParanoidiQ99JW4.
OrthoDBiEOG7GBFX3.
PhylomeDBiQ99JW4.
TreeFamiTF314113.

Miscellaneous databases

ChiTaRSiLims1. mouse.
NextBioi364741.
PROiQ99JW4.
SOURCEiSearch...

Gene expression databases

BgeeiQ99JW4.
CleanExiMM_LIMS1.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J and NOD.
    Tissue: Bone marrow, Testis and Thymus.
  2. "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].
    Strain: FVB/N.
    Tissue: Mammary tumor.
  3. "Oligomerizing potential of a focal adhesion LIM protein Hic-5 organizing a nuclear-cytoplasmic shuttling complex."
    Mori K., Asakawa M., Hayashi M., Imura M., Ohki T., Hirao E., Kim-Kaneyama J.-R., Nose K., Shibanuma M.
    J. Biol. Chem. 281:22048-22061(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TGFB1I1.
  4. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brown adipose tissue, Heart, Kidney, Lung, Spleen and Testis.

Entry informationi

Entry nameiLIMS1_MOUSE
AccessioniPrimary (citable) accession number: Q99JW4
Secondary accession number(s): Q3UAT7, Q8BTR6, Q9D5T4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 12, 2006
Last sequence update: January 23, 2007
Last modified: May 11, 2016
This is version 124 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. 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.