Reviewed, UniProtKB/Swiss-Prot Q99JW4 (LIMS1_MOUSE)

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

Gene names

Name:	Lims1
Synonyms:	Pinch1

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

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	Effector of integrin and growth factor signaling, coupling surface receptors to downstream signaling molecules involved in the regulation of cell survival, cell proliferation and cell differentiation. Focal adhesion protein part of the complex ILK-PINCH. This complex is considered to be one of the convergence points of integrin- and growth factor-signaling pathway.
Subunit structure	Interacts (via LIM zinc-binding 1) with ILK. Interacts with SH3/SH2 adapter NCK2 By similarity. Interacts (via LIM zinc-binding 5) with TGFB1I1.
Subcellular location	Cell junction › focal adhesion By similarity. Cell membrane; Peripheral membrane protein; Cytoplasmic side By similarity.
Sequence similarities	Contains 5 LIM zinc-binding domains.

Ontologies

Keywords
Cellular component	Cell junction Cell membrane Membrane
Domain	LIM domain Repeat
Ligand	Metal-binding Zinc
PTM	Acetylation
Gene Ontology (GO)
Biological process	cell-cell adhesion Inferred from mutant phenotype. Source: MGI cell-matrix adhesion Inferred from mutant phenotype. Source: MGI chordate embryonic development Inferred from mutant phenotype. Source: MGI establishment or maintenance of cell polarity Inferred from mutant phenotype. Source: MGI
Cellular component	focal adhesion Inferred from direct assay. Source: MGI
Molecular function	protein binding Inferred from sequence or structural similarity. Source: UniProtKB zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed By similarity
	Chain	2 – 325	324	LIM and senescent cell antigen-like-containing domain protein 1		PRO_0000266009
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 By similarity
Experimental info
	Sequence conflict	59	1	C → S in BAE30227. Ref.1
	Sequence conflict	123	1	N → D in BAB29637. Ref.1
	Sequence conflict	148	1	I → T in BAB29637. Ref.1
	Sequence conflict	170	1	A → V in BAC40663. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q99JW4-1 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: E665FEA59B5FFDFE	FASTA	325	37,240
	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 WCVSCFACST CNTKLTLKNK FVEFDMKPVC 310 320 KKCYEKFPLE LKKRLKKLSE TLGRK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 16141072] [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: 15489334] [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: 16737959] [Abstract] Cited for: INTERACTION WITH TGFB1I1.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	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.
IPI	IPI00108427.
RefSeq	NP_080424.2.
UniGene	Mm.402697 Mm.443353 Mm.57734
3D structure databases
SMR	Q99JW4. Positions 1-70, 71-129, 125-190, 188-251.
ModBase	Search...
PTM databases
PhosphoSite	Q99JW4.
Genome annotation databases
Ensembl	ENSMUSG00000019920. Mus musculus. [Contig view]
GeneID	110829.
KEGG	mmu:110829.
Organism-specific databases
MGI	MGI:1195263. Lims1.
Phylogenomic databases
HOVERGEN	Q99JW4.
Gene expression databases
ArrayExpress	Q99JW4.
Bgee	Q99JW4.
CleanEx	MM_LIMS1.
GermOnline	ENSMUSG00000019920. Mus musculus.
Family and domain databases
InterPro	IPR017351. PINCH. IPR001781. Znf_LIM. [Graphical view]
Gene3D	G3DSA:2.10.110.10. Znf_LIM. 4 hits.
Pfam	PF00412. LIM. 5 hits. [Graphical view]
PIRSF	PIRSF038003. PINCH. 1 hit.
ProDom	PD000094. LIM. 5 hits. [Graphical view] [Entries sharing at least one domain]
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 Resources
NextBio	364741.
SOURCE	Search...

Entry information

Entry name

LIMS1_MOUSE

Accession

Primary (citable) accession number: Q99JW4
Secondary accession number(s): Q3UAT7, Q8BTR6, Q9D5T4

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 12, 2006
Last sequence update:	January 23, 2007
Last modified:	June 16, 2009
This is version 58 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)