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P19973

- LSP1_MOUSE

UniProt

P19973 - LSP1_MOUSE

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Protein
Lymphocyte-specific protein 1
Gene
Lsp1, Pp52, S37, Wp34
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

May play a role in mediating neutrophil activation and chemotaxis.1 Publication

GO - Molecular functioni

  1. actin binding Source: MGI
  2. signal transducer activity Source: InterPro

GO - Biological processi

  1. apoptotic process Source: MGI
  2. chemotaxis Source: MGI
  3. cytoskeleton organization Source: MGI
  4. defense response Source: MGI
Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
Lymphocyte-specific protein 1
Alternative name(s):
52 kDa phosphoprotein
Short name:
pp52
Lymphocyte-specific antigen WP34
S37 protein
Gene namesi
Name:Lsp1
Synonyms:Pp52, S37, Wp34
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 7

Organism-specific databases

MGIiMGI:96832. Lsp1.

Subcellular locationi

GO - Cellular componenti

  1. plasma membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi195 – 1951S → A: No effect on phosphorylation by PKC, PKA, MAPKAPK2 and CaMK2. 1 Publication
Mutagenesisi243 – 2431S → A: Complete loss of phosphorylation by MAPKAPK2, partial loss of phosphorylation by PKA, no effect on phosphorylation by PKC and CaMK2. 1 Publication
Mutagenesisi243 – 2431S → E: Complete loss of phosphorylation by MAPKAPK2, partial loss of phosphorylation by PKA, no effect on phosphorylation by PKC and CaMK2. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 330330Lymphocyte-specific protein 1
PRO_0000084504Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei77 – 771Phosphoserine; by CK2 Reviewed prediction
Modified residuei78 – 781Phosphoserine; by CK2 Reviewed prediction
Modified residuei166 – 1661Phosphothreonine1 Publication
Modified residuei168 – 1681Phosphoserine1 Publication
Modified residuei180 – 1801Phosphoserine By similarity
Modified residuei243 – 2431Phosphoserine; by MAPKAPK21 Publication
Modified residuei318 – 3181N6-acetyllysine By similarity

Post-translational modificationi

Phosphorylated by casein kinase II, protein kinase C and MAPKAPK2. Phosphorylation by PKC induces translocation from membrane to cytoplasm. Phosphorylation by MAPKAPK2 may regulate neutrophil chemotaxis.3 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP19973.
PaxDbiP19973.
PRIDEiP19973.

PTM databases

PhosphoSiteiP19973.

Expressioni

Tissue specificityi

Isoform 1 is expressed in normal mouse B and T-lymphocytes and in transformed B-cells but not (or in smaller amounts) in nine T-lymphoma lines tested. Isoform 2 is expressed in non-lymphoid cell lines (myocytes, stromal cells, fibroblasts).

Gene expression databases

ArrayExpressiP19973.
BgeeiP19973.
CleanExiMM_LSP1.
GenevestigatoriP19973.

Interactioni

Protein-protein interaction databases

BioGridi201211. 2 interactions.
IntActiP19973. 1 interaction.

Structurei

3D structure databases

ProteinModelPortaliP19973.

Family & Domainsi

Phylogenomic databases

eggNOGiNOG149207.
GeneTreeiENSGT00730000111324.
HOVERGENiHBG001610.
InParanoidiA2A6J6.
KOiK14957.
OMAiRLTAQWS.
OrthoDBiEOG7FNC7W.
PhylomeDBiP19973.
TreeFamiTF336257.

Family and domain databases

InterProiIPR006018. Caldesmon_LSP.
IPR002211. Lymphspecific.
[Graphical view]
PANTHERiPTHR18949. PTHR18949. 1 hit.
PfamiPF02029. Caldesmon. 1 hit.
[Graphical view]
PRINTSiPR01083. LYMPHSPCIFIC.

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P19973-1) [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

MAEAAIDPRC EEQEELHAED SEGLTTQWRE EDEEEAAREQ RQRERERQLQ    50
DQDKDKEDDG GHSLEQPGQQ TLISLKSSEL DEDEGFGDWS QKPEPRQQFW 100
GNEGTAEGTE PSQSERPEEK QTEESSHQAK VHLEESNLSY REPDPEDAVG 150
GSGEAEEHLI RHQVRTPSPL ALEDTVELSS PPLSPTTKLA DRTESLNRSI 200
KKSNSVKKSQ PTLPISTIDE RLQQYTQATE SSGRTPKLSR QPSIELPSMA 250
VASTKTLWET GEVQSQSASK TPSCQDIVAG DMSKKSLWEQ KGGSKISSTI 300
KSTPSGKRYK FVATGHGKYE KVLVDEGSAP 330
Length:330
Mass (Da):36,714
Last modified:February 1, 1996 - v2
Checksum:iCCC27150F02859FB
GO
Isoform 2 (identifier: P19973-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-23: MAEAAIDPRCEEQEELHAEDSEG → MNGPALLRRNASKRGLEKLLR

Show »
Length:328
Mass (Da):36,548
Checksum:i43522E589AF1F6F0
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 2323MAEAA…EDSEG → MNGPALLRRNASKRGLEKLL R in isoform 2.
VSP_004313Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti125 – 1273SSH → RQV in BAC27463. 1 Publication
Sequence conflicti155 – 1562AE → PK1 Publication
Sequence conflicti158 – 1636Missing in AAH03796. 1 Publication
Sequence conflicti160 – 1601I → T1 Publication
Sequence conflicti168 – 1681S → N1 Publication
Sequence conflicti253 – 2531S → G1 Publication
Sequence conflicti283 – 2831S → T1 Publication
Sequence conflicti283 – 2831S → T1 Publication
Isoform 2 (identifier: P19973-2)
Sequence conflicti16 – 161L → Q in AAB37543. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M90316 mRNA. Translation: AAA65108.1.
S74179 mRNA. Translation: AAB32257.1.
M89956 mRNA. Translation: AAB48537.1.
D49691 mRNA. Translation: BAA08541.1.
AL603651 Genomic DNA. Translation: CAM23282.1.
AL603651 Genomic DNA. Translation: CAM23283.1.
BC003796 mRNA. Translation: AAH03796.1.
U30942, U30939, U30941 Genomic DNA. Translation: AAB37542.1.
U30942, U30940, U30941 Genomic DNA. Translation: AAB37543.1.
AK031587 mRNA. Translation: BAC27463.1.
CCDSiCCDS40193.1. [P19973-2]
CCDS52450.1. [P19973-1]
PIRiA30533.
A46521.
RefSeqiNP_001129543.1. NM_001136071.2. [P19973-1]
NP_001258437.1. NM_001271508.1.
NP_001258439.1. NM_001271510.1. [P19973-1]
NP_062264.1. NM_019391.3. [P19973-2]
UniGeneiMm.234003.

Genome annotation databases

EnsembliENSMUST00000018963; ENSMUSP00000018963; ENSMUSG00000018819. [P19973-1]
ENSMUST00000038946; ENSMUSP00000040637; ENSMUSG00000018819. [P19973-2]
ENSMUST00000105968; ENSMUSP00000101588; ENSMUSG00000018819. [P19973-1]
GeneIDi16985.
KEGGimmu:16985.
UCSCiuc009knb.2. mouse. [P19973-1]
uc009knf.1. mouse. [P19973-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M90316 mRNA. Translation: AAA65108.1 .
S74179 mRNA. Translation: AAB32257.1 .
M89956 mRNA. Translation: AAB48537.1 .
D49691 mRNA. Translation: BAA08541.1 .
AL603651 Genomic DNA. Translation: CAM23282.1 .
AL603651 Genomic DNA. Translation: CAM23283.1 .
BC003796 mRNA. Translation: AAH03796.1 .
U30942 , U30939 , U30941 Genomic DNA. Translation: AAB37542.1 .
U30942 , U30940 , U30941 Genomic DNA. Translation: AAB37543.1 .
AK031587 mRNA. Translation: BAC27463.1 .
CCDSi CCDS40193.1. [P19973-2 ]
CCDS52450.1. [P19973-1 ]
PIRi A30533.
A46521.
RefSeqi NP_001129543.1. NM_001136071.2. [P19973-1 ]
NP_001258437.1. NM_001271508.1.
NP_001258439.1. NM_001271510.1. [P19973-1 ]
NP_062264.1. NM_019391.3. [P19973-2 ]
UniGenei Mm.234003.

3D structure databases

ProteinModelPortali P19973.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 201211. 2 interactions.
IntActi P19973. 1 interaction.

PTM databases

PhosphoSitei P19973.

Proteomic databases

MaxQBi P19973.
PaxDbi P19973.
PRIDEi P19973.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000018963 ; ENSMUSP00000018963 ; ENSMUSG00000018819 . [P19973-1 ]
ENSMUST00000038946 ; ENSMUSP00000040637 ; ENSMUSG00000018819 . [P19973-2 ]
ENSMUST00000105968 ; ENSMUSP00000101588 ; ENSMUSG00000018819 . [P19973-1 ]
GeneIDi 16985.
KEGGi mmu:16985.
UCSCi uc009knb.2. mouse. [P19973-1 ]
uc009knf.1. mouse. [P19973-2 ]

Organism-specific databases

CTDi 4046.
MGIi MGI:96832. Lsp1.

Phylogenomic databases

eggNOGi NOG149207.
GeneTreei ENSGT00730000111324.
HOVERGENi HBG001610.
InParanoidi A2A6J6.
KOi K14957.
OMAi RLTAQWS.
OrthoDBi EOG7FNC7W.
PhylomeDBi P19973.
TreeFami TF336257.

Miscellaneous databases

NextBioi 291068.
PROi P19973.
SOURCEi Search...

Gene expression databases

ArrayExpressi P19973.
Bgeei P19973.
CleanExi MM_LSP1.
Genevestigatori P19973.

Family and domain databases

InterProi IPR006018. Caldesmon_LSP.
IPR002211. Lymphspecific.
[Graphical view ]
PANTHERi PTHR18949. PTHR18949. 1 hit.
Pfami PF02029. Caldesmon. 1 hit.
[Graphical view ]
PRINTSi PR01083. LYMPHSPCIFIC.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "A new lymphocyte-specific gene which encodes a putative Ca2+-binding protein is not expressed in transformed T lymphocyte lines."
    Jongstra J., Tidmarsh G.F., Jongstra-Bilen J., Davis M.M.
    J. Immunol. 141:3999-4004(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE (ISOFORM 1).
    Strain: BALB/c.
  2. "Alternatively spliced pp52 mRNA in nonlymphoid stromal cells."
    Gimble J.M., Dorheim M.-A., Youkhana K., Hudson J., Nead M., Gilly M., Wood W.J. Jr., Hermanson G.G., Kuehl M., Wall R., Kincade P.W.
    J. Immunol. 150:115-121(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
  3. "The LSP1 gene is expressed in cultured normal and transformed mouse macrophages."
    Jongstra J., Ittel M.E., Iscove N.N., Brady G.
    Mol. Immunol. 31:1125-1131(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Strain: BALB/c.
  4. "Protein kinase C phosphorylates p50 LSP1 and induces translocation of p50 LSP1 in T lymphocytes."
    Matsumoto N., Kojima S., Osawa T., Toyoshima S.
    J. Biochem. 117:222-229(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PHOSPHORYLATION.
    Strain: ICR.
    Tissue: Thymus.
  5. "Lymphocyte isoforms of mouse p50 LSP1, which are phosphorylated in mitogen-activated T cells, are formed through alternative splicing and phosphorylation."
    Matsumoto N., Kita K., Kojima S., Yamamoto K., Irimura T., Miyagi M., Tsunasawa S., Toyoshima S.
    J. Biochem. 118:237-243(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), ALTERNATIVE SPLICING.
    Strain: ICR.
    Tissue: Thymus.
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  7. "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 2).
    Strain: FVB/N.
    Tissue: Mammary gland.
  8. "Alternatively spliced exons encode the tissue-specific 5' termini of leukocyte pp52 and stromal cell S37 mRNA isoforms."
    Thompson A.A., Omori S.A., Gilly M.J., May W., Gordon M.S., Wood W.J. Jr., Miyoshi E., Malone C.S., Gimble J., Denny C.T., Wall R.
    Genomics 32:352-357(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 1-124 (ISOFORMS 1 AND 2), ALTERNATIVE SPLICING.
    Strain: BALB/c.
    Tissue: Leukocyte and Stromal cell.
  9. "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] OF 1-127 (ISOFORM 2).
    Strain: C57BL/6J.
    Tissue: Testis.
  10. "Characterization of the 50 kDa protein phosphorylated in concanavalin A-stimulated mouse T cells."
    Matsumoto N., Toyoshima S., Osawa T.
    J. Biochem. 113:630-636(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 55-81; 131-144; 211-229; 238-255 AND 311-330, PHOSPHORYLATION.
    Tissue: T-cell.
  11. "MAPKAPK2-mediated LSP1 phosphorylation and FMLP-induced neutrophil polarization."
    Wu Y., Zhan L., Ai Y., Hannigan M., Gaestel M., Huang C.-K., Madri J.A.
    Biochem. Biophys. Res. Commun. 358:170-175(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-243 BY MAPKAPK2, MUTAGENESIS OF SER-195 AND SER-243, FUNCTION.
  12. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-166 AND SER-168, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiLSP1_MOUSE
AccessioniPrimary (citable) accession number: P19973
Secondary accession number(s): A2A6J5
, A2A6J6, P97339, Q04950, Q62022, Q62023, Q62024, Q8CD28, Q99L65
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: February 1, 1996
Last modified: July 9, 2014
This is version 135 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

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

External Data

Dasty 3

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