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P19973 (LSP1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 135. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Lymphocyte-specific protein 1
Alternative name(s):
52 kDa phosphoprotein
Short name=pp52
Lymphocyte-specific antigen WP34
S37 protein
Gene names
Name:Lsp1
Synonyms:Pp52, S37, Wp34
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length330 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

May play a role in mediating neutrophil activation and chemotaxis. Ref.11

Subcellular location

Cell membrane; Peripheral membrane protein; Cytoplasmic side.

Tissue specificity

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).

Post-translational modification

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. Ref.4 Ref.10 Ref.11

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P19973-1)

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: P19973-2)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 330330Lymphocyte-specific protein 1
PRO_0000084504

Amino acid modifications

Modified residue771Phosphoserine; by CK2 Potential
Modified residue781Phosphoserine; by CK2 Potential
Modified residue1661Phosphothreonine Ref.12
Modified residue1681Phosphoserine Ref.12
Modified residue1801Phosphoserine By similarity
Modified residue2431Phosphoserine; by MAPKAPK2 Ref.11
Modified residue3181N6-acetyllysine By similarity

Natural variations

Alternative sequence1 – 2323MAEAA…EDSEG → MNGPALLRRNASKRGLEKLL R in isoform 2.
VSP_004313

Experimental info

Mutagenesis1951S → A: No effect on phosphorylation by PKC, PKA, MAPKAPK2 and CaMK2. Ref.11
Mutagenesis2431S → A: Complete loss of phosphorylation by MAPKAPK2, partial loss of phosphorylation by PKA, no effect on phosphorylation by PKC and CaMK2. Ref.11
Mutagenesis2431S → E: Complete loss of phosphorylation by MAPKAPK2, partial loss of phosphorylation by PKA, no effect on phosphorylation by PKC and CaMK2. Ref.11
Sequence conflict125 – 1273SSH → RQV in BAC27463. Ref.9
Sequence conflict155 – 1562AE → PK Ref.1
Sequence conflict158 – 1636Missing in AAH03796. Ref.7
Sequence conflict1601I → T Ref.1
Sequence conflict1681S → N Ref.1
Sequence conflict2531S → G Ref.1
Sequence conflict2831S → T Ref.4
Sequence conflict2831S → T Ref.5
Isoform 2:
Sequence conflict161L → Q in AAB37543. Ref.8

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified February 1, 1996. Version 2.
Checksum: CCC27150F02859FB

FASTA33036,714
        10         20         30         40         50         60 
MAEAAIDPRC EEQEELHAED SEGLTTQWRE EDEEEAAREQ RQRERERQLQ DQDKDKEDDG 

        70         80         90        100        110        120 
GHSLEQPGQQ TLISLKSSEL DEDEGFGDWS QKPEPRQQFW GNEGTAEGTE PSQSERPEEK 

       130        140        150        160        170        180 
QTEESSHQAK VHLEESNLSY REPDPEDAVG GSGEAEEHLI RHQVRTPSPL ALEDTVELSS 

       190        200        210        220        230        240 
PPLSPTTKLA DRTESLNRSI KKSNSVKKSQ PTLPISTIDE RLQQYTQATE SSGRTPKLSR 

       250        260        270        280        290        300 
QPSIELPSMA VASTKTLWET GEVQSQSASK TPSCQDIVAG DMSKKSLWEQ KGGSKISSTI 

       310        320        330 
KSTPSGKRYK FVATGHGKYE KVLVDEGSAP 

« Hide

Isoform 2 [UniParc].

Checksum: 43522E589AF1F6F0
Show »

FASTA32836,548

References

« Hide 'large scale' references
[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]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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]"Large-scale phosphorylation analysis of mouse liver."
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-166 AND SER-168, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS40193.1. [P19973-2]
CCDS52450.1. [P19973-1]
PIRA30533.
A46521.
RefSeqNP_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]
UniGeneMm.234003.

3D structure databases

ProteinModelPortalP19973.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid201211. 2 interactions.
IntActP19973. 1 interaction.

PTM databases

PhosphoSiteP19973.

Proteomic databases

MaxQBP19973.
PaxDbP19973.
PRIDEP19973.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000018963; ENSMUSP00000018963; ENSMUSG00000018819. [P19973-1]
ENSMUST00000038946; ENSMUSP00000040637; ENSMUSG00000018819. [P19973-2]
ENSMUST00000105968; ENSMUSP00000101588; ENSMUSG00000018819. [P19973-1]
GeneID16985.
KEGGmmu:16985.
UCSCuc009knb.2. mouse. [P19973-1]
uc009knf.1. mouse. [P19973-2]

Organism-specific databases

CTD4046.
MGIMGI:96832. Lsp1.

Phylogenomic databases

eggNOGNOG149207.
GeneTreeENSGT00730000111324.
HOVERGENHBG001610.
InParanoidA2A6J6.
KOK14957.
OMARLTAQWS.
OrthoDBEOG7FNC7W.
PhylomeDBP19973.
TreeFamTF336257.

Gene expression databases

ArrayExpressP19973.
BgeeP19973.
CleanExMM_LSP1.
GenevestigatorP19973.

Family and domain databases

InterProIPR006018. Caldesmon_LSP.
IPR002211. Lymphspecific.
[Graphical view]
PANTHERPTHR18949. PTHR18949. 1 hit.
PfamPF02029. Caldesmon. 1 hit.
[Graphical view]
PRINTSPR01083. LYMPHSPCIFIC.
ProtoNetSearch...

Other

NextBio291068.
PROP19973.
SOURCESearch...

Entry information

Entry nameLSP1_MOUSE
AccessionPrimary (citable) accession number: P19973
Secondary accession number(s): A2A6J5 expand/collapse secondary AC list , A2A6J6, P97339, Q04950, Q62022, Q62023, Q62024, Q8CD28, Q99L65
Entry history
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 statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

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