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P30204

- MSRE_MOUSE

UniProt

P30204 - MSRE_MOUSE

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Protein

Macrophage scavenger receptor types I and II

Gene

Msr1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Membrane glycoproteins implicated in the pathologic deposition of cholesterol in arterial walls during atherogenesis. Two types of receptor subunits exist. These receptors mediate the endocytosis of a diverse group of macromolecules, including modified low density lipoproteins (LDL).

GO - Molecular functioni

  1. low-density lipoprotein particle binding Source: BHF-UCL
  2. scavenger receptor activity Source: InterPro

GO - Biological processi

  1. cholesterol transport Source: BHF-UCL
  2. lipoprotein transport Source: MGI
  3. plasma lipoprotein particle clearance Source: BHF-UCL
  4. positive regulation of cholesterol storage Source: BHF-UCL
  5. positive regulation of macrophage derived foam cell differentiation Source: BHF-UCL
Complete GO annotation...

Keywords - Molecular functioni

Receptor

Keywords - Biological processi

Endocytosis

Enzyme and pathway databases

ReactomeiREACT_196581. Scavenging by Class A Receptors.
REACT_209041. Scavenging by Class A Receptors.

Names & Taxonomyi

Protein namesi
Recommended name:
Macrophage scavenger receptor types I and II
Alternative name(s):
Macrophage acetylated LDL receptor I and II
Scavenger receptor type A
Short name:
SR-A
CD_antigen: CD204
Gene namesi
Name:Msr1
Synonyms:Scvr
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 8

Organism-specific databases

MGIiMGI:98257. Msr1.

Subcellular locationi

GO - Cellular componenti

  1. collagen trimer Source: UniProtKB-KW
  2. cytoplasmic vesicle Source: Ensembl
  3. cytosol Source: Ensembl
  4. integral component of membrane Source: UniProtKB-KW
  5. low-density lipoprotein particle Source: UniProtKB-KW
  6. plasma membrane Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

LDL, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 458458Macrophage scavenger receptor types I and IIPRO_0000181628Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei32 – 321Phosphoserine1 Publication
Modified residuei36 – 361Phosphoserine1 Publication
Glycosylationi94 – 941N-linked (GlcNAc...)Sequence Analysis
Glycosylationi107 – 1071N-linked (GlcNAc...)Sequence Analysis
Glycosylationi147 – 1471N-linked (GlcNAc...)Sequence Analysis
Glycosylationi188 – 1881N-linked (GlcNAc...)Sequence Analysis
Glycosylationi253 – 2531N-linked (GlcNAc...)Sequence Analysis
Glycosylationi271 – 2711N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi382 ↔ 446PROSITE-ProRule annotation
Disulfide bondi395 ↔ 456PROSITE-ProRule annotation
Disulfide bondi426 ↔ 436PROSITE-ProRule annotation

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiP30204.
PaxDbiP30204.
PRIDEiP30204.

PTM databases

PhosphoSiteiP30204.

Expressioni

Gene expression databases

BgeeiP30204.
CleanExiMM_MSR1.
ExpressionAtlasiP30204. baseline and differential.
GenevestigatoriP30204.

Interactioni

Subunit structurei

Homotrimer.

Protein-protein interaction databases

IntActiP30204. 1 interaction.

Structurei

3D structure databases

ProteinModelPortaliP30204.
SMRiP30204. Positions 357-458.
ModBaseiSearch...
MobiDBiSearch...

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 5555CytoplasmicSequence AnalysisAdd
BLAST
Topological domaini79 – 458380ExtracellularSequence AnalysisAdd
BLAST

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei56 – 7823Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
BLAST

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini277 – 35074Collagen-likeAdd
BLAST
Domaini357 – 457101SRCRPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni79 – 11436SpacerCuratedAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili209 – 25951Sequence AnalysisAdd
BLAST

Sequence similaritiesi

Contains 1 collagen-like domain.Curated
Contains 1 SRCR domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil, Collagen, Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG150350.
GeneTreeiENSGT00760000119263.
HOGENOMiHOG000085659.
HOVERGENiHBG002473.
InParanoidiP30204.
KOiK06558.
OMAiKWEMKNC.
OrthoDBiEOG7V1FQV.
TreeFamiTF330855.

Family and domain databases

Gene3Di3.10.250.10. 1 hit.
InterProiIPR008160. Collagen.
IPR003543. Macro_scav_rcpt.
IPR001190. SRCR.
IPR017448. SRCR-like_dom.
[Graphical view]
PfamiPF01391. Collagen. 2 hits.
PF03523. Macscav_rec. 1 hit.
PF00530. SRCR. 1 hit.
[Graphical view]
PRINTSiPR01408. MACSCAVRCPTR.
PR00258. SPERACTRCPTR.
SMARTiSM00202. SR. 1 hit.
[Graphical view]
SUPFAMiSSF56487. SSF56487. 1 hit.
PROSITEiPS00420. SRCR_1. 1 hit.
PS50287. SRCR_2. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform I (identifier: P30204-1) [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

        10         20         30         40         50
MTKEMTENQR LCPHEQEDAD CSSESVKFDA RSMTASLPHS TKNGPSLQEK
60 70 80 90 100
LKSFKAALIA LYLLVFAVLI PVVGIVTAQL LNWEMKNCLV CSLNTSDTSQ
110 120 130 140 150
GPMEKENTSK VEMRFTIIME HMKDMEERIE SISNSKADLI DTERFQNFSM
160 170 180 190 200
ATDQRLNDIL LQLNSLISSV QEHGNSLDAI SKSLQSLNMT LLDVQLHTET
210 220 230 240 250
LNVRVRESTA KQQEDISKLE ERVYKVSAEV QSVKEEQAHV EQEVKQEVRV
260 270 280 290 300
LNNITNDLRL KDWEHSQTLK NITFIQGPPG PQGEKGDRGL TGQTGPPGAP
310 320 330 340 350
GIRGIPGVKG DRGQIGFPGG RGNPGAPGKP GRSGSPGPKG QKGEKGSVGG
360 370 380 390 400
STPLKTVRLV GGSGAHEGRV EIFHQGQWGT ICDDRWDIRA GQVVCRSLGY
410 420 430 440 450
QEVLAVHKRA HFGQGTGPIW LNEVMCFGRE SSIENCKINQ WGVLSCSHSE

DAGVTCTS
Length:458
Mass (Da):50,170
Last modified:July 27, 2011 - v3
Checksum:iDA069B90A6B59EB5
GO
Isoform II (identifier: P30204-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     352-354: TPL → RSV
     355-458: Missing.

Show »
Length:354
Mass (Da):38,773
Checksum:i348E084D2D8B644B
GO

Sequence cautioni

The sequence AAA39747.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
The sequence AAA39748.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti16 – 161Q → R in AAA39747. (PubMed:8394868)Curated
Sequence conflicti16 – 161Q → R in AAA39748. (PubMed:8394868)Curated
Sequence conflicti16 – 161Q → R in BAA02650. (PubMed:8380589)Curated
Sequence conflicti16 – 161Q → R in AAF14001. 1 PublicationCurated
Sequence conflicti16 – 161Q → R in BAC40779. (PubMed:16141072)Curated
Sequence conflicti16 – 161Q → R in AAH03814. (PubMed:15489334)Curated
Sequence conflicti47 – 471L → V in AAA39747. (PubMed:8394868)Curated
Sequence conflicti47 – 471L → V in AAA39748. (PubMed:8394868)Curated
Sequence conflicti47 – 471L → V in BAA02650. (PubMed:8380589)Curated
Sequence conflicti47 – 471L → V in BAC40779. (PubMed:16141072)Curated
Sequence conflicti47 – 471L → V in AAH03814. (PubMed:15489334)Curated
Sequence conflicti93 – 931L → R in AAA39747. (PubMed:8394868)Curated
Sequence conflicti93 – 931L → R in AAA39748. (PubMed:8394868)Curated
Sequence conflicti93 – 931L → R in BAA02650. (PubMed:8380589)Curated
Sequence conflicti93 – 931L → R in AAF14001. 1 PublicationCurated
Sequence conflicti93 – 931L → R in BAC40779. (PubMed:16141072)Curated
Sequence conflicti93 – 931L → R in AAH03814. (PubMed:15489334)Curated
Sequence conflicti110 – 1101K → N in AAA39747. (PubMed:8394868)Curated
Sequence conflicti110 – 1101K → N in AAA39748. (PubMed:8394868)Curated
Sequence conflicti110 – 1101K → N in BAA02650. (PubMed:8380589)Curated
Sequence conflicti110 – 1101K → N in BAC40779. (PubMed:16141072)Curated
Sequence conflicti110 – 1101K → N in AAH03814. (PubMed:15489334)Curated
Sequence conflicti120 – 1201E → A in AAA39747. (PubMed:8394868)Curated
Sequence conflicti120 – 1201E → A in AAA39748. (PubMed:8394868)Curated
Sequence conflicti120 – 1201E → A in BAA02650. (PubMed:8380589)Curated
Sequence conflicti120 – 1201E → A in BAC40779. (PubMed:16141072)Curated
Sequence conflicti120 – 1201E → A in AAH03814. (PubMed:15489334)Curated
Sequence conflicti130 – 1301E → Q in AAA39747. (PubMed:8394868)Curated
Sequence conflicti130 – 1301E → Q in AAA39748. (PubMed:8394868)Curated
Sequence conflicti130 – 1301E → Q in BAA02650. (PubMed:8380589)Curated
Sequence conflicti130 – 1301E → Q in BAC40779. (PubMed:16141072)Curated
Sequence conflicti130 – 1301E → Q in AAH03814. (PubMed:15489334)Curated
Sequence conflicti143 – 1431E → G in AAA39747. (PubMed:8394868)Curated
Sequence conflicti143 – 1431E → G in AAA39748. (PubMed:8394868)Curated
Sequence conflicti143 – 1431E → G in BAA02650. (PubMed:8380589)Curated
Sequence conflicti143 – 1431E → G in AAF14001. 1 PublicationCurated
Sequence conflicti143 – 1431E → G in BAC40779. (PubMed:16141072)Curated
Sequence conflicti143 – 1431E → G in AAH03814. (PubMed:15489334)Curated
Sequence conflicti168 – 1681S → L in AAA39747. (PubMed:8394868)Curated
Sequence conflicti168 – 1681S → L in AAA39748. (PubMed:8394868)Curated
Sequence conflicti168 – 1681S → L in BAA02650. (PubMed:8380589)Curated
Sequence conflicti168 – 1681S → L in BAC40779. (PubMed:16141072)Curated
Sequence conflicti168 – 1681S → L in AAH03814. (PubMed:15489334)Curated
Sequence conflicti202 – 2021N → H in AAA39747. (PubMed:8394868)Curated
Sequence conflicti202 – 2021N → H in AAA39748. (PubMed:8394868)Curated
Sequence conflicti202 – 2021N → H in BAA02650. (PubMed:8380589)Curated
Sequence conflicti202 – 2021N → H in BAC40779. (PubMed:16141072)Curated
Sequence conflicti202 – 2021N → H in AAH03814. (PubMed:15489334)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei352 – 3543TPL → RSV in isoform II. 4 PublicationsVSP_006231
Alternative sequencei355 – 458104Missing in isoform II. 4 PublicationsVSP_006232Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L04274 mRNA. Translation: AAA39747.1. Different initiation.
L04275 mRNA. Translation: AAA39748.1. Different initiation.
D13382 mRNA. Translation: BAA02650.1.
AF203781 mRNA. Translation: AAF14001.1.
M59445 mRNA. Translation: AAA37464.1.
M59446 mRNA. Translation: AAA37465.1.
U13873 Genomic DNA. Translation: AAC13774.1.
AK089178 mRNA. Translation: BAC40779.1.
AC111028 Genomic DNA. No translation available.
BC003814 mRNA. Translation: AAH03814.1.
CCDSiCCDS52542.1. [P30204-1]
CCDS52543.1. [P30204-2]
PIRiB44407.
I73338.
RefSeqiNP_001106797.1. NM_001113326.1. [P30204-1]
UniGeneiMm.239291.

Genome annotation databases

EnsembliENSMUST00000026021; ENSMUSP00000026021; ENSMUSG00000025044. [P30204-1]
ENSMUST00000170091; ENSMUSP00000132535; ENSMUSG00000025044. [P30204-2]
GeneIDi20288.
KEGGimmu:20288.
UCSCiuc012gcm.1. mouse. [P30204-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L04274 mRNA. Translation: AAA39747.1 . Different initiation.
L04275 mRNA. Translation: AAA39748.1 . Different initiation.
D13382 mRNA. Translation: BAA02650.1 .
AF203781 mRNA. Translation: AAF14001.1 .
M59445 mRNA. Translation: AAA37464.1 .
M59446 mRNA. Translation: AAA37465.1 .
U13873 Genomic DNA. Translation: AAC13774.1 .
AK089178 mRNA. Translation: BAC40779.1 .
AC111028 Genomic DNA. No translation available.
BC003814 mRNA. Translation: AAH03814.1 .
CCDSi CCDS52542.1. [P30204-1 ]
CCDS52543.1. [P30204-2 ]
PIRi B44407.
I73338.
RefSeqi NP_001106797.1. NM_001113326.1. [P30204-1 ]
UniGenei Mm.239291.

3D structure databases

ProteinModelPortali P30204.
SMRi P30204. Positions 357-458.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi P30204. 1 interaction.

Chemistry

BindingDBi P30204.
ChEMBLi CHEMBL4399.

PTM databases

PhosphoSitei P30204.

Proteomic databases

MaxQBi P30204.
PaxDbi P30204.
PRIDEi P30204.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000026021 ; ENSMUSP00000026021 ; ENSMUSG00000025044 . [P30204-1 ]
ENSMUST00000170091 ; ENSMUSP00000132535 ; ENSMUSG00000025044 . [P30204-2 ]
GeneIDi 20288.
KEGGi mmu:20288.
UCSCi uc012gcm.1. mouse. [P30204-1 ]

Organism-specific databases

CTDi 4481.
MGIi MGI:98257. Msr1.

Phylogenomic databases

eggNOGi NOG150350.
GeneTreei ENSGT00760000119263.
HOGENOMi HOG000085659.
HOVERGENi HBG002473.
InParanoidi P30204.
KOi K06558.
OMAi KWEMKNC.
OrthoDBi EOG7V1FQV.
TreeFami TF330855.

Enzyme and pathway databases

Reactomei REACT_196581. Scavenging by Class A Receptors.
REACT_209041. Scavenging by Class A Receptors.

Miscellaneous databases

ChiTaRSi MSR1. mouse.
NextBioi 297995.
PROi P30204.
SOURCEi Search...

Gene expression databases

Bgeei P30204.
CleanExi MM_MSR1.
ExpressionAtlasi P30204. baseline and differential.
Genevestigatori P30204.

Family and domain databases

Gene3Di 3.10.250.10. 1 hit.
InterProi IPR008160. Collagen.
IPR003543. Macro_scav_rcpt.
IPR001190. SRCR.
IPR017448. SRCR-like_dom.
[Graphical view ]
Pfami PF01391. Collagen. 2 hits.
PF03523. Macscav_rec. 1 hit.
PF00530. SRCR. 1 hit.
[Graphical view ]
PRINTSi PR01408. MACSCAVRCPTR.
PR00258. SPERACTRCPTR.
SMARTi SM00202. SR. 1 hit.
[Graphical view ]
SUPFAMi SSF56487. SSF56487. 1 hit.
PROSITEi PS00420. SRCR_1. 1 hit.
PS50287. SRCR_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Structures and high and low affinity ligand binding properties of murine type I and type II macrophage scavenger receptors."
    Ashkenas J., Penman M., Vasile E., Acton S., Freeman M.W., Krieger M.
    J. Lipid Res. 34:983-1000(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS I AND II).
  2. "Charged collagen structure mediates the recognition of negatively charged macromolecules by macrophage scavenger receptors."
    Doi T., Wada Y., Kodama T., Higashi K.I., Kurihara Y., Miyazaki T., Nakamura H., Uesugi S., Imanishi T., Kawabe Y., Itakura H., Yazaki Y., Matsumoto A.
    J. Biol. Chem. 268:2126-2133(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM II).
  3. "Identification of a functional domain in class A scavenger receptors that mediates metabolism of AcLDL."
    Rateri D.L., Whitman S.C., Block A.E., Daugherty A.
    Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE (ISOFORM I).
    Strain: C57BL/6.
  4. "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] (ISOFORM II).
    Strain: NOD.
    Tissue: Thymus.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  6. "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 II).
  7. "An ancient, highly conserved family of cysteine-rich protein domains revealed by cloning type I and type II murine macrophage scavenger receptors."
    Freeman M., Ashkenas J., Rees D.J., Kingsley D.M., Copeland N.G., Jenkins N.A., Krieger M.
    Proc. Natl. Acad. Sci. U.S.A. 87:8810-8814(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 349-458.
  8. "Structure of the murine macrophage scavenger receptor gene and evaluation of sequences that regulate expression in the macrophage cell line, P388D."
    Aftring R.P., Freeman M.W.
    J. Lipid Res. 36:1305-1314(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-4.
  9. "The phagosomal proteome in interferon-gamma-activated macrophages."
    Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
    Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-32 AND SER-36, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiMSRE_MOUSE
AccessioniPrimary (citable) accession number: P30204
Secondary accession number(s): E9QNQ5, Q923G0, Q9QZ56
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: July 27, 2011
Last modified: October 29, 2014
This is version 143 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

External Data

Dasty 3