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Q61029

- LAP2B_MOUSE

UniProt

Q61029 - LAP2B_MOUSE

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Protein

Lamina-associated polypeptide 2, isoforms beta/delta/epsilon/gamma

Gene
Tmpo, Lap2
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

May help direct the assembly of the nuclear lamina and thereby help maintain the structural organization of the nuclear envelope. Possible receptor for attachment of lamin filaments to the inner nuclear membrane. May be involved in the control of initiation of DNA replication through its interaction with NAKAP95 By similarity.

GO - Molecular functioni

  1. DNA binding Source: UniProtKB-KW
  2. protein binding Source: IntAct

GO - Biological processi

  1. regulation of transcription, DNA-templated Source: MGI
Complete GO annotation...

Keywords - Ligandi

DNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Lamina-associated polypeptide 2, isoforms beta/delta/epsilon/gamma
Alternative name(s):
Thymopoietin isoforms beta/delta/epsilon/gamma
Short name:
TP beta/delta/epsilon/gamma
Gene namesi
Name:Tmpo
Synonyms:Lap2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 10

Organism-specific databases

MGIiMGI:106920. Tmpo.

Subcellular locationi

Nucleus inner membrane; Single-pass type II membrane protein By similarity. Chromosome By similarity
Note: Tightly associated with the nuclear lamina By similarity.

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei410 – 43021Helical; Signal-anchor for type II membrane protein; Reviewed predictionAdd
BLAST
Topological domaini431 – 45222Lumenal Reviewed predictionAdd
BLAST

GO - Cellular componenti

  1. chromatin Source: MGI
  2. integral component of membrane Source: UniProtKB-KW
  3. nuclear envelope Source: MGI
  4. nuclear inner membrane Source: UniProtKB-SubCell
  5. nucleus Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Membrane, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 452452Lamina-associated polypeptide 2, isoforms beta/delta/epsilon/gammaPRO_0000206146Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei59 – 591Phosphoserine By similarity
Modified residuei66 – 661Phosphoserine2 Publications
Modified residuei67 – 671Phosphoserine2 Publications
Modified residuei74 – 741Phosphothreonine3 Publications
Modified residuei79 – 791Phosphoserine By similarity
Modified residuei153 – 1531Phosphothreonine By similarity
Modified residuei155 – 1551Phosphoserine By similarity
Modified residuei159 – 1591Phosphothreonine2 Publications
Modified residuei163 – 1631Phosphothreonine By similarity
Modified residuei176 – 1761Phosphoserine1 Publication
Modified residuei179 – 1791Phosphoserine; by PKC1 Publication
Modified residuei183 – 1831Phosphoserine By similarity
Modified residuei206 – 2061N6-acetyllysine1 Publication
Modified residuei210 – 2101Phosphothreonine By similarity
Modified residuei264 – 2641Phosphoserine By similarity
Modified residuei291 – 2911Phosphoserine By similarity
Modified residuei305 – 3051Phosphoserine By similarity
Modified residuei311 – 3111Phosphothreonine By similarity
Modified residuei314 – 3141Phosphoserine By similarity
Modified residuei319 – 3191Citrulline
Modified residuei361 – 3611Phosphoserine By similarity
Modified residuei384 – 3841Phosphoserine By similarity
Modified residuei388 – 3881N6-acetyllysine1 Publication

Post-translational modificationi

Mitosis-specific phosphorylation specifically abolishes its binding to lamin B and chromosomes By similarity.
Citrullinated by PADI4.

Keywords - PTMi

Acetylation, Citrullination, Phosphoprotein

Proteomic databases

PRIDEiQ61029.

Expressioni

Gene expression databases

ArrayExpressiQ61029.
BgeeiQ61029.
CleanExiMM_TMPO.
GenevestigatoriQ61029.

Interactioni

Subunit structurei

Interacts with LMNB1, LMNB2, BANF1, AKAP8L, GMCL and chromosomes By similarity.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Zbtb7bQ643212EBI-6172136,EBI-642868

Protein-protein interaction databases

BioGridi204234. 3 interactions.
IntActiQ61029. 3 interactions.
MINTiMINT-4109431.

Structurei

3D structure databases

ProteinModelPortaliQ61029.
SMRiQ61029. Positions 2-56, 102-158.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini5 – 4844LEM-likeAdd
BLAST
Domaini109 – 15345LEMAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 409409Nucleoplasmic Reviewed predictionAdd
BLAST
Regioni49 – 10860LinkerAdd
BLAST
Regioni137 – 242106NAKAP95-binding NAdd
BLAST
Regioni298 – 37073Binds lamins BAdd
BLAST
Regioni299 – 37375NAKAP95-binding CAdd
BLAST

Domaini

Has two structurally independent, non-interacting domains: LEM-like (also called LAP2-N or LEM-D) and LEM (also called LAP2-C or LEM-B). LEM-like binds DNA while LEM interacts with BANF1 By similarity.

Sequence similaritiesi

Belongs to the LEM family.
Contains 1 LEM domain.
Contains 1 LEM-like domain.

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

GeneTreeiENSGT00510000048934.
HOGENOMiHOG000113280.
HOVERGENiHBG000166.
OMAiTGNFKHA.

Family and domain databases

Gene3Di1.10.720.40. 2 hits.
InterProiIPR013146. LEM-like_dom.
IPR011015. LEM/LEM-like_dom.
IPR003887. LEM_dom.
[Graphical view]
PfamiPF03020. LEM. 1 hit.
PF08198. Thymopoietin. 1 hit.
[Graphical view]
SMARTiSM00540. LEM. 1 hit.
[Graphical view]
SUPFAMiSSF63451. SSF63451. 2 hits.
PROSITEiPS50954. LEM. 1 hit.
PS50955. LEM_LIKE. 1 hit.
[Graphical view]

Sequences (6)i

Sequence statusi: Complete.

This entry describes 6 isoformsi produced by alternative splicing. Align

Isoform Beta (identifier: Q61029-1) [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

MPEFLEDPSV LTKDKLKSEL VANNVTLPAG EQRKDVYVQL YLQHLTARNR    50
PPLAAGANSK GPPDFSSDEE REPTPVLGSG ASVGRGRGAV GRKATKKTDK 100
PRLEDKDDLD VTELSNEELL DQLVRYGVNP GPIVGTTRKL YEKKLLKLRE 150
QGTESRSSTP LPTVSSSAEN TRQNGSNDSD RYSDNDEDSK IELKLEKREP 200
LKGRAKTPVT LKQRRTEHNQ SYSQAGVTET EWTSGSSTGG PLQALTREST 250
RGSRRTPRKR VETSQHFRID GAVISESTPI AETIKASSNE SLVANRLTGN 300
FKHASSILPI TEFSDITRRT PKKPLTRAEV GEKTEERRVD RDILKEMFPY 350
EASTPTGISA SCRRPIKGAA GRPLELSDFR MEESFSSKYV PKYAPLADVK 400
SEKTKKRRSV PMWIKMLLFA LVAVFLFLVY QAMETNQGNP FTNFLQDTKI 450
SN 452
Length:452
Mass (Da):50,373
Last modified:July 27, 2011 - v4
Checksum:i132AF11B458DCFBA
GO
Isoform Alpha (identifier: Q61033-1) [UniParc]FASTAAdd to Basket

The sequence of this isoform can be found in the external entry Q61033.
Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.
Length:693
Mass (Da):75,168
GO
Isoform Zeta (identifier: Q61033-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform can be found in the external entry Q61033.
Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.

Note: Contains a N6-acetyllysine at position 206.

Length:225
Mass (Da):24,990
GO
Isoform Delta (identifier: Q61029-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     221-292: Missing.

Show »
Length:380
Mass (Da):42,650
Checksum:iF2BE6B5556030A49
GO
Isoform Epsilon (identifier: Q61029-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     221-260: Missing.

Show »
Length:412
Mass (Da):46,050
Checksum:iC54639DAB8788CEE
GO
Isoform Gamma (identifier: Q61029-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     221-329: Missing.

Show »
Length:343
Mass (Da):38,502
Checksum:iBA62B6D869B0FDAD
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei221 – 329109Missing in isoform Gamma. VSP_010132Add
BLAST
Alternative sequencei221 – 29272Missing in isoform Delta. VSP_010131Add
BLAST
Alternative sequencei221 – 26040Missing in isoform Epsilon. VSP_010130Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti72 – 732EP → DA in AAC52574. 1 Publication
Sequence conflicti72 – 732EP → DA in AAC52575. 1 Publication
Sequence conflicti72 – 732EP → DA in AAC52576. 1 Publication
Sequence conflicti72 – 732EP → DA in AAC52577. 1 Publication
Sequence conflicti422 – 4243VAV → GAC in AAC52574. 1 Publication
Sequence conflicti422 – 4243VAV → GAC in AAC52575. 1 Publication
Sequence conflicti422 – 4243VAV → GAC in AAC52576. 1 Publication
Sequence conflicti422 – 4243VAV → GAC in AAC52577. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U39074 mRNA. Translation: AAC52574.1.
U39075 mRNA. Translation: AAC52575.1.
U39076 mRNA. Translation: AAC52576.1.
U39077 mRNA. Translation: AAC52577.1.
AK150305 mRNA. Translation: BAE29455.1.
AK150515 mRNA. Translation: BAE29627.1.
AK153281 mRNA. Translation: BAE31865.1.
AK165851 mRNA. Translation: BAE38413.1.
CH466539 Genomic DNA. Translation: EDL21533.1.
CCDSiCCDS36032.1. [Q61029-4]
CCDS36033.1. [Q61029-2]
CCDS36034.1. [Q61029-3]
CCDS36035.1. [Q61029-1]
RefSeqiNP_001073598.1. NM_001080129.2. [Q61029-1]
NP_001073600.1. NM_001080131.2. [Q61029-2]
NP_001073601.1. NM_001080132.2. [Q61029-4]
UniGeneiMm.159684.
Mm.439157.

Genome annotation databases

EnsembliENSMUST00000072239; ENSMUSP00000072092; ENSMUSG00000019961. [Q61029-1]
ENSMUST00000092219; ENSMUSP00000089864; ENSMUSG00000019961. [Q61029-3]
ENSMUST00000099355; ENSMUSP00000096956; ENSMUSG00000019961. [Q61029-2]
ENSMUST00000105293; ENSMUSP00000100930; ENSMUSG00000019961. [Q61029-4]
GeneIDi21917.
KEGGimmu:21917.
UCSCiuc007gtq.1. mouse. [Q61029-1]
uc007gts.1. mouse. [Q61029-2]
uc007gtt.1. mouse. [Q61029-4]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U39074 mRNA. Translation: AAC52574.1 .
U39075 mRNA. Translation: AAC52575.1 .
U39076 mRNA. Translation: AAC52576.1 .
U39077 mRNA. Translation: AAC52577.1 .
AK150305 mRNA. Translation: BAE29455.1 .
AK150515 mRNA. Translation: BAE29627.1 .
AK153281 mRNA. Translation: BAE31865.1 .
AK165851 mRNA. Translation: BAE38413.1 .
CH466539 Genomic DNA. Translation: EDL21533.1 .
CCDSi CCDS36032.1. [Q61029-4 ]
CCDS36033.1. [Q61029-2 ]
CCDS36034.1. [Q61029-3 ]
CCDS36035.1. [Q61029-1 ]
RefSeqi NP_001073598.1. NM_001080129.2. [Q61029-1 ]
NP_001073600.1. NM_001080131.2. [Q61029-2 ]
NP_001073601.1. NM_001080132.2. [Q61029-4 ]
UniGenei Mm.159684.
Mm.439157.

3D structure databases

ProteinModelPortali Q61029.
SMRi Q61029. Positions 2-56, 102-158.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 204234. 3 interactions.
IntActi Q61029. 3 interactions.
MINTi MINT-4109431.

Proteomic databases

PRIDEi Q61029.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000072239 ; ENSMUSP00000072092 ; ENSMUSG00000019961 . [Q61029-1 ]
ENSMUST00000092219 ; ENSMUSP00000089864 ; ENSMUSG00000019961 . [Q61029-3 ]
ENSMUST00000099355 ; ENSMUSP00000096956 ; ENSMUSG00000019961 . [Q61029-2 ]
ENSMUST00000105293 ; ENSMUSP00000100930 ; ENSMUSG00000019961 . [Q61029-4 ]
GeneIDi 21917.
KEGGi mmu:21917.
UCSCi uc007gtq.1. mouse. [Q61029-1 ]
uc007gts.1. mouse. [Q61029-2 ]
uc007gtt.1. mouse. [Q61029-4 ]

Organism-specific databases

CTDi 7112.
MGIi MGI:106920. Tmpo.

Phylogenomic databases

GeneTreei ENSGT00510000048934.
HOGENOMi HOG000113280.
HOVERGENi HBG000166.
OMAi TGNFKHA.

Miscellaneous databases

ChiTaRSi TMPO. mouse.
NextBioi 301476.
PROi Q61029.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q61029.
Bgeei Q61029.
CleanExi MM_TMPO.
Genevestigatori Q61029.

Family and domain databases

Gene3Di 1.10.720.40. 2 hits.
InterProi IPR013146. LEM-like_dom.
IPR011015. LEM/LEM-like_dom.
IPR003887. LEM_dom.
[Graphical view ]
Pfami PF03020. LEM. 1 hit.
PF08198. Thymopoietin. 1 hit.
[Graphical view ]
SMARTi SM00540. LEM. 1 hit.
[Graphical view ]
SUPFAMi SSF63451. SSF63451. 2 hits.
PROSITEi PS50954. LEM. 1 hit.
PS50955. LEM_LIKE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "The characterization and localization of the mouse thymopoietin/lamina-associated polypeptide 2 gene and its alternatively spliced products."
    Berger R., Theodor L., Shoham J., Gokkel E., Brok-Simoni F., Avraham K.B., Copeland N.G., Jenkins N.A., Rechavi G., Simon A.J.
    Genome Res. 6:361-370(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS ALPHA; BETA; GAMMA; DELTA; EPSILON AND ZETA).
    Strain: C57BL/6 X DBA/2.
    Tissue: Thymus.
  2. "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.
    Tissue: Bone marrow and Lung.
  3. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "Identification of phosphorylation sites in native lamina-associated polypeptide 2 beta."
    Dreger M., Otto H., Neubauer G., Mann M., Hucho F.
    Biochemistry 38:9426-9434(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 61-85 AND 173-194 (ISOFORM BETA), PHOSPHORYLATION AT THR-74; THR-159; SER-176 AND SER-179, IDENTIFICATION BY MASS SPECTROMETRY.
  5. "LAP2 binding protein 1 (L2BP1/BAF) is a candidate mediator of LAP2-chromatin interaction."
    Furukawa K.
    J. Cell Sci. 112:2485-2492(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH BANF1.
  6. "Nuclear membrane protein LAP2beta mediates transcriptional repression alone and together with its binding partner GCL (germ-cell-less)."
    Nili E., Cojocaru G.S., Kalma Y., Ginsberg D., Copeland N.G., Gilbert D.J., Jenkins N.A., Berger R., Shaklai S., Amariglio N., Brok-Simoni F., Simon A.J., Rechavi G.
    J. Cell Sci. 114:3297-3307(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH GMCL.
  7. "Comprehensive identification of phosphorylation sites in postsynaptic density preparations."
    Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.
    Mol. Cell. Proteomics 5:914-922(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain.
  8. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-66; SER-67; THR-74 AND THR-159, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
    Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
    Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-66; SER-67 AND THR-74, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.
  11. Cited for: CITRULLINATION AT ARG-319.
  12. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-206 AND LYS-388, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.

Entry informationi

Entry nameiLAP2B_MOUSE
AccessioniPrimary (citable) accession number: Q61029
Secondary accession number(s): Q3UCI5
, Q61030, Q61031, Q61032
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 26, 2004
Last sequence update: July 27, 2011
Last modified: July 9, 2014
This is version 124 of the entry and version 4 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
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi