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Protein

Transgelin-2

Gene

TAGLN2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

GO - Biological processi

  • epithelial cell differentiation Source: UniProtKB
Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
Transgelin-2
Alternative name(s):
Epididymis tissue protein Li 7e
SM22-alpha homolog
Gene namesi
Name:TAGLN2
Synonyms:KIAA0120
ORF Names:CDABP0035
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:11554. TAGLN2.

Subcellular locationi

GO - Cellular componenti

  • extracellular exosome Source: UniProtKB
  • vesicle Source: UniProtKB
Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA36325.

Polymorphism and mutation databases

DMDMi586000.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed2 Publications
Chaini2 – 199198Transgelin-2PRO_0000204786Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine2 Publications
Modified residuei17 – 171N6-acetyllysine1 Publication
Modified residuei20 – 201N6-acetyllysine1 Publication
Modified residuei163 – 1631Phosphoserine4 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP37802.
PaxDbiP37802.
PRIDEiP37802.

2D gel databases

DOSAC-COBS-2DPAGEP37802.
OGPiP37802.
REPRODUCTION-2DPAGEP37802.

PTM databases

PhosphoSiteiP37802.

Expressioni

Tissue specificityi

Expressed in epididymis (at protein level).1 Publication

Gene expression databases

BgeeiP37802.
CleanExiHS_TAGLN2.
ExpressionAtlasiP37802. baseline and differential.
GenevisibleiP37802. HS.

Organism-specific databases

HPAiHPA001925.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
ACTBP607093EBI-1056740,EBI-353944

Protein-protein interaction databases

BioGridi113995. 36 interactions.
IntActiP37802. 12 interactions.
MINTiMINT-5001664.
STRINGi9606.ENSP00000357075.

Structurei

Secondary structure

1
199
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi24 – 3714Combined sources
Beta strandi38 – 403Combined sources
Helixi49 – 579Combined sources
Helixi60 – 6910Combined sources
Turni72 – 743Combined sources
Helixi86 – 10318Combined sources
Turni107 – 1093Combined sources
Helixi113 – 1175Combined sources
Helixi122 – 13615Combined sources
Beta strandi140 – 1423Combined sources
Beta strandi148 – 1514Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1WYMNMR-A16-157[»]
ProteinModelPortaliP37802.
SMRiP37802. Positions 9-158.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP37802.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini24 – 136113CHPROSITE-ProRule annotationAdd
BLAST
Repeati174 – 19926Calponin-likeAdd
BLAST

Sequence similaritiesi

Belongs to the calponin family.Curated
Contains 1 calponin-like repeat.PROSITE-ProRule annotation
Contains 1 CH (calponin-homology) domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG5199.
GeneTreeiENSGT00550000074447.
HOGENOMiHOG000232113.
HOVERGENiHBG005186.
InParanoidiP37802.
OMAiFRMANRG.
OrthoDBiEOG718KD9.
PhylomeDBiP37802.
TreeFamiTF313921.

Family and domain databases

Gene3Di1.10.418.10. 1 hit.
InterProiIPR000557. Calponin_repeat.
IPR001715. CH-domain.
IPR003096. SM22_calponin.
IPR001061. TAGLN2.
[Graphical view]
PANTHERiPTHR18959:SF44. PTHR18959:SF44. 1 hit.
PfamiPF00402. Calponin. 1 hit.
PF00307. CH. 1 hit.
[Graphical view]
PRINTSiPR00888. SM22CALPONIN.
SMARTiSM00033. CH. 1 hit.
[Graphical view]
SUPFAMiSSF47576. SSF47576. 1 hit.
PROSITEiPS01052. CALPONIN_1. 1 hit.
PS51122. CALPONIN_2. 1 hit.
PS50021. CH. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P37802-1) [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
MANRGPAYGL SREVQQKIEK QYDADLEQIL IQWITTQCRK DVGRPQPGRE
60 70 80 90 100
NFQNWLKDGT VLCELINALY PEGQAPVKKI QASTMAFKQM EQISQFLQAA
110 120 130 140 150
ERYGINTTDI FQTVDLWEGK NMACVQRTLM NLGGLAVARD DGLFSGDPNW
160 170 180 190
FPKKSKENPR NFSDNQLQEG KNVIGLQMGT NRGASQAGMT GYGMPRQIL
Length:199
Mass (Da):22,391
Last modified:January 23, 2007 - v3
Checksum:i07DFC1652CE2383D
GO
Isoform 2 (identifier: P37802-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MSAFSLALALVSSPQPPPPIGM

Note: No experimental confirmation available.
Show »
Length:220
Mass (Da):24,454
Checksum:iDD4502C038B8D6F6
GO

Sequence cautioni

The sequence BAA04802.2 differs from that shown. Reason: Erroneous initiation. Curated
The sequence CAI14604.1 differs from that shown. Reason: Erroneous initiation. Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti69 – 691L → Q.1 Publication
Corresponds to variant rs17849636 [ dbSNP | Ensembl ].
VAR_047903

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 11M → MSAFSLALALVSSPQPPPPI GM in isoform 2. 1 PublicationVSP_055311

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY007127 mRNA. Translation: AAG01993.1.
D21261 mRNA. Translation: BAA04802.2. Different initiation.
GU727636 mRNA. Translation: ADU87638.1.
AK291562 mRNA. Translation: BAF84251.1.
CR542126 mRNA. Translation: CAG46923.1.
CR542136 mRNA. Translation: CAG46933.1.
AL513485 Genomic DNA. Translation: CAI14603.1.
AL513485 Genomic DNA. Translation: CAI14604.1. Different initiation.
AL513485 Genomic DNA. Translation: CAI14602.1.
CH471121 Genomic DNA. Translation: EAW52760.1.
BC002616 mRNA. Translation: AAH02616.1.
BC009357 mRNA. Translation: AAH09357.1.
CCDSiCCDS1189.1. [P37802-1]
CCDS60314.1. [P37802-2]
RefSeqiNP_001264152.1. NM_001277223.1. [P37802-1]
NP_001264153.1. NM_001277224.1. [P37802-2]
NP_003555.1. NM_003564.2. [P37802-1]
UniGeneiHs.517168.

Genome annotation databases

EnsembliENST00000320307; ENSP00000357075; ENSG00000158710. [P37802-1]
ENST00000368096; ENSP00000357076; ENSG00000158710. [P37802-2]
ENST00000368097; ENSP00000357077; ENSG00000158710. [P37802-1]
GeneIDi8407.
KEGGihsa:8407.
UCSCiuc001fun.2. human. [P37802-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY007127 mRNA. Translation: AAG01993.1.
D21261 mRNA. Translation: BAA04802.2. Different initiation.
GU727636 mRNA. Translation: ADU87638.1.
AK291562 mRNA. Translation: BAF84251.1.
CR542126 mRNA. Translation: CAG46923.1.
CR542136 mRNA. Translation: CAG46933.1.
AL513485 Genomic DNA. Translation: CAI14603.1.
AL513485 Genomic DNA. Translation: CAI14604.1. Different initiation.
AL513485 Genomic DNA. Translation: CAI14602.1.
CH471121 Genomic DNA. Translation: EAW52760.1.
BC002616 mRNA. Translation: AAH02616.1.
BC009357 mRNA. Translation: AAH09357.1.
CCDSiCCDS1189.1. [P37802-1]
CCDS60314.1. [P37802-2]
RefSeqiNP_001264152.1. NM_001277223.1. [P37802-1]
NP_001264153.1. NM_001277224.1. [P37802-2]
NP_003555.1. NM_003564.2. [P37802-1]
UniGeneiHs.517168.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1WYMNMR-A16-157[»]
ProteinModelPortaliP37802.
SMRiP37802. Positions 9-158.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi113995. 36 interactions.
IntActiP37802. 12 interactions.
MINTiMINT-5001664.
STRINGi9606.ENSP00000357075.

PTM databases

PhosphoSiteiP37802.

Polymorphism and mutation databases

DMDMi586000.

2D gel databases

DOSAC-COBS-2DPAGEP37802.
OGPiP37802.
REPRODUCTION-2DPAGEP37802.

Proteomic databases

MaxQBiP37802.
PaxDbiP37802.
PRIDEiP37802.

Protocols and materials databases

DNASUi8407.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000320307; ENSP00000357075; ENSG00000158710. [P37802-1]
ENST00000368096; ENSP00000357076; ENSG00000158710. [P37802-2]
ENST00000368097; ENSP00000357077; ENSG00000158710. [P37802-1]
GeneIDi8407.
KEGGihsa:8407.
UCSCiuc001fun.2. human. [P37802-1]

Organism-specific databases

CTDi8407.
GeneCardsiGC01M159887.
HGNCiHGNC:11554. TAGLN2.
HPAiHPA001925.
MIMi604634. gene.
neXtProtiNX_P37802.
PharmGKBiPA36325.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG5199.
GeneTreeiENSGT00550000074447.
HOGENOMiHOG000232113.
HOVERGENiHBG005186.
InParanoidiP37802.
OMAiFRMANRG.
OrthoDBiEOG718KD9.
PhylomeDBiP37802.
TreeFamiTF313921.

Miscellaneous databases

ChiTaRSiTAGLN2. human.
EvolutionaryTraceiP37802.
GeneWikiiTAGLN2.
GenomeRNAii8407.
NextBioi31472.
PROiP37802.
SOURCEiSearch...

Gene expression databases

BgeeiP37802.
CleanExiHS_TAGLN2.
ExpressionAtlasiP37802. baseline and differential.
GenevisibleiP37802. HS.

Family and domain databases

Gene3Di1.10.418.10. 1 hit.
InterProiIPR000557. Calponin_repeat.
IPR001715. CH-domain.
IPR003096. SM22_calponin.
IPR001061. TAGLN2.
[Graphical view]
PANTHERiPTHR18959:SF44. PTHR18959:SF44. 1 hit.
PfamiPF00402. Calponin. 1 hit.
PF00307. CH. 1 hit.
[Graphical view]
PRINTSiPR00888. SM22CALPONIN.
SMARTiSM00033. CH. 1 hit.
[Graphical view]
SUPFAMiSSF47576. SSF47576. 1 hit.
PROSITEiPS01052. CALPONIN_1. 1 hit.
PS51122. CALPONIN_2. 1 hit.
PS50021. CH. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Pediatric leukemia cDNA sequencing project."
    Zhou J., Yu W., Tang H., Mei G., Tsang Y.T.M., Bouck J., Gibbs R.A., Margolin J.F.
    Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Leukemia.
  2. "Prediction of the coding sequences of unidentified human genes. III. The coding sequences of 40 new genes (KIAA0081-KIAA0120) deduced by analysis of cDNA clones from human cell line KG-1."
    Nagase T., Miyajima N., Tanaka A., Sazuka T., Seki N., Sato S., Tabata S., Ishikawa K., Kawarabayasi Y., Kotani H., Nomura N.
    DNA Res. 2:37-43(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Bone marrow.
  3. "Systematic mapping and functional analysis of a family of human epididymal secretory sperm-located proteins."
    Li J., Liu F., Wang H., Liu X., Liu J., Li N., Wan F., Wang W., Zhang C., Jin S., Liu J., Zhu P., Liu Y.
    Mol. Cell. Proteomics 9:2517-2528(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
    Tissue: Epididymis.
  4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Placenta.
  5. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
    Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y., LaBaer J.
    Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  6. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. "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 1), VARIANT GLN-69.
    Tissue: Lymph and Uterus.
  9. "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides."
    Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J.
    Nat. Biotechnol. 21:566-569(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-12 (ISOFORMS 1/2).
    Tissue: Platelet.
  10. Bienvenut W.V., Claeys D.
    Submitted (FEB-2006) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 2-12; 41-57; 79-154 AND 161-196 (ISOFORMS 1/2), CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Platelet.
  11. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-163, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Platelet.
  12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  14. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-163, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  15. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-17 AND LYS-20, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-163, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  17. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  18. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-163, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  19. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  20. "Solution structure of the CH domain of human transgelin-2."
    RIKEN structural genomics initiative (RSGI)
    Submitted (AUG-2005) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 16-157.

Entry informationi

Entry nameiTAGL2_HUMAN
AccessioniPrimary (citable) accession number: P37802
Secondary accession number(s): E9KL39
, Q5JRQ6, Q5JRQ7, Q6FGI1, Q9BUH5, Q9H4P0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: January 23, 2007
Last modified: June 24, 2015
This is version 157 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.