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Protein

Tight junction protein ZO-3

Gene

TJP3

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

Functioni

GO - Biological processi

Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
Tight junction protein ZO-3
Alternative name(s):
Tight junction protein 3
Zona occludens protein 3
Zonula occludens protein 3
Gene namesi
Name:TJP3
Synonyms:ZO3
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 19

Organism-specific databases

HGNCiHGNC:11829. TJP3.

Subcellular locationi

GO - Cellular componenti

  • apical plasma membrane Source: Ensembl
  • cell junction Source: HPA
  • nucleoplasm Source: HPA
  • nucleus Source: UniProtKB
  • tight junction Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Membrane, Tight junction

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA36534.

Polymorphism and mutation databases

BioMutaiTJP3.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 919919Tight junction protein ZO-3PRO_0000094546Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei136 – 1361Phosphoserine1 Publication
Modified residuei164 – 1641Phosphoserine4 Publications
Modified residuei169 – 1691PhosphoserineBy similarity
Modified residuei319 – 3191Phosphoserine1 Publication
Modified residuei325 – 3251Phosphothreonine1 Publication
Modified residuei327 – 3271Phosphoserine1 Publication
Modified residuei371 – 3711Phosphoserine1 Publication
Modified residuei591 – 5911Phosphoserine1 Publication
Modified residuei905 – 9051Phosphoserine2 Publications
Modified residuei906 – 9061Phosphoserine3 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiO95049.
PaxDbiO95049.
PRIDEiO95049.

PTM databases

PhosphoSiteiO95049.

Expressioni

Gene expression databases

BgeeiO95049.
CleanExiHS_TJP3.
ExpressionAtlasiO95049. baseline and differential.
GenevestigatoriO95049.

Organism-specific databases

HPAiCAB013244.
HPA053337.

Interactioni

Subunit structurei

Interacts with occludin, claudins and ZO-1. Interacts with INADL (By similarity). Interacts with UBN1. Interacts with FASLG.By similarity2 Publications

Protein-protein interaction databases

BioGridi118025. 5 interactions.
IntActiO95049. 2 interactions.
MINTiMINT-210473.
STRINGi9606.ENSP00000262968.

Structurei

Secondary structure

1
919
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi478 – 4825Combined sources
Beta strandi490 – 4934Combined sources
Beta strandi501 – 5066Combined sources
Beta strandi522 – 5276Combined sources
Beta strandi533 – 5397Combined sources
Helixi542 – 55514Combined sources
Helixi596 – 6027Combined sources
Beta strandi606 – 6149Combined sources
Beta strandi621 – 6255Combined sources
Helixi628 – 63811Combined sources
Turni640 – 6423Combined sources
Beta strandi643 – 6453Combined sources
Helixi661 – 6699Combined sources
Beta strandi673 – 6764Combined sources
Helixi680 – 6889Combined sources
Beta strandi694 – 7018Combined sources
Helixi703 – 71311Combined sources
Helixi721 – 73515Combined sources
Helixi736 – 7383Combined sources
Beta strandi740 – 7456Combined sources
Beta strandi747 – 7493Combined sources
Helixi751 – 76313Combined sources
Beta strandi766 – 7716Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3KFVX-ray2.80A475-775[»]
ProteinModelPortaliO95049.
SMRiO95049. Positions 6-93, 196-271, 379-772.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO95049.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini11 – 9383PDZ 1PROSITE-ProRule annotationAdd
BLAST
Domaini195 – 27278PDZ 2PROSITE-ProRule annotationAdd
BLAST
Domaini380 – 44667PDZ 3PROSITE-ProRule annotationAdd
BLAST
Domaini475 – 54975SH3PROSITE-ProRule annotationAdd
BLAST
Domaini580 – 761182Guanylate kinase-likePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the MAGUK family.Curated
Contains 1 guanylate kinase-like domain.PROSITE-ProRule annotation
Contains 3 PDZ (DHR) domains.PROSITE-ProRule annotation
Contains 1 SH3 domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, SH3 domain

Phylogenomic databases

eggNOGiNOG239704.
GeneTreeiENSGT00640000091263.
HOGENOMiHOG000230923.
HOVERGENiHBG017627.
InParanoidiO95049.
KOiK06097.
OrthoDBiEOG7T1RB4.
TreeFamiTF315606.

Family and domain databases

Gene3Di2.30.42.10. 3 hits.
3.40.50.300. 1 hit.
InterProiIPR008145. GK/Ca_channel_bsu.
IPR008144. Guanylate_kin-like.
IPR027417. P-loop_NTPase.
IPR001478. PDZ.
IPR011511. SH3_2.
IPR001452. SH3_domain.
IPR005417. ZO.
IPR005420. ZO-3.
[Graphical view]
PANTHERiPTHR13865:SF11. PTHR13865:SF11. 1 hit.
PfamiPF00625. Guanylate_kin. 1 hit.
PF00595. PDZ. 3 hits.
PF07653. SH3_2. 1 hit.
[Graphical view]
PRINTSiPR01597. ZONOCCLUDNS.
PR01600. ZONOCCLUDNS3.
SMARTiSM00072. GuKc. 1 hit.
SM00228. PDZ. 3 hits.
SM00326. SH3. 1 hit.
[Graphical view]
SUPFAMiSSF50044. SSF50044. 1 hit.
SSF50156. SSF50156. 3 hits.
SSF52540. SSF52540. 1 hit.
PROSITEiPS50052. GUANYLATE_KINASE_2. 1 hit.
PS50106. PDZ. 3 hits.
PS50002. SH3. 1 hit.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 5 (identifier: O95049-1) [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
MEELTIWEQH TATLSKDPRR GFGIAISGGR DRPGGSMVVS DVVPGGPAEG
60 70 80 90 100
RLQTGDHIVM VNGVSMENAT SAFAIQILKT CTKMANITVK RPRRIHLPAT
110 120 130 140 150
KASPSSPGRQ DSDEDDGPQR VEEVDQGRGY DGDSSSGSGR SWDERSRRPR
160 170 180 190 200
PGRRGRAGSH GRRSPGGGSE ANGLALVSGF KRLPRQDVQM KPVKSVLVKR
210 220 230 240 250
RDSEEFGVKL GSQIFIKHIT DSGLAARHRG LQEGDLILQI NGVSSQNLSL
260 270 280 290 300
NDTRRLIEKS EGKLSLLVLR DRGQFLVNIP PAVSDSDSSP LEDISDLASE
310 320 330 340 350
LSQAPPSHIP PPPRHAQRSP EASQTDSPVE SPRLRRESSV DSRTISEPDE
360 370 380 390 400
QRSELPRESS YDIYRVPSSQ SMEDRGYSPD TRVVRFLKGK SIGLRLAGGN
410 420 430 440 450
DVGIFVSGVQ AGSPADGQGI QEGDQILQVN DVPFQNLTRE EAVQFLLGLP
460 470 480 490 500
PGEEMELVTQ RKQDIFWKMV QSRVGDSFYI RTHFELEPSP PSGLGFTRGD
510 520 530 540 550
VFHVLDTLHP GPGQSHARGG HWLAVRMGRD LREQERGIIP NQSRAEQLAS
560 570 580 590 600
LEAAQRAVGV GPGSSAGSNA RAEFWRLRGL RRGAKKTTQR SREDLSALTR
610 620 630 640 650
QGRYPPYERV VLREASFKRP VVILGPVADI AMQKLTAEMP DQFEIAETVS
660 670 680 690 700
RTDSPSKIIK LDTVRVIAEK DKHALLDVTP SAIERLNYVQ YYPIVVFFIP
710 720 730 740 750
ESRPALKALR QWLAPASRRS TRRLYAQAQK LRKHSSHLFT ATIPLNGTSD
760 770 780 790 800
TWYQELKAII REQQTRPIWT AEDQLDGSLE DNLDLPHHGL ADSSADLSCD
810 820 830 840 850
SRVNSDYETD GEGGAYTDGE GYTDGEGGPY TDVDDEPPAP ALARSSEPVQ
860 870 880 890 900
ADESQSPRDR GRISAHQGAQ VDSRHPQGQW RQDSMRTYER EALKKKFMRV
910
HDAESSDEDG YDWGPATDL
Length:919
Mass (Da):101,397
Last modified:March 19, 2014 - v3
Checksum:iD36EB684E7E4A6C8
GO
Isoform 3 (identifier: O95049-3) [UniParc]FASTAAdd to basket

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

Note: No experimental confirmation available.

Show »
Length:938
Mass (Da):103,424
Checksum:i603411581EB7FA85
GO
Isoform 4 (identifier: O95049-4) [UniParc]FASTAAdd to basket

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

Show »
Length:928
Mass (Da):102,415
Checksum:iB418537346F205CF
GO
Isoform 6 (identifier: O95049-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-36: Missing.

Show »
Length:883
Mass (Da):97,488
Checksum:i511564BFC624B3A8
GO

Sequence cautioni

The sequence AAC72274.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence EAW69293.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti19 – 191R → H in AAI08907 (PubMed:15489334).Curated
Sequence conflicti96 – 961H → L in BAG52285 (PubMed:14702039).Curated
Sequence conflicti449 – 4491L → P in BAG54652 (PubMed:14702039).Curated
Sequence conflicti802 – 8021R → H in BAG52285 (PubMed:14702039).Curated
Sequence conflicti901 – 9011H → R in BAG52285 (PubMed:14702039).Curated
Sequence conflicti917 – 9171T → M in BAG65278 (PubMed:14702039).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti898 – 8981M → T.1 Publication
Corresponds to variant rs1046268 [ dbSNP | Ensembl ].
VAR_056114

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 3636Missing in isoform 6. 1 PublicationVSP_053844Add
BLAST
Alternative sequencei1 – 11M → MNLCGLMPIFPAPLDQVADM in isoform 3. 1 PublicationVSP_040238
Alternative sequencei1 – 11M → MAVRFQVADM in isoform 4. 1 PublicationVSP_047022

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK091118 mRNA. Translation: BAG52285.1.
AK128237 mRNA. Translation: BAG54652.1.
AK304462 mRNA. Translation: BAG65278.1.
AC005954 Genomic DNA. Translation: AAC72274.1. Sequence problems.
AC006125 Genomic DNA. No translation available.
CH471139 Genomic DNA. Translation: EAW69293.1. Sequence problems.
BC108906 mRNA. Translation: AAI08907.1.
CCDSiCCDS32873.2. [O95049-1]
CCDS59332.1. [O95049-4]
RefSeqiNP_001254489.1. NM_001267560.1. [O95049-1]
NP_001254490.1. NM_001267561.1. [O95049-4]
UniGeneiHs.25527.

Genome annotation databases

EnsembliENST00000539908; ENSP00000439991; ENSG00000105289. [O95049-5]
ENST00000541714; ENSP00000439278; ENSG00000105289. [O95049-1]
ENST00000587686; ENSP00000467864; ENSG00000105289. [O95049-3]
ENST00000589378; ENSP00000465419; ENSG00000105289. [O95049-4]
GeneIDi27134.
KEGGihsa:27134.
UCSCiuc010xhu.3. human. [O95049-3]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK091118 mRNA. Translation: BAG52285.1.
AK128237 mRNA. Translation: BAG54652.1.
AK304462 mRNA. Translation: BAG65278.1.
AC005954 Genomic DNA. Translation: AAC72274.1. Sequence problems.
AC006125 Genomic DNA. No translation available.
CH471139 Genomic DNA. Translation: EAW69293.1. Sequence problems.
BC108906 mRNA. Translation: AAI08907.1.
CCDSiCCDS32873.2. [O95049-1]
CCDS59332.1. [O95049-4]
RefSeqiNP_001254489.1. NM_001267560.1. [O95049-1]
NP_001254490.1. NM_001267561.1. [O95049-4]
UniGeneiHs.25527.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3KFVX-ray2.80A475-775[»]
ProteinModelPortaliO95049.
SMRiO95049. Positions 6-93, 196-271, 379-772.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi118025. 5 interactions.
IntActiO95049. 2 interactions.
MINTiMINT-210473.
STRINGi9606.ENSP00000262968.

PTM databases

PhosphoSiteiO95049.

Polymorphism and mutation databases

BioMutaiTJP3.

Proteomic databases

MaxQBiO95049.
PaxDbiO95049.
PRIDEiO95049.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000539908; ENSP00000439991; ENSG00000105289. [O95049-5]
ENST00000541714; ENSP00000439278; ENSG00000105289. [O95049-1]
ENST00000587686; ENSP00000467864; ENSG00000105289. [O95049-3]
ENST00000589378; ENSP00000465419; ENSG00000105289. [O95049-4]
GeneIDi27134.
KEGGihsa:27134.
UCSCiuc010xhu.3. human. [O95049-3]

Organism-specific databases

CTDi27134.
GeneCardsiGC19P003708.
H-InvDBHIX0014645.
HGNCiHGNC:11829. TJP3.
HPAiCAB013244.
HPA053337.
MIMi612689. gene.
neXtProtiNX_O95049.
PharmGKBiPA36534.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG239704.
GeneTreeiENSGT00640000091263.
HOGENOMiHOG000230923.
HOVERGENiHBG017627.
InParanoidiO95049.
KOiK06097.
OrthoDBiEOG7T1RB4.
TreeFamiTF315606.

Miscellaneous databases

EvolutionaryTraceiO95049.
GeneWikiiTJP3.
GenomeRNAii27134.
NextBioi13603241.
PROiO95049.
SOURCEiSearch...

Gene expression databases

BgeeiO95049.
CleanExiHS_TJP3.
ExpressionAtlasiO95049. baseline and differential.
GenevestigatoriO95049.

Family and domain databases

Gene3Di2.30.42.10. 3 hits.
3.40.50.300. 1 hit.
InterProiIPR008145. GK/Ca_channel_bsu.
IPR008144. Guanylate_kin-like.
IPR027417. P-loop_NTPase.
IPR001478. PDZ.
IPR011511. SH3_2.
IPR001452. SH3_domain.
IPR005417. ZO.
IPR005420. ZO-3.
[Graphical view]
PANTHERiPTHR13865:SF11. PTHR13865:SF11. 1 hit.
PfamiPF00625. Guanylate_kin. 1 hit.
PF00595. PDZ. 3 hits.
PF07653. SH3_2. 1 hit.
[Graphical view]
PRINTSiPR01597. ZONOCCLUDNS.
PR01600. ZONOCCLUDNS3.
SMARTiSM00072. GuKc. 1 hit.
SM00228. PDZ. 3 hits.
SM00326. SH3. 1 hit.
[Graphical view]
SUPFAMiSSF50044. SSF50044. 1 hit.
SSF50156. SSF50156. 3 hits.
SSF52540. SSF52540. 1 hit.
PROSITEiPS50052. GUANYLATE_KINASE_2. 1 hit.
PS50106. PDZ. 3 hits.
PS50002. SH3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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] (ISOFORMS 4; 5 AND 6).
    Tissue: Stomach, Testis and Tongue.
  2. "The DNA sequence and biology of human chromosome 19."
    Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V.
    , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
    Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "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 3), VARIANT THR-898.
  5. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-164; SER-905 AND SER-906, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  6. "Identification of SH3 domain interaction partners of human FasL (CD178) by phage display screening."
    Voss M., Lettau M., Janssen O.
    BMC Immunol. 10:53-53(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH FASLG.
  7. "Characterization of the ubinuclein protein as a new member of the nuclear and adhesion complex components (NACos)."
    Aho S., Lupo J., Coly P.-A., Sabine A., Castellazzi M., Morand P., Sergeant A., Manet E., Boyer V., Gruffat H.
    Biol. Cell 101:319-334(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH UBN1.
  8. "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-164, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  9. "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-164; SER-905 AND SER-906, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. "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-164, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-136; SER-319; THR-325; SER-327; SER-371; SER-591 AND SER-906, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  12. "Crystal structure of the SH3-kinase fragment of tight junction protein 3 (TJP3) in apo-form."
    Structural genomics consortium (SGC)
    Submitted (NOV-2009) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 475-775.

Entry informationi

Entry nameiZO3_HUMAN
AccessioniPrimary (citable) accession number: O95049
Secondary accession number(s): A6NFP3
, B3KR73, B3KXZ0, B4E2W6, F5H2X0, F5H4S9, K7EK22, Q32N01
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 11, 2001
Last sequence update: March 19, 2014
Last modified: April 29, 2015
This is version 131 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, Reference proteome

Documents

  1. Human chromosome 19
    Human chromosome 19: 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.