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Protein

E3 ubiquitin-protein ligase Praja-1

Gene

PJA1

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

Functioni

Has E2-dependent E3 ubiquitin-protein ligase activity. Ubiquitinates MAGED1 antigen leading to its subsequent degradation by proteasome (By similarity). May be involved in protein sorting.By similarity1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri595 – 63642RING-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  1. ligase activity Source: UniProtKB-KW
  2. ubiquitin-protein transferase activity Source: Ensembl
  3. zinc ion binding Source: InterPro

GO - Biological processi

  1. protein catabolic process Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Ubl conjugation pathway

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.

Names & Taxonomyi

Protein namesi
Recommended name:
E3 ubiquitin-protein ligase Praja-1 (EC:6.3.2.-)
Short name:
Praja1
Alternative name(s):
RING finger protein 70
Gene namesi
Name:PJA1
Synonyms:RNF70
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome X

Organism-specific databases

HGNCiHGNC:16648. PJA1.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: Ensembl
Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA33342.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 643643E3 ubiquitin-protein ligase Praja-1PRO_0000055999Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei277 – 2771Phosphothreonine2 Publications

Post-translational modificationi

Substrate for E2-dependent ubiquitination.

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ8NG27.
PaxDbiQ8NG27.
PRIDEiQ8NG27.

PTM databases

PhosphoSiteiQ8NG27.

Expressioni

Tissue specificityi

Expressed in various regions of the brain including the cerebellum, cerebral cortex, medulla, occipital pole, frontal lobe, temporal lobe and putamen. Highest levels in the cerebral cortex.1 Publication

Gene expression databases

BgeeiQ8NG27.
CleanExiHS_PJA1.
ExpressionAtlasiQ8NG27. baseline and differential.
GenevestigatoriQ8NG27.

Organism-specific databases

HPAiHPA000595.

Interactioni

Subunit structurei

Binds ubiquitin-conjugating enzymes (E2s). In vitro, interacts with the ubiquitin-conjugating enzyme, UBE2D2.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
MAGED1Q9Y5V34EBI-714606,EBI-716006
NDNL2Q96MG72EBI-714606,EBI-2557356

Protein-protein interaction databases

BioGridi122109. 48 interactions.
IntActiQ8NG27. 12 interactions.
MINTiMINT-1384058.
STRINGi9606.ENSP00000355014.

Structurei

Secondary structure

1
643
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi571 – 5755Combined sources
Beta strandi579 – 5813Combined sources
Beta strandi587 – 5915Combined sources
Turni596 – 5983Combined sources
Beta strandi607 – 6115Combined sources
Turni612 – 6143Combined sources
Beta strandi615 – 6184Combined sources
Helixi619 – 6268Combined sources
Turni633 – 6353Combined sources
Beta strandi638 – 6403Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2L0BNMR-A564-643[»]
ProteinModelPortaliQ8NG27.
SMRiQ8NG27. Positions 532-643.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi276 – 2827Poly-Asp
Compositional biasi340 – 3434Poly-Arg

Domaini

The RING-type zinc finger domain interacts with an ubiquitin-conjugating enzyme (E2) and facilitates ubiquitination.By similarity

Sequence similaritiesi

Contains 1 RING-type zinc finger.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri595 – 63642RING-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiNOG239209.
GeneTreeiENSGT00530000062967.
HOGENOMiHOG000230900.
HOVERGENiHBG003815.
InParanoidiQ8NG27.
KOiK10633.
OMAiYSRYPPR.
OrthoDBiEOG7TJ3HJ.
PhylomeDBiQ8NG27.
TreeFamiTF330711.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PfamiPF13639. zf-RING_2. 1 hit.
[Graphical view]
SMARTiSM00184. RING. 1 hit.
[Graphical view]
PROSITEiPS50089. ZF_RING_2. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q8NG27-1) [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
MGQESSKPVW PNPTGGYQSN TGRRYGRRHA YVSFRPPTSQ RERIASQRKT
60 70 80 90 100
NSEVPMHRSA PSQTTKRSRS PFSTTRRSWD DSESSGTNLN IDNEDYSRYP
110 120 130 140 150
PREYRASGSR RGMAYGHIDS YGADDSEEEG AGPVERPPVR GKTGKFKDDK
160 170 180 190 200
LYDPEKGARS LAGPPPHFSS FSRDVREERD KLDPVPAARC SASRADFLPQ
210 220 230 240 250
SSVASQSSSE GKLATKGDSS ERERREQNLP ARPSRAPVSI CGGGENTSKS
260 270 280 290 300
AEEPVVRPKI RNLASPNCVK PKIFFDTDDD DDMPHSTSRW RDTANDNEGH
310 320 330 340 350
SDGLARRGRG ESSSGYPEPK YPEDKREARS DQVKPEKVPR RRRTMADPDF
360 370 380 390 400
WTHSDDYYKY CDEDSDSDKE WIAALRRKYR SREQTLSSSG ESWETLPGKE
410 420 430 440 450
EREPPQAKVS ASTGTSPGPG ASASAGAGAG ASAGSNGSNY LEEVREPSLQ
460 470 480 490 500
EEQASLEEGE IPWLQYHEND SSSEGDNDSG HELMQPGVFM LDGNNNLEDD
510 520 530 540 550
SSVSEDLEVD WSLFDGFADG LGVAEAISYV DPQFLTYMAL EERLAQAMET
560 570 580 590 600
ALAHLESLAV DVEVANPPAS KESIDALPEI LVTEDHGAVG QEMCCPICCS
610 620 630 640
EYVKGEVATE LPCHHYFHKP CVSIWLQKSG TCPVCRCMFP PPL
Length:643
Mass (Da):71,002
Last modified:May 23, 2003 - v2
Checksum:iF3DFD1F77809318D
GO
Isoform 2 (identifier: Q8NG27-2) [UniParc]FASTAAdd to Basket

Also known as: PJA1-beta, Praja1-beta

The sequence of this isoform differs from the canonical sequence as follows:
     98-285: Missing.

Note: No experimental confirmation available. PubMed:12036302 reported that isoform 2 arises by alternative initiation.

Show »
Length:455
Mass (Da):50,445
Checksum:iA4C247465CF65396
GO
Isoform 3 (identifier: Q8NG27-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-55: Missing.

Note: Gene prediction based on EST data.

Show »
Length:588
Mass (Da):64,729
Checksum:i2D1B424ED1BA7D87
GO

Sequence cautioni

The sequence BAB13928.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti432 – 4321S → N.1 Publication
Corresponds to variant rs5937160 [ dbSNP | Ensembl ].
VAR_052088
Natural varianti606 – 6061E → D.1 Publication
Corresponds to variant rs11539157 [ dbSNP | Ensembl ].
VAR_052089

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 5555Missing in isoform 3. CuratedVSP_046995Add
BLAST
Alternative sequencei98 – 285188Missing in isoform 2. 1 PublicationVSP_007518Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF262024 mRNA. Translation: AAM53039.1.
AF264620 mRNA. Translation: AAM53040.1.
AL157699 Genomic DNA. Translation: CAI41604.1.
AL157699 Genomic DNA. Translation: CAI41605.1.
CH471132 Genomic DNA. Translation: EAX05367.1.
BC048323 mRNA. Translation: AAH48323.1.
BC075803 mRNA. Translation: AAH75803.1.
BC105051 mRNA. Translation: AAI05052.1.
BC105053 mRNA. Translation: AAI05054.1.
AK021892 mRNA. Translation: BAB13928.1. Different initiation.
CCDSiCCDS14392.1. [Q8NG27-2]
CCDS14393.1. [Q8NG27-1]
CCDS35316.1. [Q8NG27-3]
RefSeqiNP_001027568.1. NM_001032396.2. [Q8NG27-3]
NP_071763.2. NM_022368.4. [Q8NG27-2]
NP_660095.1. NM_145119.3. [Q8NG27-1]
XP_005262349.1. XM_005262292.1. [Q8NG27-3]
UniGeneiHs.522679.

Genome annotation databases

EnsembliENST00000361478; ENSP00000355014; ENSG00000181191. [Q8NG27-1]
ENST00000374571; ENSP00000363699; ENSG00000181191. [Q8NG27-3]
ENST00000374583; ENSP00000363711; ENSG00000181191. [Q8NG27-1]
ENST00000374584; ENSP00000363712; ENSG00000181191. [Q8NG27-2]
GeneIDi64219.
KEGGihsa:64219.
UCSCiuc004dxg.3. human. [Q8NG27-2]
uc004dxh.3. human. [Q8NG27-1]

Polymorphism databases

DMDMi31076980.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF262024 mRNA. Translation: AAM53039.1.
AF264620 mRNA. Translation: AAM53040.1.
AL157699 Genomic DNA. Translation: CAI41604.1.
AL157699 Genomic DNA. Translation: CAI41605.1.
CH471132 Genomic DNA. Translation: EAX05367.1.
BC048323 mRNA. Translation: AAH48323.1.
BC075803 mRNA. Translation: AAH75803.1.
BC105051 mRNA. Translation: AAI05052.1.
BC105053 mRNA. Translation: AAI05054.1.
AK021892 mRNA. Translation: BAB13928.1. Different initiation.
CCDSiCCDS14392.1. [Q8NG27-2]
CCDS14393.1. [Q8NG27-1]
CCDS35316.1. [Q8NG27-3]
RefSeqiNP_001027568.1. NM_001032396.2. [Q8NG27-3]
NP_071763.2. NM_022368.4. [Q8NG27-2]
NP_660095.1. NM_145119.3. [Q8NG27-1]
XP_005262349.1. XM_005262292.1. [Q8NG27-3]
UniGeneiHs.522679.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2L0BNMR-A564-643[»]
ProteinModelPortaliQ8NG27.
SMRiQ8NG27. Positions 532-643.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi122109. 48 interactions.
IntActiQ8NG27. 12 interactions.
MINTiMINT-1384058.
STRINGi9606.ENSP00000355014.

PTM databases

PhosphoSiteiQ8NG27.

Polymorphism databases

DMDMi31076980.

Proteomic databases

MaxQBiQ8NG27.
PaxDbiQ8NG27.
PRIDEiQ8NG27.

Protocols and materials databases

DNASUi64219.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000361478; ENSP00000355014; ENSG00000181191. [Q8NG27-1]
ENST00000374571; ENSP00000363699; ENSG00000181191. [Q8NG27-3]
ENST00000374583; ENSP00000363711; ENSG00000181191. [Q8NG27-1]
ENST00000374584; ENSP00000363712; ENSG00000181191. [Q8NG27-2]
GeneIDi64219.
KEGGihsa:64219.
UCSCiuc004dxg.3. human. [Q8NG27-2]
uc004dxh.3. human. [Q8NG27-1]

Organism-specific databases

CTDi64219.
GeneCardsiGC0XM068297.
HGNCiHGNC:16648. PJA1.
HPAiHPA000595.
MIMi300420. gene.
neXtProtiNX_Q8NG27.
PharmGKBiPA33342.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG239209.
GeneTreeiENSGT00530000062967.
HOGENOMiHOG000230900.
HOVERGENiHBG003815.
InParanoidiQ8NG27.
KOiK10633.
OMAiYSRYPPR.
OrthoDBiEOG7TJ3HJ.
PhylomeDBiQ8NG27.
TreeFamiTF330711.

Enzyme and pathway databases

ReactomeiREACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.

Miscellaneous databases

GeneWikiiPJA1.
GenomeRNAii64219.
NextBioi66135.
PROiQ8NG27.
SOURCEiSearch...

Gene expression databases

BgeeiQ8NG27.
CleanExiHS_PJA1.
ExpressionAtlasiQ8NG27. baseline and differential.
GenevestigatoriQ8NG27.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PfamiPF13639. zf-RING_2. 1 hit.
[Graphical view]
SMARTiSM00184. RING. 1 hit.
[Graphical view]
PROSITEiPS50089. ZF_RING_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "PJA1, encoding a RING-H2 finger ubiquitin ligase, is a novel human X chromosome gene abundantly expressed in brain."
    Yu P., Chen Y., Tagle D.A., Cai T.
    Genomics 79:869-874(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, TISSUE SPECIFICITY, INTERACTION WITH UBE2D2.
    Tissue: Brain.
  2. "The DNA sequence of the human X chromosome."
    Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.
    , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
    Nature 434:325-337(2005) [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 1), VARIANTS ASN-432 AND ASP-606.
    Tissue: Brain, Kidney and Uterus.
  5. "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] OF 282-643 (ISOFORM 1).
    Tissue: Embryo.
  6. "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 THR-277, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  7. "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 THR-277, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiPJA1_HUMAN
AccessioniPrimary (citable) accession number: Q8NG27
Secondary accession number(s): A2A322
, Q5JUT8, Q5JUT9, Q8NG28, Q9HAC1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 23, 2003
Last sequence update: May 23, 2003
Last modified: January 7, 2015
This is version 119 of the entry and version 2 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 X
    Human chromosome X: 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.