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Q8NG27 (PJA1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 114. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
E3 ubiquitin-protein ligase Praja-1

Short name=Praja1
EC=6.3.2.-
Alternative name(s):
RING finger protein 70
Gene names
Name:PJA1
Synonyms:RNF70
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length643 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.1

Subunit structure

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

Tissue specificity

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. Ref.1

Domain

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

Post-translational modification

Substrate for E2-dependent ubiquitination.

Sequence similarities

Contains 1 RING-type zinc finger.

Sequence caution

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

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

MAGED1Q9Y5V34EBI-714606,EBI-716006
NDNL2Q96MG72EBI-714606,EBI-2557356

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q8NG27-1)

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.
Isoform 2 (identifier: Q8NG27-2)

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.
Isoform 3 (identifier: Q8NG27-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-55: Missing.
Note: Gene prediction based on EST data.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 643643E3 ubiquitin-protein ligase Praja-1
PRO_0000055999

Regions

Zinc finger595 – 63642RING-type
Compositional bias276 – 2827Poly-Asp
Compositional bias340 – 3434Poly-Arg

Amino acid modifications

Modified residue2771Phosphothreonine Ref.6 Ref.7

Natural variations

Alternative sequence1 – 5555Missing in isoform 3.
VSP_046995
Alternative sequence98 – 285188Missing in isoform 2.
VSP_007518
Natural variant4321S → N. Ref.4
Corresponds to variant rs5937160 [ dbSNP | Ensembl ].
VAR_052088
Natural variant6061E → D. Ref.4
Corresponds to variant rs11539157 [ dbSNP | Ensembl ].
VAR_052089

Secondary structure

.................. 643
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified May 23, 2003. Version 2.
Checksum: F3DFD1F77809318D

FASTA64371,002
        10         20         30         40         50         60 
MGQESSKPVW PNPTGGYQSN TGRRYGRRHA YVSFRPPTSQ RERIASQRKT NSEVPMHRSA 

        70         80         90        100        110        120 
PSQTTKRSRS PFSTTRRSWD DSESSGTNLN IDNEDYSRYP PREYRASGSR RGMAYGHIDS 

       130        140        150        160        170        180 
YGADDSEEEG AGPVERPPVR GKTGKFKDDK LYDPEKGARS LAGPPPHFSS FSRDVREERD 

       190        200        210        220        230        240 
KLDPVPAARC SASRADFLPQ SSVASQSSSE GKLATKGDSS ERERREQNLP ARPSRAPVSI 

       250        260        270        280        290        300 
CGGGENTSKS AEEPVVRPKI RNLASPNCVK PKIFFDTDDD DDMPHSTSRW RDTANDNEGH 

       310        320        330        340        350        360 
SDGLARRGRG ESSSGYPEPK YPEDKREARS DQVKPEKVPR RRRTMADPDF WTHSDDYYKY 

       370        380        390        400        410        420 
CDEDSDSDKE WIAALRRKYR SREQTLSSSG ESWETLPGKE EREPPQAKVS ASTGTSPGPG 

       430        440        450        460        470        480 
ASASAGAGAG ASAGSNGSNY LEEVREPSLQ EEQASLEEGE IPWLQYHEND SSSEGDNDSG 

       490        500        510        520        530        540 
HELMQPGVFM LDGNNNLEDD SSVSEDLEVD WSLFDGFADG LGVAEAISYV DPQFLTYMAL 

       550        560        570        580        590        600 
EERLAQAMET ALAHLESLAV DVEVANPPAS KESIDALPEI LVTEDHGAVG QEMCCPICCS 

       610        620        630        640 
EYVKGEVATE LPCHHYFHKP CVSIWLQKSG TCPVCRCMFP PPL 

« Hide

Isoform 2 (PJA1-beta) (Praja1-beta) [UniParc].

Checksum: A4C247465CF65396
Show »

FASTA45550,445
Isoform 3 [UniParc].

Checksum: 2D1B424ED1BA7D87
Show »

FASTA58864,729

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
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. expand/collapse author list , 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].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS14392.1. [Q8NG27-2]
CCDS14393.1. [Q8NG27-1]
CCDS35316.1. [Q8NG27-3]
RefSeqNP_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]
UniGeneHs.522679.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2L0BNMR-A564-643[»]
ProteinModelPortalQ8NG27.
SMRQ8NG27. Positions 532-643.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid122109. 37 interactions.
IntActQ8NG27. 12 interactions.
MINTMINT-1384058.
STRING9606.ENSP00000355014.

PTM databases

PhosphoSiteQ8NG27.

Polymorphism databases

DMDM31076980.

Proteomic databases

MaxQBQ8NG27.
PaxDbQ8NG27.
PRIDEQ8NG27.

Protocols and materials databases

DNASU64219.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000361478; ENSP00000355014; ENSG00000181191. [Q8NG27-1]
ENST00000374571; ENSP00000363699; ENSG00000181191. [Q8NG27-3]
ENST00000374583; ENSP00000363711; ENSG00000181191. [Q8NG27-1]
ENST00000374584; ENSP00000363712; ENSG00000181191. [Q8NG27-2]
GeneID64219.
KEGGhsa:64219.
UCSCuc004dxg.3. human. [Q8NG27-2]
uc004dxh.3. human. [Q8NG27-1]

Organism-specific databases

CTD64219.
GeneCardsGC0XM068297.
HGNCHGNC:16648. PJA1.
HPAHPA000595.
MIM300420. gene.
neXtProtNX_Q8NG27.
PharmGKBPA33342.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG239209.
HOGENOMHOG000230900.
HOVERGENHBG003815.
InParanoidQ8NG27.
KOK10633.
OMAYSRYPPR.
OrthoDBEOG7TJ3HJ.
PhylomeDBQ8NG27.
TreeFamTF330711.

Enzyme and pathway databases

ReactomeREACT_6900. Immune System.

Gene expression databases

ArrayExpressQ8NG27.
BgeeQ8NG27.
CleanExHS_PJA1.
GenevestigatorQ8NG27.

Family and domain databases

Gene3D3.30.40.10. 1 hit.
InterProIPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PfamPF13639. zf-RING_2. 1 hit.
[Graphical view]
SMARTSM00184. RING. 1 hit.
[Graphical view]
PROSITEPS50089. ZF_RING_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiPJA1.
GenomeRNAi64219.
NextBio66135.
PROQ8NG27.
SOURCESearch...

Entry information

Entry namePJA1_HUMAN
AccessionPrimary (citable) accession number: Q8NG27
Secondary accession number(s): A2A322 expand/collapse secondary AC list , Q5JUT8, Q5JUT9, Q8NG28, Q9HAC1
Entry history
Integrated into UniProtKB/Swiss-Prot: May 23, 2003
Last sequence update: May 23, 2003
Last modified: July 9, 2014
This is version 114 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome X

Human chromosome X: entries, gene names and cross-references to MIM