Reviewed, UniProtKB/Swiss-Prot Q8NG27 (PJA1_HUMAN)

Names and origin

Protein names

Recommended name:
    E3 ubiquitin-protein ligase Praja1
      Short name=Praja-1
    EC=6.3.2.-
Alternative name(s):
    RING finger protein 70

Gene names

Name:	PJA1
Synonyms:	RNF70

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	643 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Has E2-dependent E3 ubiquitin-protein ligase activity. Ubiquitinates MAGED1 antigen leading to its subsequent degradation by proteosome By similarity. May be involved in protein sorting.
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.
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.

Ontologies

Keywords
Biological process	Ubl conjugation pathway
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Zinc-finger
Ligand	Metal-binding Zinc
Molecular function	Ligase
PTM	Ubl conjugation
Gene Ontology (GO)
Biological process	modification-dependent protein catabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	nucleolus Inferred from direct assay. Source: HPA
Molecular function	ligase activity Inferred from electronic annotation. Source: UniProtKB-KW protein binding Inferred from electronic annotation. Source: InterPro zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Alternative products

This entry describes 2 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. Ref.1 reported that isoform 2 arises by alternative initiation.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 643	643	E3 ubiquitin-protein ligase Praja1		PRO_0000055999
Regions
	Zinc finger	595 – 636	42	RING-type
	Compositional bias	276 – 282	7	Poly-Asp
	Compositional bias	340 – 343	4	Poly-Arg
Natural variations
	Alternative sequence	98 – 285	188	Missing in isoform 2.		VSP_007518
	Natural variant	432	1	S → N: dbSNP rs5937160. Ref.3		VAR_052088
	Natural variant	606	1	E → D: dbSNP rs11539157. Ref.3		VAR_052089

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified May 23, 2003. Version 2. Checksum: F3DFD1F77809318D	FASTA	643	71,002
	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
	Isoform 2 (PJA1-beta) (Praja1-beta). Checksum: A4C247465CF65396	FASTA	455	50,445
	10 20 30 40 50 60 MGQESSKPVW PNPTGGYQSN TGRRYGRRHA YVSFRPPTSQ RERIASQRKT NSEVPMHRSA 70 80 90 100 110 120 PSQTTKRSRS PFSTTRRSWD DSESSGTNLN IDNEDYSSTS RWRDTANDNE GHSDGLARRG 130 140 150 160 170 180 RGESSSGYPE PKYPEDKREA RSDQVKPEKV PRRRRTMADP DFWTHSDDYY KYCDEDSDSD 190 200 210 220 230 240 KEWIAALRRK YRSREQTLSS SGESWETLPG KEEREPPQAK VSASTGTSPG PGASASAGAG 250 260 270 280 290 300 AGASAGSNGS NYLEEVREPS LQEEQASLEE GEIPWLQYHE NDSSSEGDND SGHELMQPGV 310 320 330 340 350 360 FMLDGNNNLE DDSSVSEDLE VDWSLFDGFA DGLGVAEAIS YVDPQFLTYM ALEERLAQAM 370 380 390 400 410 420 ETALAHLESL AVDVEVANPP ASKESIDALP EILVTEDHGA VGQEMCCPIC CSEYVKGEVA 430 440 450 TELPCHHYFH KPCVSIWLQK SGTCPVCRCM FPPPL

References

	« Hide 'large scale' referencesShow '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: 12036302] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), INTERACTION WITH UBE2D2.
[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: 15772651] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANTS ASN-432 AND ASP-606. Tissue: Brain, Kidney and Uterus.
[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: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 282-643 (ISOFORM 1). Tissue: Embryo.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF262024 mRNA. Translation: AAM53039.1. AF264620 mRNA. Translation: AAM53040.1. AL157699 Genomic DNA. Translation: CAI41604.1. 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.
IPI	IPI00251615. IPI00294448.
RefSeq	NP_001027568.1. NP_071763.2. NP_660095.1.
UniGene	Hs.522679
3D structure databases
ModBase	Search...
Protein-protein interaction databases
IntAct	Q8NG27. 7 interactions.
PTM databases
PhosphoSite	Q8NG27.
Proteomic databases
PRIDE	Q8NG27.
Genome annotation databases
Ensembl	ENSG00000181191. Homo sapiens. [Contig view]
GeneID	64219.
KEGG	hsa:64219.
Organism-specific databases
GeneCards	GC0XM068297.
H-InvDB	HIX0016847.
HGNC	HGNC:16648. PJA1.
HPA	HPA000595.
MIM	300420. gene.
PharmGKB	PA33342.
GenAtlas	Search...
Phylogenomic databases
HOGENOM	Q8NG27.
HOVERGEN	Q8NG27.
OMA	Q8NG27. NLASPNC.
Gene expression databases
ArrayExpress	Q8NG27.
Bgee	Q8NG27.
CleanEx	HS_PJA1.
GermOnline	ENSG00000181191. Homo sapiens.
Family and domain databases
InterPro	IPR018957. Znf_C3HC4_RING-type. IPR001841. Znf_RING. IPR017907. Znf_RING_CS. [Graphical view]
Pfam	PF00097. zf-C3HC4. 1 hit. [Graphical view]
SMART	SM00184. RING. 1 hit. [Graphical view]
PROSITE	PS00518. ZF_RING_1. False negative. PS50089. ZF_RING_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	66135.
SOURCE	Search...

Entry information

Entry name

PJA1_HUMAN

Accession

Primary (citable) accession number: Q8NG27
Secondary accession number(s): Q5JUT9, Q8NG28, Q9HAC1

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 23, 2003
Last sequence update:	May 23, 2003
Last modified:	June 16, 2009
This is version 63 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)