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Q9H0F5

- RNF38_HUMAN

UniProt

Q9H0F5 - RNF38_HUMAN

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Protein

E3 ubiquitin-protein ligase RNF38

Gene

RNF38

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

Functioni

Acts as an E3 ubiquitin-protein ligase able to ubiquitinate p53/TP53 which promotes its relocalization to discrete foci associated with PML nuclear bodies. Exhibits preference for UBE2D2 as a E2 enzyme.1 Publication

Pathwayi

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri463 – 50442RING-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

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

GO - Biological processi

  1. male gonad development Source: Ensembl
  2. protein ubiquitination Source: FlyBase
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Ubl conjugation pathway

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
E3 ubiquitin-protein ligase RNF38 (EC:6.3.2.-)
Alternative name(s):
RING finger protein 38
Gene namesi
Name:RNF38
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 9

Organism-specific databases

HGNCiHGNC:18052. RNF38.

Subcellular locationi

Nucleus 1 Publication

GO - Cellular componenti

  1. nucleus Source: FlyBase
  2. sperm flagellum Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA34438.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 515515E3 ubiquitin-protein ligase RNF38PRO_0000056078Add
BLAST

Proteomic databases

PaxDbiQ9H0F5.
PRIDEiQ9H0F5.

PTM databases

PhosphoSiteiQ9H0F5.

Expressioni

Tissue specificityi

Widely expressed with highest levels in testis.1 Publication

Gene expression databases

BgeeiQ9H0F5.
CleanExiHS_RNF38.
GenevestigatoriQ9H0F5.

Organism-specific databases

HPAiHPA015853.

Interactioni

Protein-protein interaction databases

BioGridi127416. 16 interactions.
IntActiQ9H0F5. 9 interactions.
MINTiMINT-4720518.
STRINGi9606.ENSP00000259605.

Structurei

Secondary structure

1
515
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi449 – 4513
Beta strandi453 – 4553
Beta strandi457 – 4593
Turni464 – 4674
Beta strandi475 – 4795
Turni480 – 4823
Beta strandi483 – 4864
Helixi489 – 4968
Turni501 – 5033

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1X4JNMR-A445-506[»]
ProteinModelPortaliQ9H0F5.
SMRiQ9H0F5. Positions 445-507.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9H0F5.

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi57 – 7115Bipartite nuclear localization signal 1Add
BLAST
Motifi115 – 13117Bipartite nuclear localization signal 2Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi239 – 404166Pro-richAdd
BLAST

Sequence similaritiesi

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

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri463 – 50442RING-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiCOG5540.
GeneTreeiENSGT00730000110459.
HOGENOMiHOG000231638.
HOVERGENiHBG059283.
InParanoidiQ9H0F5.
OMAiNQHHFSG.
OrthoDBiEOG74TWZV.
PhylomeDBiQ9H0F5.
TreeFamiTF325756.

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 (5)i

Sequence statusi: Complete.

This entry describes 5 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9H0F5-1) [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
MACKISPGAN SASLPGHPNK VICERVRLQS LFPLLPSDQN TTVQEDAHFK
60 70 80 90 100
AFFQSEDSPS PKRQRLSHSV FDYTSASPAP SPPMRPWEMT SNRQPPSVRP
110 120 130 140 150
SQHHFSGERC NTPARNRRSP PVRRQRGRRD RLSRHNSISQ DENYHHLPYA
160 170 180 190 200
QQQAIEEPRA FHPPNVSPRL LHPAAHPPQQ NAVMVDIHDQ LHQGTVPVSY
210 220 230 240 250
TVTTVAPHGI PLCTGQHIPA CSTQQVPGCS VVFSGQHLPV CSVPPPMLQA
260 270 280 290 300
CSVQHLPVPY AAFPPLISSD PFLIHPPHLS PHHPPHLPPP GQFVPFQTQQ
310 320 330 340 350
SRSPLQRIEN EVELLGEHLP VGGFTYPPSA HPPTLPPSAP LQFLTHDPLH
360 370 380 390 400
QEVSFGVPYP PFMPRRLTGR SRYRSQQPIP PPPYHPSLLP YVLSMLPVPP
410 420 430 440 450
AVGPTFSFEL DVEDGEVENY EALLNLAERL GEAKPRGLTK ADIEQLPSYR
460 470 480 490 500
FNPNNHQSEQ TLCVVCMCDF ESRQLLRVLP CNHEFHAKCV DKWLKANRTC
510
PICRADASEV HRDSE
Length:515
Mass (Da):57,595
Last modified:December 21, 2004 - v4
Checksum:iABFE9486CA732AFA
GO
Isoform 2 (identifier: Q9H0F5-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     5-54: Missing.

Note: No experimental confirmation available.

Show »
Length:465
Mass (Da):52,106
Checksum:i18A919182C967BA6
GO
Isoform 3 (identifier: Q9H0F5-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-83: Missing.

Show »
Length:432
Mass (Da):48,562
Checksum:iCCC2D1396DB31D2C
GO
Isoform 4 (identifier: Q9H0F5-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-44: MACKISPGAN...LPSDQNTTVQ → MQHTCTQQKK...NLAGFQLQSP
     45-120: Missing.

Note: No experimental confirmation available.

Show »
Length:439
Mass (Da):49,265
Checksum:i76E2EFFA9FDFA02D
GO
Isoform 5 (identifier: Q9H0F5-5) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-183: Missing.

Note: No experimental confirmation available.

Show »
Length:332
Mass (Da):36,836
Checksum:i4A2E365DA4A094A0
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti308 – 3081I → K in CAB66751. (PubMed:11230166)Curated
Sequence conflicti421 – 4211E → G in BAG52726. (PubMed:14702039)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti206 – 2061A → T.1 Publication
Corresponds to variant rs183475137 [ dbSNP | Ensembl ].
VAR_055400

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 183183Missing in isoform 5. 1 PublicationVSP_053845Add
BLAST
Alternative sequencei1 – 8383Missing in isoform 3. 1 PublicationVSP_037337Add
BLAST
Alternative sequencei1 – 4444MACKI…NTTVQ → MQHTCTQQKKVTYKHIARFS PRNRLCQADAVFNNNLAGFQ LQSP in isoform 4. 1 PublicationVSP_053846Add
BLAST
Alternative sequencei5 – 5450Missing in isoform 2. 1 PublicationVSP_012243Add
BLAST
Alternative sequencei45 – 12076Missing in isoform 4. 1 PublicationVSP_053847Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF394047 mRNA. Translation: AAM73697.1.
AL136817 mRNA. Translation: CAB66751.3.
AK024996 mRNA. Translation: BAB15050.1.
AK093480 mRNA. Translation: BAG52726.1.
AL161792, AL354935 Genomic DNA. Translation: CAO03553.1.
AL354935, AL161792 Genomic DNA. Translation: CAO03540.1.
AL354935, AL161792 Genomic DNA. Translation: CAO03541.1.
AL161792, AL354935 Genomic DNA. Translation: CAO03554.1.
CH471071 Genomic DNA. Translation: EAW58305.1.
BC033786 mRNA. Translation: AAH33786.2.
CCDSiCCDS6603.1. [Q9H0F5-1]
CCDS6604.1. [Q9H0F5-2]
RefSeqiNP_073618.3. NM_022781.4. [Q9H0F5-1]
NP_919309.1. NM_194328.2. [Q9H0F5-3]
NP_919310.1. NM_194329.2. [Q9H0F5-2]
NP_919311.1. NM_194330.2. [Q9H0F5-3]
NP_919313.1. NM_194332.2. [Q9H0F5-3]
XP_005251423.1. XM_005251366.1. [Q9H0F5-3]
XP_005251424.1. XM_005251367.1. [Q9H0F5-3]
XP_005251425.1. XM_005251368.1. [Q9H0F5-3]
XP_006716784.1. XM_006716721.1. [Q9H0F5-3]
UniGeneiHs.333503.

Genome annotation databases

EnsembliENST00000259605; ENSP00000259605; ENSG00000137075. [Q9H0F5-1]
ENST00000350199; ENSP00000343947; ENSG00000137075. [Q9H0F5-3]
ENST00000353739; ENSP00000335239; ENSG00000137075. [Q9H0F5-2]
ENST00000357058; ENSP00000349566; ENSG00000137075. [Q9H0F5-3]
ENST00000377877; ENSP00000367109; ENSG00000137075. [Q9H0F5-4]
ENST00000377885; ENSP00000367117; ENSG00000137075. [Q9H0F5-3]
ENST00000611646; ENSP00000483536; ENSG00000137075. [Q9H0F5-4]
GeneIDi152006.
KEGGihsa:152006.
UCSCiuc003zzh.3. human. [Q9H0F5-1]
uc003zzi.3. human. [Q9H0F5-2]

Polymorphism databases

DMDMi56749664.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF394047 mRNA. Translation: AAM73697.1 .
AL136817 mRNA. Translation: CAB66751.3 .
AK024996 mRNA. Translation: BAB15050.1 .
AK093480 mRNA. Translation: BAG52726.1 .
AL161792 , AL354935 Genomic DNA. Translation: CAO03553.1 .
AL354935 , AL161792 Genomic DNA. Translation: CAO03540.1 .
AL354935 , AL161792 Genomic DNA. Translation: CAO03541.1 .
AL161792 , AL354935 Genomic DNA. Translation: CAO03554.1 .
CH471071 Genomic DNA. Translation: EAW58305.1 .
BC033786 mRNA. Translation: AAH33786.2 .
CCDSi CCDS6603.1. [Q9H0F5-1 ]
CCDS6604.1. [Q9H0F5-2 ]
RefSeqi NP_073618.3. NM_022781.4. [Q9H0F5-1 ]
NP_919309.1. NM_194328.2. [Q9H0F5-3 ]
NP_919310.1. NM_194329.2. [Q9H0F5-2 ]
NP_919311.1. NM_194330.2. [Q9H0F5-3 ]
NP_919313.1. NM_194332.2. [Q9H0F5-3 ]
XP_005251423.1. XM_005251366.1. [Q9H0F5-3 ]
XP_005251424.1. XM_005251367.1. [Q9H0F5-3 ]
XP_005251425.1. XM_005251368.1. [Q9H0F5-3 ]
XP_006716784.1. XM_006716721.1. [Q9H0F5-3 ]
UniGenei Hs.333503.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1X4J NMR - A 445-506 [» ]
ProteinModelPortali Q9H0F5.
SMRi Q9H0F5. Positions 445-507.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 127416. 16 interactions.
IntActi Q9H0F5. 9 interactions.
MINTi MINT-4720518.
STRINGi 9606.ENSP00000259605.

PTM databases

PhosphoSitei Q9H0F5.

Polymorphism databases

DMDMi 56749664.

Proteomic databases

PaxDbi Q9H0F5.
PRIDEi Q9H0F5.

Protocols and materials databases

DNASUi 152006.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000259605 ; ENSP00000259605 ; ENSG00000137075 . [Q9H0F5-1 ]
ENST00000350199 ; ENSP00000343947 ; ENSG00000137075 . [Q9H0F5-3 ]
ENST00000353739 ; ENSP00000335239 ; ENSG00000137075 . [Q9H0F5-2 ]
ENST00000357058 ; ENSP00000349566 ; ENSG00000137075 . [Q9H0F5-3 ]
ENST00000377877 ; ENSP00000367109 ; ENSG00000137075 . [Q9H0F5-4 ]
ENST00000377885 ; ENSP00000367117 ; ENSG00000137075 . [Q9H0F5-3 ]
ENST00000611646 ; ENSP00000483536 ; ENSG00000137075 . [Q9H0F5-4 ]
GeneIDi 152006.
KEGGi hsa:152006.
UCSCi uc003zzh.3. human. [Q9H0F5-1 ]
uc003zzi.3. human. [Q9H0F5-2 ]

Organism-specific databases

CTDi 152006.
GeneCardsi GC09M036336.
HGNCi HGNC:18052. RNF38.
HPAi HPA015853.
MIMi 612488. gene.
neXtProti NX_Q9H0F5.
PharmGKBi PA34438.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5540.
GeneTreei ENSGT00730000110459.
HOGENOMi HOG000231638.
HOVERGENi HBG059283.
InParanoidi Q9H0F5.
OMAi NQHHFSG.
OrthoDBi EOG74TWZV.
PhylomeDBi Q9H0F5.
TreeFami TF325756.

Enzyme and pathway databases

UniPathwayi UPA00143 .

Miscellaneous databases

ChiTaRSi RNF38. human.
EvolutionaryTracei Q9H0F5.
GeneWikii RNF38.
GenomeRNAii 152006.
NextBioi 35466719.
PROi Q9H0F5.
SOURCEi Search...

Gene expression databases

Bgeei Q9H0F5.
CleanExi HS_RNF38.
Genevestigatori Q9H0F5.

Family and domain databases

Gene3Di 3.30.40.10. 1 hit.
InterProi IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view ]
Pfami PF13639. zf-RING_2. 1 hit.
[Graphical view ]
SMARTi SM00184. RING. 1 hit.
[Graphical view ]
PROSITEi PS50089. ZF_RING_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and characterization of a novel human gene RNF38 encoding a conserved putative protein with a RING finger domain."
    Eisenberg I., Hochner H., Levi T., Yelin R., Kahan T., Mitrani-Rosenbaum S.
    Biochem. Biophys. Res. Commun. 294:1169-1176(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), TISSUE SPECIFICITY, VARIANT THR-206.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Testis.
  3. "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 AND 5).
    Tissue: Colon and Testis.
  4. "DNA sequence and analysis of human chromosome 9."
    Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L.
    , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
    Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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 2).
    Tissue: Brain.
  7. "RNF38 encodes a nuclear ubiquitin protein ligase that modifies p53."
    Sheren J.E., Kassenbrock C.K.
    Biochem. Biophys. Res. Commun. 440:473-478(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, NUCLEAR LOCALIZATION SIGNAL, SUBCELLULAR LOCATION.
  8. "Solution structure of RING finger in RING finger protein 38."
    RIKEN structural genomics initiative (RSGI)
    Submitted (NOV-2005) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 445-506.

Entry informationi

Entry nameiRNF38_HUMAN
AccessioniPrimary (citable) accession number: Q9H0F5
Secondary accession number(s): A6PVP9
, B1AM81, B1AM82, B3KSG4, E7EVL3, Q7LB33, Q8N0Y0, Q9H748
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 21, 2004
Last sequence update: December 21, 2004
Last modified: October 29, 2014
This is version 110 of the entry and version 4 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 9
    Human chromosome 9: 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. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3