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Protein

E3 ubiquitin-protein ligase RNF123

Gene

RNF123

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

Functioni

Catalytic subunit of the KPC complex that acts as E3 ubiquitin-protein ligase. Required for poly-ubiquitination and proteasome-mediated degradation of CDKN1B during G1 phase of the cell cycle.2 Publications

Pathwayi: protein ubiquitination

This protein is involved in the pathway protein ubiquitination, which is part of Protein modification.
View all proteins of this organism that are known to be involved in the pathway protein ubiquitination and in Protein modification.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri1254 – 129239RING-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Ubl conjugation pathway

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiR-HSA-983168. Antigen processing: Ubiquitination & Proteasome degradation.
UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
E3 ubiquitin-protein ligase RNF123 (EC:6.3.2.-)
Alternative name(s):
Kip1 ubiquitination-promoting complex protein 1
RING finger protein 123
Gene namesi
Name:RNF123
Synonyms:KPC1
ORF Names:FP1477
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 3

Organism-specific databases

HGNCiHGNC:21148. RNF123.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134916827.

Polymorphism and mutation databases

BioMutaiRNF123.
DMDMi74748090.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedCombined sources
Chaini2 – 13141313E3 ubiquitin-protein ligase RNF123PRO_0000250447Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineCombined sources
Modified residuei675 – 6751PhosphoserineBy similarity

Post-translational modificationi

Ubiquitinated, leading to its degradation. Deubiquitinated by USP19, thereby stimulating CDKN1B ubiquitin-dependent degradation (By similarity).By similarity

Keywords - PTMi

Acetylation, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ5XPI4.
MaxQBiQ5XPI4.
PaxDbiQ5XPI4.
PeptideAtlasiQ5XPI4.
PRIDEiQ5XPI4.

PTM databases

iPTMnetiQ5XPI4.
PhosphoSiteiQ5XPI4.

Expressioni

Gene expression databases

BgeeiQ5XPI4.
CleanExiHS_RNF123.
ExpressionAtlasiQ5XPI4. baseline and differential.
GenevisibleiQ5XPI4. HS.

Interactioni

Subunit structurei

Component of the KPC complex composed of RNF123/KPC1 and UBAC1/KPC2. Interacts with UBAC1 and CDKN1B via its N-terminal domain.2 Publications

Protein-protein interaction databases

BioGridi121971. 39 interactions.
IntActiQ5XPI4. 13 interactions.
MINTiMINT-1187266.
STRINGi9606.ENSP00000328287.

Structurei

Secondary structure

1
1314
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi1250 – 12534Combined sources
Turni1255 – 12573Combined sources
Beta strandi1258 – 12614Combined sources
Beta strandi1264 – 12674Combined sources
Turni1268 – 12703Combined sources
Beta strandi1271 – 12733Combined sources
Helixi1275 – 12817Combined sources
Turni1282 – 12843Combined sources
Beta strandi1296 – 13005Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2MA6NMR-A1247-1304[»]
ProteinModelPortaliQ5XPI4.
SMRiQ5XPI4. Positions 1244-1304.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini74 – 254181B30.2/SPRYPROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi1237 – 12448Poly-Ala

Sequence similaritiesi

Contains 1 B30.2/SPRY domain.PROSITE-ProRule annotation
Contains 1 RING-type zinc finger.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri1254 – 129239RING-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiKOG2242. Eukaryota.
KOG4692. Eukaryota.
ENOG410XQ4V. LUCA.
GeneTreeiENSGT00530000063442.
HOVERGENiHBG079909.
InParanoidiQ5XPI4.
KOiK12169.
OMAiAVMMYNL.
PhylomeDBiQ5XPI4.
TreeFamiTF313546.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR001870. B30.2/SPRY.
IPR013320. ConA-like_dom.
IPR003877. SPRY_dom.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PfamiPF00622. SPRY. 1 hit.
[Graphical view]
SMARTiSM00184. RING. 1 hit.
SM00449. SPRY. 1 hit.
[Graphical view]
SUPFAMiSSF49899. SSF49899. 1 hit.
PROSITEiPS50188. B302_SPRY. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q5XPI4-1) [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
MASKGAGMSF SRKSYRLTSD AEKSRVTGIV QEKLLNDYLN RIFSSSEHAP
60 70 80 90 100
PAATSRKPLN FQNLPEHLDQ LLQVDNEEEE SQGQVEGRLG PSTVVLDHTG
110 120 130 140 150
GFEGLLLVDD DLLGVIGHSN FGTIRSTTCV YKGKWLYEVL ISSQGLMQIG
160 170 180 190 200
WCTISCRFNQ EEGVGDTHNS YAYDGNRVRK WNVTTTNYGK AWAAGDIVSC
210 220 230 240 250
LIDLDDGTLS FCLNGVSLGT AFENLSRGLG MAYFPAISLS FKESVAFNFG
260 270 280 290 300
SRPLRYPVAG YRPLQDPPSA DLVRAQRLLG CFRAVLSVEL DPVEGRLLDK
310 320 330 340 350
ESSKWRLRGQ PTVLLTLAHI FHHFAPLLRK VYLVEAVLMS FLLGIVEKGT
360 370 380 390 400
PTQAQSVVHQ VLDLLWLFME DYEVQDCLKQ LMMSLLRLYR FSPIVPDLGL
410 420 430 440 450
QIHYLRLTIA ILRHEKSRKF LLSNVLFDVL RSVVFFYIKS PLRVEEAGLQ
460 470 480 490 500
ELIPTTWWPH CSSREGKEST EMKEETAEER LRRRAYERGC QRLRKRIEVV
510 520 530 540 550
EELQVQILKL LLDNKDDNGG EASRYIFLTK FRKFLQENAS GRGNMPMLCP
560 570 580 590 600
PEYMVCFLHR LISALRYYWD EYKASNPHAS FSEEAYIPPQ VFYNGKVDYF
610 620 630 640 650
DLQRLGGLLS HLRKTLKDDL ASKANIVIDP LELQSTAMDD LDEDEEPAPA
660 670 680 690 700
MAQRPMQALA VGGPLPLPRP GWLSSPTLGR ANRFLSTAAV SLMTPRRPLS
710 720 730 740 750
TSEKVKVRTL SVEQRTREDI EGSHWNEGLL LGRPPEEPEQ PLTENSLLEV
760 770 780 790 800
LDGAVMMYNL SVHQQLGKMV GVSDDVNEYA MALRDTEDKL RRCPKRRKDI
810 820 830 840 850
LAELTKSQKV FSEKLDHLSR RLAWVHATVY SQEKMLDIYW LLRVCLRTIE
860 870 880 890 900
HGDRTGSLFA FMPEFYLSVA INSYSALKNY FGPVHSMEEL PGYEETLTRL
910 920 930 940 950
AAILAKHFAD ARIVGTDIRD SLMQALASYV CYPHSLRAVE RIPEEQRIAM
960 970 980 990 1000
VRNLLAPYEQ RPWAQTNWIL VRLWRGCGFG YRYTRLPHLL KTKLEDANLP
1010 1020 1030 1040 1050
SLQKPCPSTL LQQHMADLLQ QGPDVAPSFL NSVLNQLNWA FSEFIGMIQE
1060 1070 1080 1090 1100
IQQAAERLER NFVDSRQLKV CATCFDLSVS LLRVLEMTIT LVPEIFLDWT
1110 1120 1130 1140 1150
RPTSEMLLRR LAQLLNQVLN RVTAERNLFD RVVTLRLPGL ESVDHYPILV
1160 1170 1180 1190 1200
AVTGILVQLL VRGPASEREQ ATSVLLADPC FQLRSICYLL GQPEPPAPGT
1210 1220 1230 1240 1250
ALPAPDRKRF SLQSYADYIS ADELAQVEQM LAHLTSASAQ AAAASLPTSE
1260 1270 1280 1290 1300
EDLCPICYAH PISAVFQPCG HKSCKACINQ HLMNNKDCFF CKTTIVSVED
1310
WEKGANTSTT SSAA
Length:1,314
Mass (Da):148,515
Last modified:November 23, 2004 - v1
Checksum:iA0F8F4D68EAFB8E1
GO
Isoform 2 (identifier: Q5XPI4-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1295-1314: IVSVEDWEKGANTSTTSSAA → TSNLLACLYPHWWEPSHGPNCA

Show »
Length:1,316
Mass (Da):148,958
Checksum:i5E69B97B9A0C61F5
GO

Sequence cautioni

The sequence BAB14139.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence BAB15607.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti809 – 8091K → R in BAB14139 (PubMed:14702039).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti51 – 511P → R.
Corresponds to variant rs2960546 [ dbSNP | Ensembl ].
VAR_027561
Natural varianti387 – 3871R → Q.
Corresponds to variant rs35620248 [ dbSNP | Ensembl ].
VAR_052106
Natural varianti596 – 5961K → E.
Corresponds to variant rs35726701 [ dbSNP | Ensembl ].
VAR_052107
Natural varianti854 – 8541R → H.2 Publications
Corresponds to variant rs34823813 [ dbSNP | Ensembl ].
VAR_052108

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1295 – 131420IVSVE…TSSAA → TSNLLACLYPHWWEPSHGPN CA in isoform 2. 1 PublicationVSP_020650Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY744152 mRNA. Translation: AAU93470.1.
AC099668 Genomic DNA. No translation available.
BC041145 mRNA. Translation: AAH41145.1.
BC057392 mRNA. Translation: AAH57392.2.
BC088801 mRNA. Translation: AAH88801.1.
BC130632 mRNA. Translation: AAI30633.1.
AF370367 mRNA. Translation: AAQ15203.1.
AK022627 mRNA. Translation: BAB14139.1. Different initiation.
AK026968 mRNA. Translation: BAB15607.1. Different initiation.
AL136729 mRNA. Translation: CAB66663.2.
CCDSiCCDS33758.1. [Q5XPI4-1]
RefSeqiNP_071347.2. NM_022064.4. [Q5XPI4-1]
XP_006713348.1. XM_006713285.1. [Q5XPI4-1]
XP_011532297.1. XM_011533995.1. [Q5XPI4-1]
UniGeneiHs.553723.

Genome annotation databases

EnsembliENST00000327697; ENSP00000328287; ENSG00000164068. [Q5XPI4-1]
GeneIDi63891.
KEGGihsa:63891.
UCSCiuc003cxh.5. human. [Q5XPI4-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY744152 mRNA. Translation: AAU93470.1.
AC099668 Genomic DNA. No translation available.
BC041145 mRNA. Translation: AAH41145.1.
BC057392 mRNA. Translation: AAH57392.2.
BC088801 mRNA. Translation: AAH88801.1.
BC130632 mRNA. Translation: AAI30633.1.
AF370367 mRNA. Translation: AAQ15203.1.
AK022627 mRNA. Translation: BAB14139.1. Different initiation.
AK026968 mRNA. Translation: BAB15607.1. Different initiation.
AL136729 mRNA. Translation: CAB66663.2.
CCDSiCCDS33758.1. [Q5XPI4-1]
RefSeqiNP_071347.2. NM_022064.4. [Q5XPI4-1]
XP_006713348.1. XM_006713285.1. [Q5XPI4-1]
XP_011532297.1. XM_011533995.1. [Q5XPI4-1]
UniGeneiHs.553723.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2MA6NMR-A1247-1304[»]
ProteinModelPortaliQ5XPI4.
SMRiQ5XPI4. Positions 1244-1304.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi121971. 39 interactions.
IntActiQ5XPI4. 13 interactions.
MINTiMINT-1187266.
STRINGi9606.ENSP00000328287.

PTM databases

iPTMnetiQ5XPI4.
PhosphoSiteiQ5XPI4.

Polymorphism and mutation databases

BioMutaiRNF123.
DMDMi74748090.

Proteomic databases

EPDiQ5XPI4.
MaxQBiQ5XPI4.
PaxDbiQ5XPI4.
PeptideAtlasiQ5XPI4.
PRIDEiQ5XPI4.

Protocols and materials databases

DNASUi63891.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000327697; ENSP00000328287; ENSG00000164068. [Q5XPI4-1]
GeneIDi63891.
KEGGihsa:63891.
UCSCiuc003cxh.5. human. [Q5XPI4-1]

Organism-specific databases

CTDi63891.
GeneCardsiRNF123.
HGNCiHGNC:21148. RNF123.
MIMi614472. gene.
neXtProtiNX_Q5XPI4.
PharmGKBiPA134916827.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2242. Eukaryota.
KOG4692. Eukaryota.
ENOG410XQ4V. LUCA.
GeneTreeiENSGT00530000063442.
HOVERGENiHBG079909.
InParanoidiQ5XPI4.
KOiK12169.
OMAiAVMMYNL.
PhylomeDBiQ5XPI4.
TreeFamiTF313546.

Enzyme and pathway databases

UniPathwayiUPA00143.
ReactomeiR-HSA-983168. Antigen processing: Ubiquitination & Proteasome degradation.

Miscellaneous databases

GeneWikiiRNF123.
GenomeRNAii63891.
PROiQ5XPI4.
SOURCEiSearch...

Gene expression databases

BgeeiQ5XPI4.
CleanExiHS_RNF123.
ExpressionAtlasiQ5XPI4. baseline and differential.
GenevisibleiQ5XPI4. HS.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR001870. B30.2/SPRY.
IPR013320. ConA-like_dom.
IPR003877. SPRY_dom.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PfamiPF00622. SPRY. 1 hit.
[Graphical view]
SMARTiSM00184. RING. 1 hit.
SM00449. SPRY. 1 hit.
[Graphical view]
SUPFAMiSSF49899. SSF49899. 1 hit.
PROSITEiPS50188. B302_SPRY. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cytoplasmic ubiquitin ligase KPC regulates proteolysis of p27(Kip1) at G1 phase."
    Kamura T., Hara T., Matsumoto M., Ishida N., Okumura F., Hatakeyama S., Yoshida M., Nakayama K., Nakayama K.
    Nat. Cell Biol. 6:1229-1235(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBUNIT, SUBCELLULAR LOCATION.
  2. "The DNA sequence, annotation and analysis of human chromosome 3."
    Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J.
    , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
    Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT HIS-854.
    Tissue: Brain, Eye, Lung and Uterus.
  4. "Large-scale cDNA transfection screening for genes related to cancer development and progression."
    Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H., Qiu X., Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y., Shu H., Chen X.
    , Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S., Gu J.
    Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 545-1314 (ISOFORM 1).
  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 535-1314 (ISOFORMS 1 AND 2), VARIANT HIS-854.
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 892-1314 (ISOFORM 1).
    Tissue: Testis.
  7. "Role of the UBL-UBA protein KPC2 in degradation of p27 at G1 phase of the cell cycle."
    Hara T., Kamura T., Kotoshiba S., Takahashi H., Fujiwara K., Onoyama I., Shirakawa M., Mizushima N., Nakayama K.
    Mol. Cell. Biol. 25:9292-9303(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBUNIT.
  8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiRN123_HUMAN
AccessioniPrimary (citable) accession number: Q5XPI4
Secondary accession number(s): A1L4Q3
, A6NLS5, Q5I022, Q6PFW4, Q71RH0, Q8IW18, Q9H0M8, Q9H5L8, Q9H9T2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 3, 2006
Last sequence update: November 23, 2004
Last modified: July 6, 2016
This is version 124 of the entry and version 1 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 3
    Human chromosome 3: 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

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 one 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.