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Protein

Ubiquitin carboxyl-terminal hydrolase 19

Gene

Usp19

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Deubiquitinating enzyme that regulates the degradation of various proteins. Deubiquitinates and prevents proteasomal degradation of RNF123 which in turn stimulates CDKN1B ubiquitin-dependent degradation thereby playing a role in cell proliferation. Involved in decreased protein synthesis in atrophying skeletal muscle. Modulates transcription of major myofibrillar proteins. Also involved in turnover of endoplasmic-reticulum-associated degradation (ERAD) substrates (By similarity). Regulates the stability of BIRC2/c-IAP1 and BIRC3/c-IAP2 by preventing thier ubiquitination. Required for cells to mount an appropriate response to hypoxia and rescues HIF1A from degradation in a non-catalytic manner. Exhibits a preference towards 'Lys-63'-linked Ubiquitin chains (By similarity). Plays an important role in 17 beta-estradiol (E2)-inhibited myogenesis. Decreases the levels of ubiquitinated proteins during skeletal muscle formation and acts to repress myogenesis.By similarity1 Publication

Catalytic activityi

Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei548 – 5481NucleophilePROSITE-ProRule annotation
Active sitei1207 – 12071Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri833 – 87543MYND-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  1. cysteine-type endopeptidase activity Source: GO_Central
  2. metal ion binding Source: UniProtKB-KW
  3. ubiquitin-specific protease activity Source: UniProtKB

GO - Biological processi

  1. ER-associated ubiquitin-dependent protein catabolic process Source: UniProtKB
  2. negative regulation of skeletal muscle tissue development Source: UniProtKB
  3. positive regulation of cell cycle process Source: UniProtKB
  4. protein deubiquitination Source: UniProtKB
  5. regulation of cellular response to hypoxia Source: UniProtKB
  6. regulation of proteasomal protein catabolic process Source: GO_Central
  7. regulation of protein stability Source: UniProtKB
  8. response to endoplasmic reticulum stress Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Thiol protease

Keywords - Biological processi

Ubl conjugation pathway

Keywords - Ligandi

Metal-binding, Zinc

Protein family/group databases

MEROPSiC19.024.

Names & Taxonomyi

Protein namesi
Recommended name:
Ubiquitin carboxyl-terminal hydrolase 19 (EC:3.4.19.12)
Alternative name(s):
Deubiquitinating enzyme 19
Ubiquitin thioesterase 19
Ubiquitin-specific-processing protease 19
Gene namesi
Name:Usp19
Synonyms:Kiaa0891
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 9

Organism-specific databases

MGIiMGI:1918722. Usp19.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 13331333CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei1334 – 135421HelicalSequence AnalysisAdd
BLAST
Topological domaini1355 – 13606LumenalSequence Analysis

GO - Cellular componenti

  1. cytosol Source: UniProtKB
  2. endoplasmic reticulum membrane Source: UniProtKB
  3. integral component of membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 13601360Ubiquitin carboxyl-terminal hydrolase 19PRO_0000295157Add
BLAST

Proteomic databases

MaxQBiQ3UJD6.
PaxDbiQ3UJD6.
PRIDEiQ3UJD6.

PTM databases

PhosphoSiteiQ3UJD6.

Expressioni

Inductioni

Up-regulated by ESR1 in the presence of 17 beta-estradiol (E2).1 Publication

Gene expression databases

BgeeiQ3UJD6.
CleanExiMM_USP19.
ExpressionAtlasiQ3UJD6. baseline and differential.
GenevestigatoriQ3UJD6.

Interactioni

Subunit structurei

Interacts with and stabilizes RNF123 (By similarity). Interacts with BIRC2/c-IAP1, BIRC3/c-IAP2 and XIAP/BIRC4. Interacts with HIF1A (via N-terminus) (By similarity).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
FKBP6O753442EBI-9359023,EBI-744771From a different organism.

Protein-protein interaction databases

BioGridi214730. 3 interactions.
IntActiQ3UJD6. 26 interactions.

Structurei

3D structure databases

ProteinModelPortaliQ3UJD6.
SMRiQ3UJD6. Positions 306-444, 536-719, 1038-1257.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini51 – 14090CS 1PROSITE-ProRule annotationAdd
BLAST
Domaini322 – 424103CS 2PROSITE-ProRule annotationAdd
BLAST
Domaini539 – 1256718USPAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi524 – 5307Poly-Glu

Sequence similaritiesi

Contains 2 CS domains.PROSITE-ProRule annotation
Contains 1 MYND-type zinc finger.PROSITE-ProRule annotation
Contains 1 USP domain.Curated

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri833 – 87543MYND-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Repeat, Transmembrane, Transmembrane helix, Zinc-finger

Phylogenomic databases

eggNOGiCOG5560.
GeneTreeiENSGT00670000097750.
HOGENOMiHOG000074206.
HOVERGENiHBG061889.
InParanoidiQ3UJD6.
KOiK11847.
OMAiQASRIWQ.
PhylomeDBiQ3UJD6.
TreeFamiTF106276.

Family and domain databases

Gene3Di2.60.40.790. 2 hits.
InterProiIPR007052. CS_dom.
IPR008978. HSP20-like_chaperone.
IPR001394. Peptidase_C19_UCH.
IPR018200. USP_CS.
IPR028889. USP_dom.
IPR002893. Znf_MYND.
[Graphical view]
PfamiPF04969. CS. 2 hits.
PF00443. UCH. 1 hit.
PF01753. zf-MYND. 1 hit.
[Graphical view]
SUPFAMiSSF49764. SSF49764. 2 hits.
PROSITEiPS51203. CS. 2 hits.
PS00972. USP_1. 1 hit.
PS00973. USP_2. 1 hit.
PS50235. USP_3. 1 hit.
PS01360. ZF_MYND_1. 1 hit.
PS50865. ZF_MYND_2. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

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

Isoform 1 (identifier: Q3UJD6-1) [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
MSAGASATGP RRGPPGLEEA TSKKKQKDRA NLESKDGDAR RVSLPRKEPT
60 70 80 90 100
KDELLLDWRQ SADEVIVKLR VGTGPVRLED VDAAFTDTDC VVRLPDGRQW
110 120 130 140 150
GGVFFAEIQS SCTKVQARKG GLLQLVLPKK VPLLTWPSLL KPLGTQELVP
160 170 180 190 200
GLQCQENGQE LSPIALEPGS EPRRAKQEAR NQKRAQGRGE VGSGAGPGTQ
210 220 230 240 250
AGPSAKRAVH LRRGPEGEGS MDGPGPQGDA PSFLSDSATQ VEAEEKLCAP
260 270 280 290 300
PMNTQTSLLS SEKSLALLTV EKTVSPRNDP VAPVMVQDRD PEPEQEDQVK
310 320 330 340 350
EEMALGADPT ALVEEPESMV NLAFVKNDSY EKGPDSVVVH VYVKEIRRDS
360 370 380 390 400
SRVLFREQDF TLIFQTRDGN FLRLHPGCGP HTIFRWQVKL RNLIEPEQCT
410 420 430 440 450
FCFTASRIDI CLRKRQSQRW GGLEAPATRG AVGGAKVAVP TGPTPLDSTP
460 470 480 490 500
PGGGPHPLTG QEEARAVEKE KPKARSEDSG LDGVVARTPL EHVAPKPDPH
510 520 530 540 550
LASPKPTCMV PPMPHSPVSG DSVEEDEEEE KKVCLPGFTG LVNLGNTCFM
560 570 580 590 600
NSVIQSLSNT RELRDFFHDR SFEAEINYNN PLGTGGRLAI GFAVLLRALW
610 620 630 640 650
KGTHQAFQPS KLKAIVASKA SQFTGYAQHD AQEFMAFLLD GLHEDLNRIQ
660 670 680 690 700
NKPYTETVDS DGRPDEVVAE EAWQRHKMRN DSFIVDLFQG QYKSKLVCPV
710 720 730 740 750
CAKVSITFDP FLYLPVPLPQ KQKVLPIFYF AREPHSKPIK FLVSVSKENS
760 770 780 790 800
SASEVLDSLS QSVHVKPENL RLAEVIKNRF HRVFLPSHSL DAVSPTDVLL
810 820 830 840 850
CFELLSPELA KERVVVLEVQ QRPQVPSIPI SKCAACQRKQ QSEEEKLKRC
860 870 880 890 900
TRCYRVGYCN QFCQKTHWPD HKGLCRPENI GYPFLVSVPA SRLTYARLAQ
910 920 930 940 950
LLEGYARYSV SVFQPPFQPG RMALESQSPG CTTLLSTSSL EAGDSEREPI
960 970 980 990 1000
QPSELQLVTP VAEGDTGAHR VWPPADRGPV PSTSGLSSEM LASGPIEGCP
1010 1020 1030 1040 1050
LLAGERVSRP EAAVPGYQHS SESVNTHTPQ FFIYKIDASN REQRLEDKGE
1060 1070 1080 1090 1100
TPLELGDDCS LALVWRNNER LQEFVLVASK ELECAEDPGS AGEAARAGHF
1110 1120 1130 1140 1150
TLDQCLNLFT RPEVLAPEEA WYCPQCKQHR EASKQLLLWR LPNVLIVQLK
1160 1170 1180 1190 1200
RFSFRSFIWR DKINDLVEFP VRNLDLSKFC IGQKEEQLPS YDLYAVINHY
1210 1220 1230 1240 1250
GGMIGGHYTA CARLPNDRSS QRSDVGWRLF DDSTVTTVDE SQVVTRYAYV
1260 1270 1280 1290 1300
LFYRRRNSPV ERPPRASHSE HHPDLGPAAE AAASQASRIW QELEAEEEMV
1310 1320 1330 1340 1350
PEGPGPLGPW GPQDWVGPPP RGPTTPDEGC LRYFVLGTVA ALVALVLNVF
1360
YPLVSQSRWR
Length:1,360
Mass (Da):150,549
Last modified:October 11, 2005 - v1
Checksum:iFE9C3020D2CD9AED
GO
Isoform 2 (identifier: Q3UJD6-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1286-1340: ASRIWQELEA...LRYFVLGTVA → GLGPGQAPEV...PTYSNMEEVD
     1341-1360: Missing.

Show »
Length:1,323
Mass (Da):146,283
Checksum:i73E85AA9778738F7
GO

Sequence cautioni

The sequence BAC65678.4 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti140 – 1401L → LK in BAE42739 (PubMed:16141072).Curated
Sequence conflicti142 – 1421P → S in AAH60613 (PubMed:15489334).Curated
Sequence conflicti430 – 4312Missing in BAE42739 (PubMed:16141072).Curated
Sequence conflicti669 – 6691A → T in BAE42739 (PubMed:16141072).Curated
Sequence conflicti1058 – 10581D → E in BAE42739 (PubMed:16141072).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1286 – 134055ASRIW…LGTVA → GLGPGQAPEVAPTRTAPERF APPVDRPAPTYSNMEEVD in isoform 2. 3 PublicationsVSP_026769Add
BLAST
Alternative sequencei1341 – 136020Missing in isoform 2. 3 PublicationsVSP_026770Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK122396 mRNA. Translation: BAC65678.4. Different initiation.
AK146504 mRNA. Translation: BAE27219.1.
AK160807 mRNA. Translation: BAE36025.1.
AK171942 mRNA. Translation: BAE42739.1.
BC046824 mRNA. Translation: AAH46824.1.
BC060613 mRNA. Translation: AAH60613.1.
CCDSiCCDS23529.1. [Q3UJD6-1]
CCDS52924.1. [Q3UJD6-2]
RefSeqiNP_001161843.1. NM_001168371.2.
NP_001161844.1. NM_001168372.2. [Q3UJD6-2]
NP_001161845.1. NM_001168373.2.
NP_082080.3. NM_027804.4. [Q3UJD6-1]
NP_663382.2. NM_145407.3.
UniGeneiMm.289706.

Genome annotation databases

EnsembliENSMUST00000006854; ENSMUSP00000006854; ENSMUSG00000006676. [Q3UJD6-1]
ENSMUST00000085044; ENSMUSP00000082119; ENSMUSG00000006676. [Q3UJD6-2]
GeneIDi71472.
KEGGimmu:71472.
UCSCiuc009rpt.2. mouse. [Q3UJD6-1]
uc009rpu.2. mouse. [Q3UJD6-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK122396 mRNA. Translation: BAC65678.4. Different initiation.
AK146504 mRNA. Translation: BAE27219.1.
AK160807 mRNA. Translation: BAE36025.1.
AK171942 mRNA. Translation: BAE42739.1.
BC046824 mRNA. Translation: AAH46824.1.
BC060613 mRNA. Translation: AAH60613.1.
CCDSiCCDS23529.1. [Q3UJD6-1]
CCDS52924.1. [Q3UJD6-2]
RefSeqiNP_001161843.1. NM_001168371.2.
NP_001161844.1. NM_001168372.2. [Q3UJD6-2]
NP_001161845.1. NM_001168373.2.
NP_082080.3. NM_027804.4. [Q3UJD6-1]
NP_663382.2. NM_145407.3.
UniGeneiMm.289706.

3D structure databases

ProteinModelPortaliQ3UJD6.
SMRiQ3UJD6. Positions 306-444, 536-719, 1038-1257.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi214730. 3 interactions.
IntActiQ3UJD6. 26 interactions.

Protein family/group databases

MEROPSiC19.024.

PTM databases

PhosphoSiteiQ3UJD6.

Proteomic databases

MaxQBiQ3UJD6.
PaxDbiQ3UJD6.
PRIDEiQ3UJD6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000006854; ENSMUSP00000006854; ENSMUSG00000006676. [Q3UJD6-1]
ENSMUST00000085044; ENSMUSP00000082119; ENSMUSG00000006676. [Q3UJD6-2]
GeneIDi71472.
KEGGimmu:71472.
UCSCiuc009rpt.2. mouse. [Q3UJD6-1]
uc009rpu.2. mouse. [Q3UJD6-2]

Organism-specific databases

CTDi10869.
MGIiMGI:1918722. Usp19.
RougeiSearch...

Phylogenomic databases

eggNOGiCOG5560.
GeneTreeiENSGT00670000097750.
HOGENOMiHOG000074206.
HOVERGENiHBG061889.
InParanoidiQ3UJD6.
KOiK11847.
OMAiQASRIWQ.
PhylomeDBiQ3UJD6.
TreeFamiTF106276.

Miscellaneous databases

ChiTaRSiUsp19. mouse.
NextBioi333851.
PROiQ3UJD6.
SOURCEiSearch...

Gene expression databases

BgeeiQ3UJD6.
CleanExiMM_USP19.
ExpressionAtlasiQ3UJD6. baseline and differential.
GenevestigatoriQ3UJD6.

Family and domain databases

Gene3Di2.60.40.790. 2 hits.
InterProiIPR007052. CS_dom.
IPR008978. HSP20-like_chaperone.
IPR001394. Peptidase_C19_UCH.
IPR018200. USP_CS.
IPR028889. USP_dom.
IPR002893. Znf_MYND.
[Graphical view]
PfamiPF04969. CS. 2 hits.
PF00443. UCH. 1 hit.
PF01753. zf-MYND. 1 hit.
[Graphical view]
SUPFAMiSSF49764. SSF49764. 2 hits.
PROSITEiPS51203. CS. 2 hits.
PS00972. USP_1. 1 hit.
PS00973. USP_2. 1 hit.
PS50235. USP_3. 1 hit.
PS01360. ZF_MYND_1. 1 hit.
PS50865. ZF_MYND_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Prediction of the coding sequences of mouse homologues of KIAA gene: II. The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
    Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S., Nakajima D., Nagase T., Ohara O., Koga H.
    DNA Res. 10:35-48(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Fetal brain.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
    Strain: C57BL/6J and NOD.
    Tissue: Head, Kidney and Spleen.
  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), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 395-1360 (ISOFORM 2).
    Strain: C57BL/6.
    Tissue: Brain.
  4. "17beta-estradiol represses myogenic differentiation by increasing ubiquitin-specific peptidase 19 through estrogen receptor alpha."
    Ogawa M., Yamaji R., Higashimura Y., Harada N., Ashida H., Nakano Y., Inui H.
    J. Biol. Chem. 286:41455-41465(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INDUCTION.

Entry informationi

Entry nameiUBP19_MOUSE
AccessioniPrimary (citable) accession number: Q3UJD6
Secondary accession number(s): Q3TAC9
, Q3TUE6, Q6P9T0, Q80TP5, Q80ZW5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 10, 2007
Last sequence update: October 11, 2005
Last modified: March 4, 2015
This is version 85 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. 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.