Ubiquitin carboxyl-terminal hydrolase 19

UniProt data

UniProt name: UBP19_HUMAN (O94966)

Gene name: USP19; Synonyms=KIAA0891, ZMYND9

Organism: Homo sapiens (Human).

Function: 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. Regulates the stability of BIRC2/c-IAP1 and BIRC3/c-IAP2 by preventing their ubiquitination. Required for cells to mount an appropriate response to hypoxia and rescues HIF1A from degradation in a non- catalytic manner. 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. Exhibits a preference towards 'Lys-63'-linked Ubiquitin chains. {ECO:0000269|PubMed:19465887, ECO:0000269|PubMed:21849505, ECO:0000269|PubMed:22128162, ECO:0000269|PubMed:22689415}.

Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:19465887}; Single-pass membrane protein {ECO:0000269|PubMed:19465887}.

Transmembrane domains:

  1. 1292-1312, 21 AA, Helical. {ECO:0000255}.

Sequence: 1318 AA

10 20 30 40 50 60 MSGGASATGP RRGPPGLEDT TSKKKQKDRA NQESKDGDPR KETGSRYVAQ AGLEPLASGD 70 80 90 100 110 120 PSASASHAAG ITGSRHRTRL FFPSSSGSAS TPQEEQTKEG ACEDPHDLLA TPTPELLLDW 130 140 150 160 170 180 RQSAEEVIVK LRVGVGPLQL EDVDAAFTDT DCVVRFAGGQ QWGGVFYAEI KSSCAKVQTR 190 200 210 220 230 240 KGSLLHLTLP KKVPMLTWPS LLVEADEQLC IPPLNSQTCL LGSEENLAPL AGEKAVPPGN 250 260 270 280 290 300 DPVSPAMVRS RNPGKDDCAK EEMAVAADAA TLVDEPESMV NLAFVKNDSY EKGPDSVVVH 310 320 330 340 350 360 VYVKEICRDT SRVLFREQDF TLIFQTRDGN FLRLHPGCGP HTTFRWQVKL RNLIEPEQCT 370 380 390 400 410 420 FCFTASRIDI CLRKRQSQRW GGLEAPAARV GGAKVAVPTG PTPLDSTPPG GAPHPLTGQE 430 440 450 460 470 480 EARAVEKDKS KARSEDTGLD SVATRTPMEH VTPKPETHLA SPKPTCMVPP MPHSPVSGDS 490 500 510 520 530 540 VEEEEEEEKK VCLPGFTGLV NLGNTCFMNS VIQSLSNTRE LRDFFHDRSF EAEINYNNPL 550 560 570 580 590 600 GTGGRLAIGF AVLLRALWKG THHAFQPSKL KAIVASKASQ FTGYAQHDAQ EFMAFLLDGL 610 620 630 640 650 660 HEDLNRIQNK PYTETVDSDG RPDEVVAEEA WQRHKMRNDS FIVDLFQGQY KSKLVCPVCA 670 680 690 700 710 720 KVSITFDPFL YLPVPLPQKQ KVLPVFYFAR EPHSKPIKFL VSVSKENSTA SEVLDSLSQS 730 740 750 760 770 780 VHVKPENLRL AEVIKNRFHR VFLPSHSLDT VSPSDTLLCF ELLSSELAKE RVVVLEVQQR 790 800 810 820 830 840 PQVPSVPISK CAACQRKQQS EDEKLKRCTR CYRVGYCNQL CQKTHWPDHK GLCRPENIGY 850 860 870 880 890 900 PFLVSVPASR LTYARLAQLL EGYARYSVSV FQPPFQPGRM ALESQSPGCT TLLSTGSLEA 910 920 930 940 950 960 GDSERDPIQP PELQLVTPMA EGDTGLPRVW AAPDRGPVPS TSGISSEMLA SGPIEVGSLP 970 980 990 1000 1010 1020 AGERVSRPEA AVPGYQHPSE AMNAHTPQFF IYKIDSSNRE QRLEDKGDTP LELGDDCSLA 1030 1040 1050 1060 1070 1080 LVWRNNERLQ EFVLVASKEL ECAEDPGSAG EAARAGHFTL DQCLNLFTRP EVLAPEEAWY 1090 1100 1110 1120 1130 1140 CPQCKQHREA SKQLLLWRLP NVLIVQLKRF SFRSFIWRDK INDLVEFPVR NLDLSKFCIG 1150 1160 1170 1180 1190 1200 QKEEQLPSYD LYAVINHYGG MIGGHYTACA RLPNDRSSQR SDVGWRLFDD STVTTVDESQ 1210 1220 1230 1240 1250 1260 VVTRYAYVLF YRRRNSPVER PPRAGHSEHH PDLGPAAEAA ASQASRIWQE LEAEEEPVPE 1270 1280 1290 1300 1310 GSGPLGPWGP QDWVGPLPRG PTTPDEGCLR YFVLGTVAAL VALVLNVFYP LVSQSRWR

CATM prediction

The sequence of UBP19_HUMAN returned 2 potential models

The positions at the dimer's interface are highlighted in yellow. The position at the crossing point is highlighted in orange.

# Sequence and interface d θ Z' ω' Score
   1290      1300      1310  
 |    +    |    +    |    +
(Å) (°) (Å) (°)  
LRYFVLGTVAALVALVLNVFYALVSQS 6.9 -40.0° 4.5 44.0 -25.2
LRYFVLGTVAALVALVLNVFYALVSQS 7.0 -42.0° 1.9 33.4 -4.6
LRYFVLGTVAALVALVLNVFYPLVSQS          

* Note: this sequence contains Pro residues. CATM substituted them with Ala during the modeling. The positions are marked.

Click on the model number to visualize its details below.

MODEL 1 DETAILS

Precited structure:


Click on the image to enlarge

Download model 1 structure: PDB, PyMOL session

List of hydrogen bonds:

Donor Acceptor Distance
B, 1295, GLY, HA1 A, 1292, PHE, O 3.10Å
A, 1295, GLY, HA1 B, 1292, PHE, O 3.10Å