wanglab/gogpt-training-data huggingface dataset:
Protein: Large ribosomal subunit protein uL1B (60S ribosomal protein L1-B) (L10a) (O74836)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Large ribosomal subunit protein uL24
- Large ribosomal subunit protein uL29
- Large ribosomal subunit protein eL6
- Large ribosomal subunit protein eL14
- Large ribosomal subunit protein eL31
- Large ribosomal subunit protein eL13
- Large ribosomal subunit protein uL10
- Large ribosomal subunit protein eL28
- Large ribosomal subunit protein uL30C
- Large ribosomal subunit protein eL29
Sequence:
MSKVSVASVRSNVEQILKGSEEKKRNFTETVELQIGLKNYDPQRDKRFSGTIKLPNVPRPNMAICILGDAHDLDRAKHGGVDAMSVDDLKKLNKNKKLVKKLAKKYDAFIASEVLIKQIPRLLGPGLSKAGKFPSPVSHADDLYGKITEVKSTIKFQLKKVLCLGVAVGHVEMSEEQLIANIMLAVNFLVSLLKKGWQNIGSLVVKSTMGKPHRLY
Protein: Glutathione peroxidase (Q869A7)
Organism: Trypanosoma brucei
Interaction partners:
Sequence:
MSTIFDFEVLDADHKPYNLVQHKGSPLLIYNVASKCGYTKGGYETATALYNKYKSQGFTVLVFPCNEFGGQEAGNEEEIKEFVCTKFKAEFPIMAKINVNGENAHPLYEYMKKTKPGILATKAIKWNFTSFLIDRDGVPVERFSPGASVKDIEEKLIPLLESTQSA
Protein: Peptidyl-prolyl cis-trans isomerase A (PPIase A) (EC 5.2.1.8) (Cyclophilin A) (Cyclosporin A-binding protein) (Rotamase A) [Cleaved into: Peptidyl-prolyl cis-trans isomerase A, N-terminally processed] (P14851)
Organism: Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus)
Function: Catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides (By similarity). Exerts a strong chemotactic effect on leukocytes partly through activation of one of its membrane receptors BSG/CD147, initiating a signaling cascade that culminates in MAPK/ERK activation (By similarity). Activates endothelial cells (ECs) in a proinflammatory manner by stimulating activation of NF-kappa-B and ERK, JNK and p38 MAP-kinases and by inducing expression of adhesion molecules including SELE and VCAM1 (By similarity). Induces apoptosis in ECs by promoting the FOXO1-dependent expression of CCL2 and BCL2L11 which are involved in EC chemotaxis and apoptosis (By similarity). In response to oxidative stress, initiates proapoptotic and antiapoptotic signaling in ECs via activation of NF-kappa-B and AKT1 and up-regulation of antiapoptotic protein BCL2 (By similarity). Negatively regulates MAP3K5/ASK1 kinase activity, autophosphorylation and oxidative stress-induced apoptosis mediated by MAP3K5/ASK1 (By similarity). Necessary for the assembly of TARDBP in heterogeneous nuclear ribonucleoprotein (hnRNP) complexes and regulates TARDBP binding to RNA UG repeats and TARDBP-dependent expression of HDAC6, ATG7 and VCP which are involved in clearance of protein aggregates (By similarity). Plays an important role in platelet activation and aggregation (By similarity). Regulates calcium mobilization and integrin ITGA2B:ITGB3 bidirectional signaling via increased ROS production as well as by facilitating the interaction between integrin and the cell cytoskeleton (By similarity). Binds heparan sulfate glycosaminoglycans (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P62937}. Secreted {ECO:0000250|UniProtKB:P62937}. Nucleus {ECO:0000250|UniProtKB:P62937}. Note=Secretion occurs in response to oxidative stress in vascular smooth muscle through a vesicular secretory pathway that involves actin remodeling and myosin II activation, and mediates ERK1/2 activation. {ECO:0000250|UniProtKB:P62937}.
Interaction partners:
Sequence:
MVNPTVFFDISADGEPLGRVSFELFADKVPKTAENFRALSTGEKGFGYKGSSFHRIIPGFMCQGGDFTRHNGTGGRSIYGEKFEDENFILKHTGPGILSMANAGPNTNGSQFFICTAKTEWLDGKHVVFGKVKEGMNIVEAMERFGSRNGKTSKKITISDCGQL
Protein: C2 NT-type domain-containing protein (Q57W90)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- C2 NT-type domain-containing protein
Sequence:
MPLYNITIHPLKLAAHFCKQGCSYVVVVNRKGVELATKPAMCTVADEVAFSTPAELNQTRTFQLAFDSPKDRRMIQFAMYDVTNPKHSIRITGFEIPLAGMCSVLAGESICERKAVSFRISGRPGRLDVIFRMHPTTSPVPPLTLYAGPATGSGGSSSPVETVRLPARTVEVLKKVGVLPKDVEEVEVDAVIAQEVVVRTSMLFPSEAELRERVMTLEREVAQQEYSVRYASKDSVSSGSAACVALRSELQYWKDTVERVNLQSAQETGIALLLKAGEEGEHDDGSRALIADVEGQLEEARRELKTIERSQNDEELNTKLIPLLGQVEQLEELLEHLRKEVHVPPKTAGSSEKADVVDQWEQLARELFDKELMVEQLMHTVLTLNQLQFEPYPAAIEMGAVGDTPCELQFVRDNKRQLKNLPQVPTPKQATDLAAASGGPTSDNLLNDLFGCPSPPKPVPQPTVQADEVTSQPHFERENGGLPGAPSVFSSGVAPIWGQKPVGAPPQDDAMQPAATANTLDTTDGKVGDSMAFEKKTTEPQIMVSAGLAAAAASPPDTQNGQQLSFPFDSKQQGPTQGQQQPFPFDSKQQGPTQGQQQPFPFDSKQQGPTQGQQQPFPLGSQQQGPTQGQQQPFPFDSKQQGPTQGQQQPFPLGSQQQGPTQGQQQPFPFDSKQQGPTQGQQQPFPFDSKQQGPTQGQQQPFPFDSKQQGPTQGQQQPFPLGSQQQGPTQGQQQPFPLGSQQQGPTQGQQQPFPFDSKQQGPTQGQQQPFPFDSKQQGPTQGQQQPFPFDSKQQGPTQGQQQPFPLGSQQQGPTQGQQQPFPFDSKQQGPTQGQQQPFPFDSKQQGPTQGQQQPFPFDSKQQGPTQGQQQPFPLGSQQQGPTQGQQQPFPFDSKQQGPTQGQQQPFPFDSKQQGPTQGQQQPFPLGSQQQGPTQGQQQPFPFDSKQQGPTQGQQQPFPFDSKQQGPTQGQQQPFPLGSQQQGPTQGQQQPFPFDSKQQGPTQGQQQPFPLGSQQQGPTQGQQQPFPLGSQQQGPTQGQQQSFPFDSKQQGPTQGQQQPFPFDSKQQGPTQGQQQPFPFDSKQQGPTQGQQQPFPLGSQQQGPTQGQQQPFPLGSQQQGPTQGQQQPFPFDSKQQGVPQTPSVPGQQQQYMAPPETPVPRYVRRPLASGVSPFAPFINIPLVARACPLDIYLDGQTPTRGTEITIQNNGGFDITIGGVELRQEDMTSTSPHAGQTVPIRRWPQQMHVPRGGGRATCIIALHPSYARGSSLILLVVVYVLNEGRYTPFAARFPV
Protein: Bud site selection protein 8 (P41698)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: May be involved in positioning the distal bud pole signal.
Subcellular location: Cell membrane {ECO:0000269|PubMed:11514631, ECO:0000269|PubMed:15356260, ECO:0000269|PubMed:20678480, ECO:0000269|PubMed:21625000}; Multi-pass membrane protein {ECO:0000255}. Bud tip {ECO:0000269|PubMed:11514631, ECO:0000269|PubMed:15356260, ECO:0000269|PubMed:20678480, ECO:0000269|PubMed:21625000}. Note=Found at presumptive bud sites, bud tips, and the distal poles of daughter cells. {ECO:0000269|PubMed:11514631, ECO:0000269|PubMed:20678480, ECO:0000269|PubMed:21625000}.
Interaction partners:
- Bud site selection protein RAX1
- Bud site selection protein RAX2
- Bud site selection protein 5
- Bud site selection protein 9
- Inhibitory regulator protein BUD2/CLA2
- Ras-related protein RSR1
Sequence:
MIQSDEDNLDSSETTASTSYSGTSSVSSRLQLRTSLFFENLNGAHGNPDAETEMATVAYETTSRGQGFAVYINNERFSQIMGASTSSSSSSNSSSITQFHDTQDNNIPSNTTVRPTSLRRDNEDTVPLRNVTPSQNAAVRPERAVNSPSSQRLSCALTISTSVLMGEDVEGSPIEQEHSRVVSSLYSSLANRGNDESKNGTPPRPTSIEPNETTEHSFFSYHYDDTLEPDVEEAVRLTKNKTSNVNFISSTGSKGEGETEDEVIDQYEPVNESKFIPHKLKIPEKAGSIKSSTSDDSHSPGAPGTSARKIKIPQSPSLIGNILIPSHNSDSSNESSPKDHIGHNNEEKFSSKSTRKPSTSLEEEGPPIGLPSIPVLRSVSGPSKWTKTPLRLESGNSTKSDPFSRYEGHKTPSPLTKMNKKKNKTLPEHGQPLVLAPIKSQSSESDTGQNSIIEKPARSIRRKQQEKTDNRKEDRHDAENIDLEARMPIQHIDTASIHSFDSGQNGFRDVYSIENIIVILLCCSIVPPLFFIIGCSSRRKLVSDYRLMRLLMNKEHRAALLQGFIWDVDLRWFRMFCLILGAAETVIVMAGIAIGFGVGITRE
Protein: DNA-directed RNA polymerase subunit beta'' (EC 2.7.7.6) (PEP) (Plastid-encoded RNA polymerase subunit beta'') (RNA polymerase subunit beta'') (P0C509)
Organism: Oryza sativa subsp. japonica (Rice)
Function: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
Subcellular location: Plastid, chloroplast {ECO:0000255|HAMAP-Rule:MF_01324}.
Interaction partners:
- DNA-directed RNA polymerase subunit beta'
- Os09g0110400 protein
- DNA-directed RNA polymerase subunit alpha
- DNA-directed RNA polymerase subunit
- DNA-directed RNA polymerase I subunit RPA1
- Os12g0540700 protein
- DNA-directed RNA polymerases I and III subunit RPAC1
- Os02g0723600 protein.
- DNA-directed RNA polymerase subunit beta
- Small ribosomal subunit protein uS14c
Sequence:
MAERANLVFQNKEIDGTAMKRLISRLIDHFGMGYTSHILDQIKTLGFHQATTTSISLGIEDLLTIPSKGWLVQDAEQQSFLLEKHYYYGAVHAVEKLRQSVEIWYATSEYLKHEMNSNFRITDPSNPVYLMSFSGARGNASQVHQLVGMRGLMADPQGQMIDLPIQSNLREGLSLTEYIISCYGARKGVVDTAVRTADAGYLTRRLVEVVQHIIVRRRDCGTIQAISVSPQNGMTEKLFVQTLIGRVLANDIYIGSRCIATRNQDIGIGLVNRFITTFRAQPFRAQPIYIRTPFTCRSTSWICQLCYGRSSTHGDLVELGEAVGVIAGQSIGEPGTQLTLRTFHTGGVFTGGTADLVRSPSNGKIQFNGDLVHPTRTRHGQPAFLCYIDLHITIQSQDILHSVTIPSKSLILVQNDQYVESEQVIAEIRAGTSALHFKEKVQKHIYSESDGEMHWSTDVYHAPEYQYGNLRRLPKTSHLWILSVSMCRSSIASFSLHKDQDQMNTYSFSVDGRYIFGLSMADDEVRHRLLDTFGKKDREILDYSTPDRIMSNGHWNFVYPSILQNNFDLLAKKRRNRFAIPLQYHQEQEKEPISCFGISIEIPFMGVLRRNTIVAYFDDPRYKKDKKGSGIVKFRYRTLEDEYRTREKDSENEYGSPENEYRTREEECKTLEDEYRTREEEYETLEDEYGIPENEYETLEDEYGILEDEYRTREEESEDEYGSPENKYRPREDKYGTLEEDSEDEHGTLEEDSEEDSEDEYGNPEEDSVLKKGVLIEHRGTKEFSLKYQKEVDRFFFILQELHILPRSSSLKVLDNSIIGVDTQLTKNTRSRLGGLVRVKRKKSHTELKIFSGDIHFPEEADKILGGSLIPLEREKKDSKESKKRENWVYVQWKKILKSKEKYFVLVRPAVAYEMNEGRNLATLFPQDLLQEEGNLQLRLVNFISHENSKLTQRIYHTNSQFVRTCLVLNWEQEEKEEARASLVEIRANGLIRDFLRIGLIKSTISYTRKRYDSRSAGLILHNRLDRTNTNSFYSKAKIQSLSQHQEAIGTLLNRNKEYQSLMVLSASNCSRIGFFKNSKNPNGVKESNPRIPIPKFWGLFRNFSGLLGTIAPSISNFSSSYYLLTYNQILLKKHLLLDNLKQNFKVLQGLKHSLINENQRTSNFDSNIMLDPFQLNWHFLPHDSWEETSAKIHLGQFICENVCLFKSHIKKSGQIFIVNIDSFVIRAAKPYLATTGATVHGHYGEILYKGDRLVTFIYEKARSSDITQGLPKVEQIFEARSIDSLSPNLERRIEDWNERIPRILGGPWGFLIGAELTIAQSRISLVNKIQKVYRSQGVQIHNRHIEIIIRQVTSKVRVSEDGMSNVFSPGELIGLLRAERAGRALDESIYYRAILLGITRVSLNTQSFISEASFQETARVLAKAALRGRIDWLKGLKENVVLGGIIPVGTGFQKFVHRYPQNKNLYFEIQKKKLFASEMRDILFLHTELVSSDSDVTNNFYETSESPFTPFI
Protein: Rod outer segment membrane protein 1 (ROSP1) (P52205)
Organism: Bos taurus (Bovine)
Function: Plays a role in rod outer segment (ROS) morphogenesis (By similarity). May play a role with PRPH2 in the maintenance of the structure of ROS curved disks. Plays a role in the organization of the ROS and maintenance of ROS disk diameter (By similarity). Involved in the maintenance of the retina outer nuclear layer (By similarity).
Subcellular location: Photoreceptor inner segment membrane {ECO:0000250|UniProtKB:P32958}; Multi-pass membrane protein {ECO:0000255}. Photoreceptor outer segment membrane {ECO:0000269|PubMed:10681511}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Peripherin-2
- Rhodopsin
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Cyclic nucleotide-gated channel beta-1
- Regulator of G-protein signaling 9-binding protein
- Rod cGMP-specific 3',5'-cyclic phosphodiesterase subunit beta
Sequence:
MAPVLPLVLPLQPRIRLAQGLWLLSWLLVLVGGLTLLCSGHLLVQLWHLGTFLAPSCPFSALPQVALAASAVALGTGLVGSGASRASLDAEQYPPWRGVLGPLLVAGTAGGGGLLVLALGLALALPGTLDTGLEEGLGSALVHYKDTEVPGRCQAKRLLDELQLRHHCCGRHGYKDWFGIQWVSNRYLDPNDPDVVDRIQSNVEGLYLIDGVPFSCCNPHSPRPCLQSQLSDPHAHPLFDPRQPNLNLWSQGCHEVLLGHLQGLASTLGNMLAVTFLLQTLVLLGLRYLQTALEGLGGVIDGEGEAQGYLFPAGLKDMLKTAWLQGAGPHRPAPGETPPEEKPPKECLPEA
Protein: U6 snRNA-associated Sm-like protein LSm6 (Q06406)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of LSm protein complexes, which are involved in RNA processing and may function in a chaperone-like manner, facilitating the efficient association of RNA processing factors with their substrates. Component of the cytoplasmic LSM1-LSM7 complex, which is involved in mRNA degradation by activating the decapping step in the 5'-to-3' mRNA decay pathway. In association with PAT1, LSM1-LSM7 binds directly to RNAs near the 3'-end and prefers oligoadenylated RNAs over polyadenylated RNAs. Component of the nuclear LSM2-LSM8 complex, which is involved in splicing of nuclear mRNAs. LSM2-LSM8 associates with multiple snRNP complexes containing the U6 snRNA (U4/U6 di-snRNP, spliceosomal U4/U6.U5 tri-snRNP, and free U6 snRNP). It binds directly to the 3'-terminal U-tract of U6 snRNA and plays a role in the biogenesis and stability of the U6 snRNP and U4/U6 snRNP complexes. LSM2-LSM8 probably also is involved degradation of nuclear pre-mRNA by targeting them for decapping, and in processing of pre-tRNAs, pre-rRNAs and U3 snoRNA. Component of a nucleolar LSM2-LSM7 complex, which associates with the precursor of the RNA component of RNase P (pre-P RNA) and with the small nucleolar RNA (snoRNA) snR5. It may play a role in the maturation of a subset of nucleolus-associated small RNAs.
Subcellular location: Cytoplasm. Nucleus, nucleolus. Note=LSM1 and LSM8 act competitively with respect to the localization of LSM1-LSM7 to the cytoplasm and LSM2-LSM8 to the nucleus. LSm proteins shift to the cytoplasm under conditions of stress.
Interaction partners:
- LSM2-LSM8 complex subunit LSM8
- U2 small nuclear ribonucleoprotein A'
- Small nuclear ribonucleoprotein Sm D3
- LSM complex subunit LSM4
- Pre-mRNA-processing factor 31
- LSM1-LSM7 complex subunit LSM1
- LSM complex subunit LSM2
- 66 kDa U4/U6.U5 small nuclear ribonucleoprotein component
- Deadenylation-dependent mRNA-decapping factor PAT1
- LSM complex subunit LSM7
Sequence:
MSGKASTEGSVTTEFLSDIIGKTVNVKLASGLLYSGRLESIDGFMNVALSSATEHYESNNNKLLNKFNSDVFLRGTQVMYISEQKI
Protein: Protease inhibitor-like protein (Q7YZA1)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MAQCYPQFDSENPWLRPRQPTEPTISPNAGGSTPANAAPPTTQSPRYFACFHSCPATSEYNPICGSDNVNYYNENKFNCALNCGLSEYIGCVPPQIPF
Protein: Aspartate--tRNA(Asp/Asn) ligase (EC 6.1.1.23) (Aspartyl-tRNA synthetase) (AspRS) (Non-discriminating aspartyl-tRNA synthetase) (ND-AspRS) (P9WFW3)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00044}.
Interaction partners:
- Aspartyl/glutamyl-tRNA
- Glutamyl-tRNA
- Glutamate--tRNA ligase
- Leucine--tRNA ligase
- Threonine--tRNA ligase
- Isoleucine--tRNA ligase
- Tyrosine--tRNA ligase
- Histidine--tRNA ligase
- Phenylalanine--tRNA ligase beta subunit
- Methionine--tRNA ligase
Sequence:
MLRSHAAGLLREGDAGQQVTLAGWVARRRDHGGVIFIDLRDASGIAQVVFRDPQDTEVLAQAHRLRAEFCVSVAGVVEIRPEGNANPEIATGEIEVNATSLTVLGECAPLPFQLDEPAGEELRLKYRYLDLRRDDPAAAIRLRSRVNAAARAVLARHDFVEIETPTITRSTPEGARDFLVPARLHPGSFYALPQSPQLFKQLLMVAGMERYYQIARCYRDEDFRADRQPEFTQLDMEMSFVDAEDIIAISEEVLTELWALIGYRIPTPIPRIGYAEAMRRFGTDKPDLRFGLELVECTDFFSDTTFRVFQAPYVGAVVMPGGASQPRRTLDGWQDWAKQRGHRGLAYVLVAEDGTLGGPVAKNLTEAERTGLADHVGAKPGDCIFFSAGPVKSSRALLGAARVEIANRLGLIDPDAWAFVWVVDPPLFEPADEATAAGEVAVGSGAWTAVHHAFTAPKPEWEDRIESDTGSVLADAYDIVCNGHEIGGGSVRIHRRDIQERVFAVMGLDKAEAEEKFGFLLEAFMFGAPPHGGIAFGWDRTTALLAGMDSIREVIAFPKTGGGVDPLTDAPAPITAQQRKESGIDAQPKRVQQA
Protein: ORAI calcium release-activated calcium modulator 2 (F7EZ46)
Organism: Rattus norvegicus (Rat)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
VKEGRTHRHGLVPTMSAELNVPMDPSAPACPEPGHKGMDYRDWVRRSYLELVTSNHHSVQALSWRKLYLSRAKLKASSRTSALLSGFAMVAMVEVQLETKYQYPQPLLIAFSACTTVLVAVHLFALLISTCILPNVEAVSNIHNLNSISESPHERMHPYIELAWGFSTVLGILLFLAEVVLLCWIKFLPVDAKDQPGSHSHTGWQAALVSTIIMVPVGLIFVVFTIHFYRSLVRHKTERHNREIEELHKLKVQLDGHERSLQVV
Protein: DUF2786 domain-containing protein (Q8NNH3)
Organism: Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / BCRC 11384 / CCUG 27702 / LMG 3730 / NBRC 12168 / NCIMB 10025 / NRRL B-2784 / 534)
Interaction partners:
- CHAD domain-containing protein
Sequence:
MTLSHFSDNVTDAQDSYRQILEESIISHLGFCALRGWTPADLRHEFSADIDPLLFHALPEIAYSCSDEMYTLWVNGTRAAETSHLPVMTLEKILTELPKLSTLPDWAMLAELHALDNQDTSPMTPAQAKAHHRITALLKKAESTNFEEEAEALILKAETLRQQYRIESLLINSYDQDVQARSSTIRASRVYLEAPWIRHQYKLLNAIARVHSSEALLITKSGICTLFGEQDDVAHIIDLFNSLNRQRAHFMKTSAGARIAQLNGETSSYRRSFMISYASQISRLLISAKEDAFNELAGQAPLAHSAIVPVLENRSVRSKEALKETFPNMRTMTFKSTNRRGIIDGFNAANESHLGGESASLEDSTFMF
Protein: Dynein light chain (Q387L9)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|RuleBase:RU365010}.
Interaction partners:
- Cytoplasmic dynein 2 light intermediate chain 1
- Kinesin-like protein
- Dynein light chain, putative
- Dynein light chain, putative
- Uncharacterized protein
- Uncharacterized protein
- Dynein light chain roadblock
- Dynein light chain 2B, cytoplasmic, putative
- Dynein light chain roadblock
- Dynein light chain roadblock
Sequence:
MMSDRKTNVKLSDISEEMQNDALLVAARAVKEHQLERDIAAHIKKEFDKRHNPTWQCIAGRNFGADVVHESKHFIYFYVGQISILLWKTG
Protein: ubiquitinyl hydrolase 1 (EC 3.4.19.12) (Q803C0)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MSEGEVFHEKQRLELCAIHALNNVLQERVFTKETADDICKRLAPQCVMNPHRSVLGTGNYDVNVIMAALQSRGLAAVWWDERRSVQNLCLDKIQGFILNVPSRVSLGIVSLPLRRRHWLAVREVHGHFYNLDSKLKGPACIGGETELRSFLTEQLSQDVAEMLLVVQKEVDEDGTWLKPDDTRK
Protein: At4g22380 (Ribosomal protein L7Ae-like) (Ribosomal protein L7Ae/L30e/S12e/Gadd45 family protein) (Q8LCC7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Nucleus, nucleolus {ECO:0000256|ARBA:ARBA00004604, ECO:0000256|RuleBase:RU366039}.
Interaction partners:
- Protein SLOW WALKER 1
- U3 snoRNP-associated protein-like YAO
- U3 snoRNP-associated protein-like EMB2271
- Nucleolar protein 56
- Nucleolar protein 56
- H/ACA ribonucleoprotein complex subunit 3-like protein
- U3 small nucleolar RNA-associated protein 18 homolog
- Uncharacterized protein At3g06530
- M phase phosphoprotein 10
- Probable nucleolar protein 5-1
Sequence:
MTGEVVNPKAYPLADSQLSITIMDLVQQATNYKQLKKGANEATKTLNRGISEFVVMAADAEPLEILLHLPLLAEDKNVPYVFVPSKQALGRACGVTRPVIACSVTSNEASQLKSQIQHLKDAIEKLLI
Protein: F-box/LRR-repeat protein 5 (F-box and leucine-rich repeat protein 5) (Q8C2S5)
Organism: Mus musculus (Mouse)
Function: Component of some SCF (SKP1-cullin-F-box) protein ligase complex that plays a central role in iron homeostasis by promoting the ubiquitination and subsequent degradation of IREB2/IRP2. Upon high iron and oxygen level, it specifically recognizes and binds IREB2/IRP2, promoting its ubiquitination and degradation by the proteasome. Promotes ubiquitination and subsequent degradation of DCTN1/p150-glued (By similarity).
Subcellular location: Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q9UKA1}. Nucleus {ECO:0000250|UniProtKB:Q9UKA1}.
Interaction partners:
- S-phase kinase-associated protein 1
- Cullin-1
- Iron-responsive element-binding protein 2
- Cytoplasmic aconitate hydratase
- E3 ubiquitin-protein ligase RBX1
- F-box/LRR-repeat protein 14
- Cytosolic iron-sulfur assembly component 2B
Sequence:
MAPFPDEVDVFTAPHWRMKQLVGRYCDKLSKTNFSNNNDFRALLQSLYATFKEFKMHEQIENEYIIGLLQQRSQTIYNVHSDNKLSEMLSLFEKGLKNVKNEYEQLNYAKQLKERLEAFTRDFLPHMKEEEEVFQPMLMEYFTYEELKDIKKKVIAQHCSQKDTAELLRGLSLWNQAEERQKVLKYSVDEKADTEAEVSEHSTGITHLPPEVMLSIFSYLNPQELCRCSQVSTKWSQLAKTGSLWKHLYPVHWARGDWYSGPATELDTEPDEEWVRNRKDESRAFQEWDEDADIDESEESAEESVAISIAQMEKRVLHGLIHNVLPYVGTSVKTLVLAYSSAVSSKMVRQILELCPNLEHLDLTQTDISDSAFDSWSWLGCCQSLRHLDLSGCEKITDMALEKISRALGVLTSHQSGFLKSAGKAASTPWTSKDITMPSTTQYACLHNLTDKGIGEEIDNEHSWTEPVSSESLTSPYVWMLDAEDLADIEDAVEWRHRNVESLCVMETASNFGCSSSGCYSKDIVGLRTSVCWQQHCASPAFAYCGHSFCCTGTALRTMTTLPATSAMCRKALRTTLPRGKDLIYFGSEKSDQETGRVLLFLSLSGCYQITDHGLRALTLGGGLPYLEHLNLSGCLTVTGAGLQDLVSACPSLNDEYFYYCDNINGPHADTASGCQNLQCGFRACCRSGE
Protein: Trehalose-phosphatase (EC 3.1.3.12) (Trehalose-6-phosphate phosphatase) (TPP) (Q9XTQ5)
Organism: Caenorhabditis elegans
Function: Catalyzes the hydrolysis of trehalose 6-phosphate to trehalose and phosphate; prevents the accumulation of toxic levels of trehalose 6-phosphate.
Interaction partners:
- Trehalase
- Trehalase
- Trehalase
- Trehalase
- J domain-containing protein
- Trehalase
- GrpE protein homolog
- J domain-containing protein
- Thioredoxin domain-containing protein
- DnaJ homolog subfamily C member 10
Sequence:
MNCEKESQMTIASQSIEDFKECLYQMQEARKSVTNEILETGHIKADQVQIFKSTLEEMNDERTSKNHIRDIHSRGTTFGINIQDEIKGLQKDHHFLDAFAVESDKENNSFANVLKLCDLPGLLSKFVDDEIRFEKEVAECKAFLMDLIDTSTTGGIKPLFITDWDGTMKDYCSQYATNLQPAYSAIVMGVFSRLFTRAFAVLTAGPLRHPGILDLTALPINGPVLFSGSWGREWWLGGRRIVHDDGIPEEGSVAIGQLCEQLDEILHEGEFVQFALVGSGVQRKVDRLTLGVQTVFKQVPEDLSARYIDAVRERIHRVDPNSQYLVLENCSPLEIEVCVHSSGAVWNKGDGVAALVESLHDSLKVGKVCVAGDTASDVPMLKKAADENPENVRALFVNINKQLQENITNIVGDAKRVCFISSPDVAHAAFAQIISEFSG
Protein: Cilia- and flagella-associated protein 53 (F1N7G5)
Organism: Bos taurus (Bovine)
Function: Microtubule inner protein (MIP) part of the dynein-decorated doublet microtubules (DMTs) in cilia axoneme, which is required for motile cilia beating. May play a role in the beating of primary cilia and thereby be involved in the establishment of organ laterality during embryogenesis.
Subcellular location: Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000269|PubMed:34715025}. Cytoplasm, cytoskeleton, flagellum axoneme {ECO:0000269|PubMed:37327785}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriolar satellite {ECO:0000250|UniProtKB:Q9D439}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000250|UniProtKB:Q96M91}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q9D439}. Note=In tracheal cell cilia, localizes prominently to both centriolar satellites and axonemes (By similarity). Tightly associated with microtubules in tracheal cilia (By similarity). In embryonic node cells, localizes to the base of the node cilia at the centriolar satellites and, to a lesser extent, to the cilium axoneme (By similarity). Localizes to centriolar satellites through G1, S phase, G2 and mitosis (By similarity). Enriched on the spindle poles in mitosis (By similarity). Relocalizes from the centriolar satellite to the ciliary transition zone upon ciliogenesis (By similarity). In skin fibroblast cells, locates predominantly to the centriole with much lower levels associated with the actin cytoskeleton (By similarity). Localizes to the sperm flagellum and manchette (By similarity). {ECO:0000250|UniProtKB:Q96M91, ECO:0000250|UniProtKB:Q9D439}.
Interaction partners:
Sequence:
MYSQRFGIVQREVKGPTPKVVIVRAKPPKGQGAEHHLQRIQHSHQKHHAILASIKSIERDRLKTEWDQHNDCKFVDSLVKARVKDAMQGFIINTEERRNKLRELLASEENEYFTEMQLKEETIEEKKDRMRDKIRLLREKKEKERQDFVAEKLDQQFRERCQELRAELFCIHQKAVCEERKAQIAFNEELKRQKVVEEQMFSKLWEEDRLAKERREAKEERRQKELVENTRLGLNAQVTSIQAQRQAAQRLKEEEALLVENENAQVKLENEQDKLKKQKTKQEIRAALQKALQEKMERMQQEYREEQDLNMKLMQNALQSLQEETDKKKQKKEDMRREQKIYYQYLAQRHEEEKAQEKELDRMLEKEKEKKFAEKDKELRLEKEARKQLLNEVMCTRKLQVQEKLQRKAKEQEERTMEQERINEGLKELNCEERENFIRRCSLAQEYRKQLQMQICSQQQAREAEEEEERREFEAGIAAEKSFQDKIQGILSTHQVVPRNIHPMRRACSTKLPP
Protein: Zinc finger protein 42 homolog (Zfp-42) (Reduced expression protein 1) (REX-1) (hREX-1) (Zinc finger protein 754) (Q96MM3)
Organism: Homo sapiens (Human)
Function: Involved in the reprogramming of X-chromosome inactivation during the acquisition of pluripotency. Required for efficient elongation of TSIX, a non-coding RNA antisense to XIST. Binds DXPas34 enhancer within the TSIX promoter. Involved in ES cell self-renewal (By similarity).
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- Homeobox protein NANOG
- Polycomb protein EED
- POU domain, class 5, transcription factor 1
- E3 ubiquitin-protein ligase RING2
- Steroid hormone receptor ERR2
- E3 ubiquitin-protein ligase RING1
- Polycomb protein SUZ12
- RING1 and YY1-binding protein
- Transcription factor SOX-2
- Protein lin-28 homolog A
Sequence:
MSQQLKKRAKTRHQKGLGGRAPSGAKPRQGKSSQDLQAEIEPVSAVWALCDGYVCYEPGPQALGGDDFSDCYIECVIRGEFSQPILEEDSLFESLEYLKKGSEQQLSQKVFEASSLECSLEYMKKGVKKELPQKIVGENSLEYSEYMTGKKLPPGGIPGIDLSDPKQLAEFARKKPPINKEYDSLSAIACPQSGCTRKLRNRAALRKHLLIHGPRDHVCAECGKAFVESSKLKRHFLVHTGEKPFRCTFEGCGKRFSLDFNLRTHVRIHTGEKRFVCPFQGCNRRFIQSNNLKAHILTHANTNKNEQEGK
Protein: Phosrestin-1 (49 kDa arrestin-like protein) (Arrestin-2) (Arrestin-B) (Phosrestin I) (P19107)
Organism: Drosophila melanogaster (Fruit fly)
Function: Probably plays an important role in the photoreceptor transduction.
Subcellular location: Cell projection, rhabdomere {ECO:0000269|PubMed:8316831}.
Interaction partners:
- Opsin Rh1
- Neither inactivation nor afterpotential protein C
- Phosrestin-2
- Transient-receptor-potential-like protein
- Inactivation-no-after-potential D protein
- Calcium/calmodulin-dependent protein kinase type II alpha chain
- Opsin Rh3
- 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase
- Guanine nucleotide-binding protein subunit beta-2
- Opsin Rh4
Sequence:
MVVSVKVFKKATPNGKVTFYLGRRDFIDHIDYCDPVDGVIVVEPDYLKNRKVFGQLATTYRYGREEDEVMGVKFSKELILCREQIVPMTNPNMEMTPMQEKLVRKLGSNAYPFTFHFPPNSPSSVTLQQEGDDNGKPLGVEYTIRAFVGDSEDDRQHKRSMVSLVIKKLQYAPLNRGQRLPSSLVSKGFTFSNGKISLEVTLDREIYYHGEKTAATVQVSNNSKKSVKSIKCFIVQHTEITMVNAQFSKHVAQLETKEGCPITPGANLTKTFYLIPLAANNKDRHGIALDGHLKDEDVNLASSTMVQEGKSTGDACGIVISYSVRIKLNCGTLGGEMQTDVPFKLLQPAPGTIEKKRSNAMKKMKSIEQHRNVKGYYQDDDDNIVFEDFAKMRMNNVNMAD