wanglab/gogpt-training-data huggingface dataset:
Protein: 1,25-dihydroxyvitamin D(3) 24-hydroxylase, mitochondrial (24-OHase) (Vitamin D(3) 24-hydroxylase) (EC 1.14.15.16) (Cytochrome P450 24A1) (Cytochrome P450-CC24) (Q07973)
Organism: Homo sapiens (Human)
Function: A cytochrome P450 monooxygenase with a key role in vitamin D catabolism and calcium homeostasis. Via C24- and C23-oxidation pathways, catalyzes the inactivation of both the vitamin D precursor calcidiol (25-hydroxyvitamin D(3)) and the active hormone calcitriol (1-alpha,25-dihydroxyvitamin D(3)). With initial hydroxylation at C-24 (via C24-oxidation pathway), performs a sequential 6-step oxidation of calcitriol leading to the formation of the biliary metabolite calcitroic acid. With initial hydroxylation at C-23 (via C23-oxidation pathway), catalyzes sequential oxidation of calcidiol leading to the formation of 25(OH)D3-26,23-lactone as end product. Preferentially hydroxylates at C-25 other vitamin D active metabolites, such as CYP11A1-derived secosteroids 20S-hydroxycholecalciferol and 20S,23-dihydroxycholecalciferol. Mechanistically, uses molecular oxygen inserting one oxygen atom into a substrate, and reducing the second into a water molecule, with two electrons provided by NADPH via FDXR/adrenodoxin reductase and FDX1/adrenodoxin.
Subcellular location: Mitochondrion {ECO:0000250|UniProtKB:Q09128}.
Interaction partners:
- Vitamin D 25-hydroxylase
- 25-hydroxyvitamin D-1 alpha hydroxylase, mitochondrial
- Vitamin D-binding protein
- Carbonic anhydrase 1
- Carbonic anhydrase-related protein
- Carbonic anhydrase 5B, mitochondrial
- Carbonic anhydrase 13
- Carbonic anhydrase 14
- Parathyroid hormone
- Carbonic anhydrase 5A, mitochondrial
Sequence:
MSSPISKSRSLAAFLQQLRSPRQPPRLVTSTAYTSPQPREVPVCPLTAGGETQNAAALPGPTSWPLLGSLLQILWKGGLKKQHDTLVEYHKKYGKIFRMKLGSFESVHLGSPCLLEALYRTESAYPQRLEIKPWKAYRDYRKEGYGLLILEGEDWQRVRSAFQKKLMKPGEVMKLDNKINEVLADFMGRIDELCDERGHVEDLYSELNKWSFESICLVLYEKRFGLLQKNAGDEAVNFIMAIKTMMSTFGRMMVTPVELHKSLNTKVWQDHTLAWDTIFKSVKACIDNRLEKYSQQPSADFLCDIYHQNRLSKKELYAAVTELQLAAVETTANSLMWILYNLSRNPQVQQKLLKEIQSVLPENQVPRAEDLRNMPYLKACLKESMRLTPSVPFTTRTLDKATVLGEYALPKGTVLMLNTQVLGSSEDNFEDSSQFRPERWLQEKEKINPFAHLPFGVGKRMCIGRRLAELQLHLALCWIVRKYDIQATDNEPVEMLHSGTLVPSRELPIAFCQR
Protein: Large ribosomal subunit protein eL15y (60S ribosomal protein L15-2) (Q8VYF1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Large ribosomal subunit protein uL18y
- Large ribosomal subunit protein eL13z
- Large ribosomal subunit protein eL42z/eL42y
- At1g43860
- Large ribosomal subunit protein uL13y
- Small ribosomal subunit protein uS14z/uS14y/uS14x
- Large ribosomal subunit protein eL38z/eL38y
- Large ribosomal subunit protein eL21z/eL21y
- Large ribosomal subunit protein eL24z
- Small ribosomal subunit protein eS30z/eS30y/eS30x
Sequence:
MGAYKYVSELWRKKQSDVMRFLQRVRCWEYRQQPSIVRLVRPTRPDKARRLGYKAKQGFVVYRVRVRRGGRKRPVPKGIVYGKPTNQGVTQLKFQRSKRSVAEERAGRKLGGLRVVNSYWLNEDSTYKYYEIILVDPAHNAVRNDPRINWICNPVHKHRELRGLTSEGKKNRGLRGKGHNNHKNRPSRRATWKKNNSISLRRYR
Protein: Domoic acid biosynthesis cluster protein B (PmDabB) (A0A386L1Q6)
Organism: Pseudo-nitzschia multiseries (Marine planktonic diatom) (Nitzschia pungens f. multiseries)
Function: Unknown function: part of the gene cluster that mediates the biosynthesis of domoic acid (DA) and derivatives, natural products with neurochemical activity acting as ionotropic glutamate receptor (iGluR) agonists, thus being neurotoxins causing amnesic shellfish poisoning (ASP).
Interaction partners:
Sequence:
MMAGRKGYQSVMDENCHDKTESAYTDDRSLNGSSGSSCLKNNVIAFFLGAAVVAATQYVSIDSSLTKAVEVTSFTTSDAPAIDIAINPTRPSLDARQDFKIEGWGNQTRNDGWPSFHFEVFHFCPHLINFMYENQVHPQSRVDPSNVIYDAQHPGALAEDGFAEVLQQTLPKFYDYPVGYRLNDRPAEISAYWTLHMRIARGSEDSQWHDFASSLPEGINRIYVKKPLQWNGDHVTLFSSQTGYNILVY
Protein: Catalase-2 (EC 1.11.1.6) (O61235)
Organism: Caenorhabditis elegans
Function: Catalase involved in the oxidative stress response serving to protect cells from toxicity (Probable). For instance plays a role in defending against oxidative damage induced by excessive copper stress. Not required for maintaining normal lifespan.
Interaction partners:
- Peroxisomal catalase 1
- Superoxide dismutase
- FMN hydroxy acid dehydrogenase domain-containing protein
- 3-hydroxyanthranilate 3,4-dioxygenase
- Kynureninase
- Catalase
- Superoxide dismutase 2, mitochondrial
- Peroxiredoxin prdx-2
- Thioredoxin domain-containing protein
- Glutathione S-transferase 4
Sequence:
MPNDPSDNQLKTYKETYPKPQVITTSNGAPIYSKTAVLTAGRRGPMLMQDVVYMDEMAHFDRERIPERVVHAKGAGAHGYFEVTHDITKYCKADMFNKVGKQTPLLVRFSTVAGESGSADTVRDPRGFSLKFYTEEGNWDLVGNNTPIFFIRDAIHFPNFIHALKRNPQTHMRDPNALFDFWMNRPESIHQVMFLYSDRGIPDGFRFMNGYGAHTFKMVNKEGNPIYCKFHFKPAQGSKNLDPTDAGKLASSDPDYAIRDLFNAIESRNFPEWKMFIQVMTFEQAEKWEFNPFDVTKVWPHGDYPLIEVGKMVLNRNVKNYFAEVEQAAFCPAHIVPGIEFSPDKMLQGRIFSYTDTHYHRLGPNYIQLPVNCPYRSRAHTTQRDGAMAYESQGDAPNYFPNSFRGYRTRDDVKESTFQTTGDVDRYETGDDHNYEQPRQFWEKVLKEEERDRLVGNLASDLGGCLEEIQNGMVKEFTKVHPDFGNALRHQLCQKKH
Protein: Polyhomeotic homolog 3 (E7EX82)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MAEAEFKDHSTAMDTEPNPGTSSVSTTTSSTTTTTITTSSSRMQQPQISVYSGSDRHAVQVIQQALHRPPSSAAQYLQQMYAAQQQHLMLHTAALQQQHLSSSQLQSLAAVQASLSSGRPSTSPTGSVTQQSSMSQTSLIFTPATTVAAVQSDIPVVSSSSSSSCQSAATQVQNLTLRSQKLGVLSSSQNGPPKSTSQTQSLTICHNKTTVTSSKISQRDPSPESNKKGESPSLESRSTAVTRTSSIHQLIAPASYSPIQPHSLIKHQQIPLHSPPSKVSHHQLILQQQQQQIQPITLQNSTQDPPPSQHCIPLQNHGLPPAPSNAQSQHCSPIQSHPSPLTVSPNQSQSAQQSVVVSPPPPHSPSQSPTIIIHPQALIQPHPLVSSALQPGPNLQQSTANQVQATAQLNLPSHLPLPASPVVHIGPVQQSALVSPGQQIVSPSHQQYSSLQSSPIPIASPPQMSTSPPAQIPPLPLQSMQSLQVQPEILSQGQVLVQNALVSEEELPAAEALVQLPFQTLPPPQTVAVNLQVQPPAPVDPPVVYQVEDVCEEEMPEESDECVRMDRTPPPPTLSPAAITVGRGEDLTSEHPLLEQVELPAVASVSASVIKSPSDPSHVSVPPPPLLLPAATTRSNSTSMHSSIPSIENKPPQAIVKPQILTHVIEGFVIQEGLEPFPVSRSSLLIEQPVKKRPLLDNQVINSVCVQPELQNNTKHADNSSDTEMEDMIAEETLEEMDSELLKCEFCGKMGYANEFLRSKRFCTMSCAKRYNVSCSKKFALSRWNRKPDNQSLGHRGRRPSGPDGAAREHILRQKKTWLLMKILCHLL
Protein: Sphingosine kinase A (SK A) (SPK A) (EC 2.7.1.91) (Q86KF9)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Catalyzes the phosphorylation of sphingosine to form sphingosine-1-phosphate (S1P), which probably acts intracellularly as a second messenger perhaps by promoting cell proliferation. Overexpression of sgkA leads to increased growth rates on solid media and an increased resistance to the antitumor agents cisplatin and carboplatin.
Subcellular location: Cytoplasm {ECO:0000305}. Nucleus {ECO:0000305}. Note=Determined in cells overexpressing sgkA. Also appears enriched in some pseudopodia.
Interaction partners:
- Sphingosine-1-phosphate lyase
- sphinganine-1-phosphate aldolase
- Neutral ceramidase B
- sphingolipid 4-desaturase
- Probable sphingosine-1-phosphate phosphatase
- Neutral ceramidase A
- 3-ketodihydrosphingosine reductase
- Putative alkaline ceramidase dcd3B
- Putative alkaline ceramidase dcd3A
- Sphingosine kinase B
Sequence:
MSINSDYNKENNNISPLNTSSERRSSLRNSLNNSSNNNNNNVINTPTANSINSSGNFSPKEFVSNIDGEEIIYQNQSVEYKQRLCTIQIKQSTLIIKFNEKGGFTKYLVSDTIVGSEITNESTNEYTIYSCVMNTLDVTKETRRRKQFSLRFRDRFELNQFNDKFVEAFLDTLPMGNPRERRIRVILNPKSGKKMSDSIFKDINELFKDSKIFVKKTVTKGPDHAKKIGYKFNLKKYDTIVFISGDGLFHEFINGLLSRTDFEQARKIPLALIPGGTGNGIACSIGLQDPMSCALAVIRGFTKPLDVSVIQQGDKKWCSILSLTWGIVSDVDIESEKYRALGDVRLILGAALRILNLRIYRGKIWYLPALELNKTEIAKIPKCSYSCEICESDNPISTIENVISQQQQNNTTTNQLRRSSLNNSSNGFSPKLNTSGSISNGNDDELRSMFSKEENIKIENEIHDHQNDDVLPLLKSSSDQHFIVPPTKLPNQQFLKETKEELFAKGWKVLEGEFIGIVASTVSHLASDFIASPTAHLSDGLIDLVVINNNKKFSKAGLLSVLTESSTGAHVKSDLIDQYKVQAMILEPSNDREGIIAVDGELISYGRTSMECMRACINLICRTY
Protein: Protein kinase C (EC 2.7.11.13) (G8JY36)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MHRSDESRMSFEHRSVVRLFSNSSTTSNGSRKTSVPSAVLASAPLMSAAIGDGLGTQLSQRIEGKAFVRRGALRQKNVHEIKSHKFIARFFKQPTFCSHCKDFLWGITKQGFQCQVCTLVVHKRCHEFVNFACPGADKGVDTDDPRQQHKWKVQTYSSPTFCDHCGSLLYGILHQGMKCQSCDTNVHHRCVKNVPNMCGTDNTEKRGRLRIEAHIENDQLTIKILEAKNLIPMDPNGLSDPYVKCKLIPEDSGCKSKQKTKTLRATLNPQWNETFTYKLLPGDKDRRLSIEVWDWDRTSRNDFMGSLSFGISELMKEAASGWYKLLSAEEGEFYNINITPEYDEDMEKVRKKMNENFITRDNSSSKPKDPAAPRASTLPLGSSNHNVIKASDFNFLTVLGKGSFGKVLLGEQKTTKELFAIKVLKKDVIIQDDDVECTMTEKRVLALPEKPSFLVALHSCFQTMDRLYFVMEFVNGGDLMYQIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMCKENIFGDATTKTFCGTPDYIAPEIILYQPYGKSVDWWAYGVLLFEMLAGQPPFDGEDEDELFTAITEHNVSYPKSLSKEAVSLCKALLIKNPSKRLGCTGDDESASRDIKEHPFFRRIDWFKIETRQIQPPFKPKLKSADDTSNFDSEFTHEVPKLTPIDRLFLMNLDQTEFEGFSFVNPEYVQEC
Protein: CBL-interacting serine/threonine-protein kinase 10 (EC 2.7.11.1) (SNF1-related kinase 3.8) (SOS2-like protein kinase PKS2) (SOS3-interacting protein 1) (Q9C562)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: CIPK serine-threonine protein kinases interact with CBL proteins. Binding of a CBL protein to the regulatory NAF domain of CIPK protein lead to the activation of the kinase in a calcium-dependent manner (By similarity).
Interaction partners:
- SNF1-related protein kinase regulatory subunit gamma-1
- Calcineurin B-like protein 9
Sequence:
MENKPSVLTDKYDVGRLLGQGTFAKVYYGRSILTNQSVAIKMIDKEKVMKVGLIEQIKREISVMRIARHPNVVELYEVMATKTRIYFVMEYCKGGELFNKVAKGKLRDDVAWKYFYQLINAVDFCHSREVYHRDIKPENLLLDDNENLKVSDFGLSALADCKRQDGLLHTTCGTPAYVAPEVINRKGYDGTKADIWSCGVVLFVLLAGYLPFHDSNLMEMYRKIGKADFKAPSWFAPEVRRLLCKMLDPNPETRITIARIRESSWFRKGLHMKQKKMEKRVKEINSVEAGTAGTNENGAGPSENGAGPSENGDRVTEENHTDEPTNLNAFDLIALSAGFDLAGLFGDDNKRESRFTSQKPASVIISKLEEVAQRLKLSIRKREAGLFKLERLKEGRKGILSMDAEIFQVTPNFHLVEVKKSNGDTLEYQKLVAEDLRPALSDIVWVWQGEKDELTSQQETEYQQQQQQEQQEQEEPLKF
Protein: Type III secretory apparatus protein PcrD (Q9I327)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Subcellular location: Cell inner membrane {ECO:0000256|ARBA:ARBA00004429}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004429}.
Interaction partners:
- Type III secretion outer membrane protein PopN
- Translocation protein in type III secretion
- Lipoprotein
- Probable translocation protein in type III secretion
- Translocation protein in type III secretion
- Regulator in type III secretion
- Translocation protein in type III secretion
- Translocation protein in type III secretion
- Translocation protein in type III secretion
- Type 3 secretion system secretin
Sequence:
MNDLSGLLGRVGERKDILLVVLLLAVVFMMVLPLPPLLLDILIAVNITISVVLLMMSVYIGSPLQFSVFPAVLLITTLFRLALSVSTTRMILLQADAGQIVNTFGSFVVGGNLVVGIIIFLIITIVQFLVITKGAERVAEVSARFSLDAMPGKQMSIDGDMRAGVIDVNEARARRAVIEKESQMFGSMDGAMKFVKGDAIAGLIIIVVNILGGIAIGVTQKGLSTADALQLYAVLTVGDGMVSQVPALLIAITAGIIVTRVSSDESADLGSDIGEQVVAQPKALLIGGLLLVLFGLIPGFPTLTFLALALLVGGGGYFMLWRQRAQASAGSRDLPALLAQGAGAPSAKARGKAGGGKPKAGRLAEQEEFALTVPLLIDVDASLQERLEAMSLNEELVRVRRALYLDFGVPFPGIHLRFNEAMGDGEYLVQLQEVPVARGCLRPGWLLVRERAAQLELLAVPHEPAELQVPGEEASWVEQAHQDRLERSGCACLGLEQVLTWHLSHVLREYAEDFIGIQETRYLLEQMEQGYGELVKEAQRIVPLQRMTEILQRLVGEDISIRNMRAILEAMVEWGQKEKDVVQLTEYIRSSLKRYICYKYSSGNNILPAYLLDQAVEEQIRGGIRQTSAGSYLALDPAITQAFLERVRQTVGDLAQMQNRPVLIVSMDIRRYVRKLVESDYAGLPVLSYQELTQQINIQPLGRIVL
Protein: Nuclear pore complex protein Nup155 (155 kDa nucleoporin) (Nucleoporin Nup155) (Q99P88)
Organism: Mus musculus (Mouse)
Function: Essential component of nuclear pore complex. Could be essessential for embryogenesis. Nucleoporins may be involved both in binding and translocating proteins during nucleocytoplasmic transport.
Subcellular location: Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:P37199}. Nucleus membrane {ECO:0000250|UniProtKB:P37199}; Peripheral membrane protein {ECO:0000250|UniProtKB:P37199}; Cytoplasmic side {ECO:0000250|UniProtKB:P37199}. Nucleus membrane {ECO:0000250|UniProtKB:P37199}; Peripheral membrane protein {ECO:0000250|UniProtKB:P37199}; Nucleoplasmic side {ECO:0000250|UniProtKB:P37199}. Note=In mitosis, assumes a diffuse cytoplasmic distribution probably as a monomer, before reversing back into a punctate nuclear surface localization at the end of mitosis. {ECO:0000250|UniProtKB:P37199}.
Interaction partners:
- Nucleoporin 205
- Nuclear pore complex protein Nup93
- Nucleoporin NUP188
- Nucleoporin NUP35
- Nuclear pore complex protein Nup98-Nup96
- Nuclear pore complex protein Nup54
- E3 SUMO-protein ligase RanBP2
- Nuclear pore complex protein Nup153
- Nuclear pore complex protein Nup85
- Nuclear pore complex protein Nup107
Sequence:
MPSVLGSMMVASTSAAASLQEALENAGRLIDRQLQEDRMYPDLSELLMVSAPNSPTVSGMSDMDYPLQGPGLLSVPSLPEISTIRRVPLPPELVEQFGHMQCNCMMGVFPPISRAWLTIDSDIFMWNYEDGGDLAYFDGLSETILAVGLVKPKAGIFQPHVRHLLVLATPVDIVILGLSYANVQTGSGILNDSMCGGMQLLPDPLYSLPTDNTYLLTITSTDNGRIFLAGKDGCLYEVAYQAEAGWFSQRCRKINHSKSSLSFLVPSLLQFTFSEDDPIVQIEIDNSRNILYTRSEKGVIQVYDLGHDGQGMSRVASVSQNAIVSAAGNIARTIDRSVFKPIVQIAVIESSESLDCQLLAVTHAGVRLYFSTCPFRQPLARPNTLTLVHVRLPPGFSASSTVEKPSKVHKALYSKGILLMTASENEDNDILWCVNHDTFPFQKPMMETQMTTRVDGHSWALSAIDELKVDKIITPLNKDHIPITDSPVVVQQHMLPPKKFVLLSAQGSLMFHKLRPVDQLRHLLVSNVGGDGEEIERFFKLHQEDQACATCLILACSTAACDREVSAWATRAFFRYGGEAQMRFPATLPTPSNVGPILGSPMYSSSPVPSGSPYPNPSSLGTPSHGAQPPTMSTPMCAVGSPAMQAASMSGLTGPEIVYSGKHNGICIYFSRIMGNIWDASLVVERVFKSSNREITAIESSVPVQLLESVLQELKGLQEFLDRNSQFSGGPLGNPNTTARVQQRLVGFMRPENGNTQQMQQELQRKFQEAQLSEKISLQAIQQLVRKSYQALALWKLLCEHQFSVIVGELQKEFQEQLKITTFKDLVIRDKEVTGALIASLINCYIRDNAAVDGISLHLQDTCPLLYSTDDAVCSKANELLQRSRQVQSKTERERMLRESLKEYQKISNQVDLPSVCAQYRQVRFYEGVVELSLTAAEKKDPQGLGLHFYKHGEPEEDVVGLQTFQERLNSYKCITDTLQELVNQSKAAPQSPSVPKKPGPPVLSSDPNMLSNEEAGHHFEQMLKLAQRSKDELFSIALYNWLIQADLADKLLQIASPFLEPHLVRMARVDQNRVRYMDLLWRYYEKNRSFSSAARVLSKLADMHSTEISLQQRLEYIARAILSAKSSTAISSIAADGEFLHELEEKMEVARIQLQIQETLQRQYSHHSSVQDAISQLDSELMDITKLYGEFADPFKLAECKLAVIHCAGYSDPILVHTLWQDIIEKELNDSVALSSSDRMHALSLKLVLLGKIYAGTPRFFPLDFIVQFLEQQVCTLNWDVGFVIQTMNEIGVPLPRLLEVYDQLFKSRDPFWNRVKSPLHLLDCIHVLLTRYVENPSLVLNCERRRFTNLCLDAVCGYLVELQSMSSSVAVQAITGNFKSLQAKLERLH
Protein: Nuclear RNA export factor 2 (Q9VV73)
Organism: Drosophila melanogaster (Fruit fly)
Function: May be involved in the export of mRNA from the nucleus to the cytoplasm. In the ovaries, forms a complex with nxf2, piwi and Nxt1 which acts as effectors of cotranscriptional transposon silencing. On recruitment to a target transcript, interacts with single stranded RNA, thereby anchoring the complex via the nascent target transcript to chromatin and allowing Panx to recruit silencing effectors to establishing repressive heterochromatin at transposon loci. Does not affect piRNA biogenesis. The interaction with Panx stabilizes the nuclear protein complex. Does not bind nucleoporins, but regulates sbr/Nxf1 binding to nucleoporins and, indirectly, transposon exports.
Subcellular location: Cytoplasm {ECO:0000255|PROSITE-ProRule:PRU00611, ECO:0000269|PubMed:11780633, ECO:0000269|PubMed:31219034}. Nucleus {ECO:0000269|PubMed:31219034, ECO:0000269|PubMed:31368590, ECO:0000269|PubMed:31384064}. Nucleus, nucleoplasm {ECO:0000269|PubMed:11780633}. Note=Localized in both the nucleoplasm and the cytoplasm (PubMed:11780633). Not detected at the nuclear rim (PubMed:11780633). Nuclear localization depends on interaction with Panx (PubMed:31219034, PubMed:31384064). {ECO:0000269|PubMed:11780633, ECO:0000269|PubMed:31219034, ECO:0000269|PubMed:31384064}.
Interaction partners:
- NTF2-related export protein
- Protein panoramix
- Nuclear cap-binding protein subunit 2
- Protein Rae1
- Nuclear export factor 4
- LD24793p
- RNA-binding protein 8A
- Nuclear pore complex protein Nup214
- Nuclear pore complex protein Nup58
- Protein piwi
Sequence:
MPNQMRVLDFGDGSVPIQLDYPDSKIFSKCSSYGDRVPGTHWNEITVHHKGRLEYSPNPEQIILDALYQAIDGADFFPVFYQRGKNMDTMLVRNCKAAIDKLFKQRLSINLKGGASIPISIQLGVAQYQRHQITPTFHIARVVTRLMKQLIQRDGVDGLLNLDNFGSHPEFKNLVVSLGNPSILMNVCQVIHNDDNERFRLNGFILSNNRIRDIRPLTLLANVDYALLDLRGNKIKSAERLCRALEQFRARELLLENNPIVKISNFPANIKSLESNFELVDGKPFNMLHKIFSPLDVEIDLEVDGARIDTNNMWKLPEFENSQHWHAFMIPDPSHEFNQEVFFDFFFIRLDPTLSNFYPCYYKYINTEHVFLVRNCFDQIAHLVNNCNLEMTIPTGDRIFRYYLRMNVSTVKQHHVDPEECIQKAVSQCYVAQNRMLNLERFHSRECLKDVMVSLSSPKILTYVLSVASRKFMTTCSEIRLCHNKVLVLDGAHVLGMMGCLRAVDLSHNWVQDLSSIHSLGNLPLKSLVLHGNKLCRNYRLPSEYVRAVKEVFPQLTTLDGVDLQTNPGQSLQKNFLCDTGAYELVGAFLENYLREFENDEFRHNLYKYYSENSIFTLTCNYNVVQNHQTPKILQRLSKYNRHARNLRNKDYSKASDGVFFGCTYIVEILLQLPRVTHDFHSLQTDVMHYNGKGAVIYVAGLLRDEPPSTRNGHGSKTDIGGVLLGFSRQFVVTFDEANLGLGKRARRLKIANERLHITNPSKTAIRNAFSVNFPDPSERQAEEDSLDVKDHKLLLFQEVTGLISTWVTSIVEEADWDFERALKLFIQKNADHEIPDLAFA
Protein: U6 snRNA-associated Sm-like protein LSm4 (Like-SM protein 4) (P40070)
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. Component of the cytoplasmic LSM1-LSM7 complex which is involved in mRNA degradation by activating the decapping step. Component of the nuclear LSM2-LSM8 complex, which is involved in splicing of nuclear mRNAs. LSM2-LSM8 associates with multiple spliceosome snRNP complexes containing the U6 snRNA (U4/U6 snRNP, U4/U6.U5 snRNP, and free U6 snRNP). It binds directly to the U6 snRNA and plays a role in the biogenesis and stability of the U6 snRNP and U4/U6 snRNP complexes. It probably also is involved in degradation of nuclear pre-mRNA by targeting them for decapping. LSM4 binds specifically to the 3'-terminal U-tract of U6 snRNA. LSM2-LSM8 probably is involved in processing of pre-tRNAs, pre-rRNAs and U3 snoRNA. LSM4, probably in a complex that contains LSM2-LSM7 but not LSM1 or LSM8, associates with the precursor of the RNA component of RNase P (pre-P RNA) and may be involved in maturing pre-P RNA. LSM4 is required for processing of pre-tRNAs, pre-rRNAs and U3 snoRNA.
Subcellular location: Nucleus {ECO:0000269|PubMed:14562095}. Cytoplasm {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Small nuclear ribonucleoprotein Sm D3
- LSM2-LSM8 complex subunit LSM8
- LSM1-LSM7 complex subunit LSM1
- Pre-mRNA-processing factor 31
- LSM complex subunit LSM2
- LSM complex subunit LSM7
- Small nuclear ribonucleoprotein Sm D2
- Deadenylation-dependent mRNA-decapping factor PAT1
- 66 kDa U4/U6.U5 small nuclear ribonucleoprotein component
- Small nuclear ribonucleoprotein F
Sequence:
MLPLYLLTNAKGQQMQIELKNGEIIQGILTNVDNWMNLTLSNVTEYSEESAINSEDNAESSKAVKLNEIYIRGTFIKFIKLQDNIIDKVKQQINSNNNSNSNGPGHKRYYNNRDSNNNRGNYNRRNNNNGNSNRRPYSQNRQYNNSNSSNINNSINSINSNNQNMNNGLGGSVQHHFNSSSPQKVEF
Protein: Ypt/Rab-type GTPase ypt71 (Q9HDY0)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Ypt/Rab-type GTPases are key regulators of membrane trafficking and intracellular vesicular transport. They act as molecular switches that convert between GTP-bound and GDP-bound states, and regulate virtually all steps of membrane traffic from the formation of the transport vesicle at the donor membrane to its fusion at the target membrane. In the GDP-bound state, Ypt proteins are predominantly cytosolic, solubilized through the interaction with a GDP dissociation inhibitor (GDI). In the GTP-bound state, the proteins are membrane bound and interact with specific effector proteins that select cargo, promote vesicle movement, or verify the correct site of fusion (By similarity). Act antagonistically to ypt7 in regulating vacuolar morphology, promoting vacuolar fission.
Subcellular location: Vacuole membrane {ECO:0000269|PubMed:19453973}.
Interaction partners:
- Ypt/Rab-type GTPase ypt7
- Tubulin alpha-1 chain
- Tubulin alpha-2 chain
- Tubulin beta chain
- Vacuolar morphogenesis protein 6
- Vacuolar protein sorting-associated protein 41
- Vacuolar protein sorting-associated protein 33
- Folliculin-like protein bhd1
- Probable vacuolar protein sorting-associated protein 16 homolog
- Vacuolar membrane protein pep3
Sequence:
MSAQKRVFLKVVILGDSGVGKTCLMNQFVNQKFSREYKATIGADFLTKDVVVDDKLVTLQLWDTAGQERFQSLGMAFYRGADCCVIVYNVNNSKSFDSVENWRQEFLYQTSQDECAFPFIIVGNQIDKDASKRAVSLHRALDYCKSKHGSNMIHFEASAKENTNVTDLFETVSRLALENESSRDDFVNDFSEPLLLSKPLNNTSSCNC
Protein: Uncharacterized protein Rv1488 (P9WPR9)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Subcellular location: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
- Conserved membrane protein
- ATP-dependent zinc metalloprotease FtsH
- Conserved protein
- Proteasome-associated ATPase
- UPF0301 protein Rv0038
- 4-hydroxy-3-methylbut-2-enyl diphosphate reductase 2
- Uncharacterized zinc protease Rv2782c
- Uncharacterized protein Rv1486c
- Probable transcriptional regulatory protein
- Conserved protein
Sequence:
MQGAVAGLVFLAVLVIFAIIVVAKSVALIPQAEAAVIERLGRYSRTVSGQLTLLVPFIDRVRARVDLRERVVSFPPQPVITEDNLTLNIDTVVYFQVTVPQAAVYEISNYIVGVEQLTTTTLRNVVGGMTLEQTLTSRDQINAQLRGVLDEATGRWGLRVARVELRSIDPPPSIQASMEKQMKADREKRAMILTAEGTREAAIKQAEGQKQAQILAAEGAKQAAILAAEADRQSRMLRAQGERAAAYLQAQGQAKAIEKTFAAIKAGRPTPEMLAYQYLQTLPEMARGDANKVWVVPSDFNAALQGFTRLLGKPGEDGVFRFEPSPVEDQPKHAADGDDAEVAGWFSTDTDPSIARAVATAEAIARKPVEGSLGTPPRLTQ
Protein: Putative E3 ubiquitin-protein ligase RING1a (EC 2.3.2.27) (Polycomb complex protein RING1a) (Protein RING1a) (AtRING1a) (RING-type E3 ubiquitin transferase RING1a) (Ring finger protein 434) (Q9FKW0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Putative E3 ubiquitin-protein ligase that mediates monoubiquitination of 'Lys-119' of histone H2A (H2AK119ub), thereby playing a central role in histone code and gene regulation.
Subcellular location: Nucleus {ECO:0000269|PubMed:19097900}.
Interaction partners:
- Chromo domain-containing protein LHP1
- Protein EMBRYONIC FLOWER 1
- Histone-lysine N-methyltransferase CLF
- Probable E3 ubiquitin protein ligase DRIPH
- Polycomb group protein FERTILIZATION-INDEPENDENT ENDOSPERM
- E3 ubiquitin protein ligase DRIP2
- Histone-lysine N-methyltransferase EZA1
- E3 ubiquitin protein ligase DRIP1
- PHD finger protein ALFIN-LIKE 2
- Histone-lysine N-methyltransferase MEDEA
Sequence:
MSVKNNSFSSAEIPDVADQPRDRFNPEATQDLQEKDETKEEKEGDEEVKHDEAEEDQEVVKPNDAEEDDDGDDAEEDEEEEVEAEEDEEAEEEEEEEEEEEEEEEDSKERSPSSISGDQSEFMEIDLGEIRKDVQCPICLGIIKKTRTVMECLHRFCRECIDKSMRLGNNECPACRKHCASRRSLRDDPKFDALIAALFTNIDSYEEEELAFHEDEMARNKQIQASIAQISQRQSEALVKRRSLGKEAAVLMRSPRIASGSRRRRNSRNMEQQNASEAHEDDDNDDNNNRGRDKDSSSDERGTEVRQKKRRKRSTSRSTQHPSSSGANKNNGNCADNDTEVYRDTKGISPGLVWNPEILAWGRGGTRSNTRHGNNTSGGSSKSVRNARVNKLVEYLRSSVDGSSVELDIHVKLVSLDTKCIPDLPQPYLCCRPTLLVKQLREFVALQIHLKTEEVELLVTRRRVGEDAAIENLPAVTPASAAASKDEMLSLEDNETLSRLKIDFISSHEQHLIIAYRKKQTE
Protein: Long-chain fatty acid transport protein 3 (FATP-3) (Fatty acid transport protein 3) (Arachidonate--CoA ligase) (EC 6.2.1.15) (Long-chain-fatty-acid--CoA ligase) (EC 6.2.1.3) (Solute carrier family 27 member 3) (Very long-chain acyl-CoA synthetase homolog 3) (VLCS-3) (EC 6.2.1.-) (Q5K4L6)
Organism: Homo sapiens (Human)
Function: Mainly functions as an acyl-CoA ligase catalyzing the ATP-dependent formation of fatty acyl-CoA using LCFA and very-long-chain fatty acids (VLCFA) as substrates. Can mediate the levels of long-chain fatty acids (LCFA) in the cell by facilitating their transport across membranes (By similarity).
Subcellular location: Mitochondrion membrane {ECO:0000269|PubMed:23936004}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
- Long-chain-fatty-acid--CoA ligase 1
- Beta-alanine-activating enzyme
Sequence:
MAALLLLPLLLLLPLLLLKLHLWPQLRWLPADLAFAVRALCCKRALRARALAAAAADPEGPEGGCSLAWRLAELAQQRAAHTFLIHGSRRFSYSEAERESNRAARAFLRALGWDWGPDGGDSGEGSAGEGERAAPGAGDAAAGSGAEFAGGDGAARGGGAAAPLSPGATVALLLPAGPEFLWLWFGLAKAGLRTAFVPTALRRGPLLHCLRSCGARALVLAPEFLESLEPDLPALRAMGLHLWAAGPGTHPAGISDLLAEVSAEVDGPVPGYLSSPQSITDTCLYIFTSGTTGLPKAARISHLKILQCQGFYQLCGVHQEDVIYLALPLYHMSGSLLGIVGCMGIGATVVLKSKFSAGQFWEDCQQHRVTVFQYIGELCRYLVNQPPSKAERGHKVRLAVGSGLRPDTWERFVRRFGPLQVLETYGLTEGNVATINYTGQRGAVGRASWLYKHIFPFSLIRYDVTTGEPIRDPQGHCMATSPGEPGLLVAPVSQQSPFLGYAGGPELAQGKLLKDVFRPGDVFFNTGDLLVCDDQGFLRFHDRTGDTFRWKGENVATTEVAEVFEALDFLQEVNVYGVTVPGHEGRAGMAALVLRPPHALDLMQLYTHVSENLPPYARPRFLRLQESLATTETFKQQKVRMANEGFDPSTLSDPLYVLDQAVGAYLPLTTARYSALLAGNLRI