wanglab/gogpt-training-data huggingface dataset:
Protein: Programmed cell death protein 4 (Q1L8Y5)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Phosphatase and tensin homolog B
- Eukaryotic translation initiation factor 4B
- Eukaryotic translation initiation factor 4E-1B
- Eukaryotic translation initiation factor 4E-1A
Sequence:
MATDCEAWLNANPVEAGNLSDSFPSGDEDSTFTANVNNEINGNWISAPTSTIHEARLKAKVKRRLRKNSSRDSGRGDSLSDNGEAVRSVVPPTSPKGKLLNRRSRTGKGRGLPKKGGAGGKGVWGTPGEVYGEDEVDYKDPNYDAEQENCVYETVVLPLDEEAFEKTVTPIVQEYFEHGDANEVAELLAELNLGSMRGDVPMLAVSLALEAKASHRELTSRLLSELCGRVLTAGDVQASFHKLLKELPDLVLDTPGAPQMLGQFIARAVADSILPKTFLDGYKGRVDCEYARAALDRAAVLLRMSRWTGLRIDSLWGSGGGQRPVTQLIKEVNLLLKEYLLSGDTVEAERCLRELEVPHFHHEFVYEAVIMVLESTGERTLQMLLQLLKCLCSSTIITVDQMRRGFERVYLDMPDISIDVPCAYSILERFVEQSFNAGVIDRKLRDLCPSRGRKRLISEGDGGHLKLQNY
Protein: Presequence protease, mitochondrial (hPreP) (EC 3.4.24.-) (Pitrilysin metalloproteinase 1) (Metalloprotease 1) (hMP1) (Q5JRX3)
Organism: Homo sapiens (Human)
Function: Metalloendopeptidase of the mitochondrial matrix that functions in peptide cleavage and degradation rather than in protein processing. Has an ATP-independent activity. Specifically cleaves peptides in the range of 5 to 65 residues. Shows a preference for cleavage after small polar residues and before basic residues, but without any positional preference. Degrades the transit peptides of mitochondrial proteins after their cleavage. Also degrades other unstructured peptides. It is also able to degrade amyloid-beta protein 40, one of the peptides produced by APP processing, when it accumulates in mitochondrion. It is a highly efficient protease, at least toward amyloid-beta protein 40. Cleaves that peptide at a specific position and is probably not processive, releasing digested peptides intermediates that can be further cleaved subsequently. It is also able to degrade amyloid-beta protein 42.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:26697887}. Mitochondrion matrix {ECO:0000269|PubMed:16849325, ECO:0000269|PubMed:19196155, ECO:0000269|PubMed:21621546}.
Interaction partners:
- Amyloid-beta precursor protein
- Proteinase-activated receptor 1
- Interstitial collagenase
- Endothelial protein C receptor
- Proteinase-activated receptor 2
Sequence:
MWRCGGRQGLCVLRRLSGGHAHHRAWRWNSNRACERALQYKLGDKIHGFTVNQVTSVPELFLTAVKLTHDDTGARYLHLAREDTNNLFSVQFRTTPMDSTGVPHILEHTVLCGSQKYPCRDPFFKMLNRSLSTFMNAFTASDYTLYPFSTQNPKDFQNLLSVYLDATFFPCLRELDFWQEGWRLEHENPSDPQTPLVFKGVVFNEMKGAFTDNERIFSQHLQNRLLPDHTYSVVSGGDPLCIPELTWEQLKQFHATHYHPSNARFFTYGNFPLEQHLKQIHEEALSKFQKIEPSTVVPAQTPWDKPREFQITCGPDSFATDPSKQTTISVSFLLPDITDTFEAFTLSLLSSLLTSGPNSPFYKALIESGLGTDFSPDVGYNGYTREAYFSVGLQGIAEKDIETVRSLIDRTIDEVVEKGFEDDRIEALLHKIEIQMKHQSTSFGLMLTSYIASCWNHDGDPVELLKLGNQLAKFRQCLQENPKFLQEKVKQYFKNNQHKLTLSMRPDDKYHEKQAQVEATKLKQKVEALSPGDRQQIYEKGLELRSQQSKPQDASCLPALKVSDIEPTIPVTELDVVLTAGDIPVQYCAQPTNGMVYFRAFSSLNTLPEELRPYVPLFCSVLTKLGCGLLDYREQAQQIELKTGGMSASPHVLPDDSHMDTYEQGVLFSSLCLDRNLPDMMQLWSEIFNNPCFEEEEHFKVLVKMTAQELANGIPDSGHLYASIRAGRTLTPAGDLQETFSGMDQVRLMKRIAEMTDIKPILRKLPRIKKHLLNGDNMRCSVNATPQQMPQTEKAVEDFLRSIGRSKKERRPVRPHTVEKPVPSSSGGDAHVPHGSQVIRKLVMEPTFKPWQMKTHFLMPFPVNYVGECIRTVPYTDPDHASLKILARLMTAKFLHTEIREKGGAYGGGAKLSHNGIFTLYSYRDPNTIETLQSFGKAVDWAKSGKFTQQDIDEAKLSVFSTVDAPVAPSDKGMDHFLYGLSDEMKQAHREQLFAVSHDKLLAVSDRYLGTGKSTHGLAILGPENPKIAKDPSWIIQ
Protein: Antitoxin RelB (O50462)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Antitoxin component of a type II toxin-antitoxin (TA) system. Upon expression in M.smegmatis neutralizes the effect of toxin RelE.
Interaction partners:
- Toxin RelE
- Toxin RelG
- Toxin RelK
- Antitoxin RelJ
Sequence:
MAVVPLGEVRNRLSEYVAEVELTHERITITRHGHPAAVLISADDLASIEETLEVLRTPGASEAIREGLADVAAGRFVSNDEIRNRYTAR
Protein: Tumor necrosis factor ligand superfamily member 18 (GITR ligand) (GITRL) (Glucocorticoid-induced TNF-related ligand) (Q7TS55)
Organism: Mus musculus (Mouse)
Function: Cytokine that binds to TNFRSF18/AITR/GITR. Regulates T-cell responses. Can function as costimulator and lower the threshold for T-cell activation and T-cell proliferation. Important for interactions between activated T-lymphocytes and endothelial cells. Mediates activation of NF-kappa-B. Triggers increased phosphorylation of STAT1 and up-regulates expression of VCAM1 and ICAM1 (By similarity). Promotes leukocyte adhesion to endothelial cells. Regulates migration of monocytes from the splenic reservoir to sites of inflammation.
Subcellular location: Cell membrane {ECO:0000269|PubMed:14521928, ECO:0000269|PubMed:14608036}; Single-pass type II membrane protein {ECO:0000269|PubMed:14521928, ECO:0000269|PubMed:14608036}.
Interaction partners:
- Tumor necrosis factor receptor superfamily member 18
- Tumor necrosis factor ligand superfamily member 4
- Tumor necrosis factor receptor superfamily member 4
- Tumor necrosis factor receptor superfamily member 9
- CD70 antigen
- Tumor necrosis factor receptor superfamily member 14
- Tumor necrosis factor ligand superfamily member 9
- Cytotoxic T-lymphocyte protein 4
- Tumor necrosis factor receptor superfamily member 3
Sequence:
MEEMPLRESSPQRAERCKKSWLLCIVALLLMLLCSLGTLIYTSLKPTAIESCMVKFELSSSKWHMTSPKPHCVNTTSDGKLKILQSGTYLIYGQVIPVDKKYIKDNAPFVVQIYKKNDVLQTLMNDFQILPIGGVYELHAGDNIYLKFNSKDHIQKTNTYWGIILMPDLPFIS
Protein: SNF2 domain-containing protein ENL1 (EC 3.6.4.-) (Protein ENDOSPERMLESS 1) (A0A0P0WGX7)
Organism: Oryza sativa subsp. japonica (Rice)
Function: DNA helicase that acts as an essential component of the spindle assembly checkpoint (By similarity). Plays an indispensable role in the development of seed endosperm. Is required to secure sister chromosome separation during endosperm syncytial mitosis, which involves extremely rapid free nuclear cycles.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:25327517}. Chromosome {ECO:0000269|PubMed:25327517}. Note=Localizes to the cytoplasm during interphase, but moves to the chromosome arms during mitosis. {ECO:0000269|PubMed:25327517}.
Interaction partners:
- Os02g0116900 protein
- Os03g0205400 protein
- Os02g0307200 protein
- Os01g0857900 protein
- Os09g0110400 protein
- Os07g0172500 protein
- DNA damage-binding protein 1
- Os01g0585400 protein
- Os06g0697400 protein
- Os03g0845700 protein
Sequence:
MASPPPFDICGDLDDDPTPPAPTPLAAPTPNGLNDRLLRLTRTHQRGPSQNPNPNPNPNPKPPPPPPPQEPEPAKVKLAGRRRLCKLSTAGDESAGDDDSIRDILDDLTTRLDSLSVDRPTARPRPHVSPLPCALHADPDPSQSQLNDGTKPSSSFVDCDDDDDDAGGAYGGFGVKEEVTRKVFKASSSFGGRGNDDKMKAKGAYAFDTVSRKTTTESKASKFFGDYDDEDDIDQDAENGKENHADDVGWEKTEDFKMEPTGTGVTRKPYNLPGRIFNMLYPHQREGLRWLWVLHCRGTGGILGDDMGLGKTMQVSAFLAGLFHSRLIKRVLVVAPKTLLTHWTKELSVVSLKDKIRDYSGPNANARNYELKYAFKEGGILLTTYDIVRNNFKMIKGNFTNDFDDEEETLWNYVILDEGHIIKNPKTQRAQSLFEIPCAHRIVISGTPIQNNLKEMWALFYFCCPEVLGDKEQFKARYEHAIIQGNDKNATNRQKHIGSNVAKELRERIKPYFLRRMKNEVFLDSGTGEDKKLAKKNELIIWLKLTSCQRQLYEAFLNSELVHSSMQGSPLAAITILKKICDHPLLLTKKAAEGVLEGMDAMLNNQEMGMVEKMAMNLADMAHDDDDVELQVGQDVSCKLSFMMSLLQNLVSEGHNVLIFSQTRKMLNIIQEAIILEGYKFLRIDGTTKISERERIVKDFQEGPGAPIFLLTTQVGGLGLTLTKAARVIVVDPAWNPSTDNQSVDRAYRIGQMKDVIVYRLMTSGTIEEKIYKLQVFKGALFRTATEHKEQTRYFSKRDIQELFSLPEQGFDVSLTQKQLQEEHGQQLVMDDSLRKHIQFLEQQGIAGVSHHSLLFSKTAILPTLNDNDGLDSRRAMPMAKHYYKGASSDYVANGAAYAMKPKEFIARTYSPNSTSTESPEEIKAKINRLSQTLANTVLVAKLPDRGDKIRRQINELDEKLTVIESSPEPLERKGPTEVICLDDLSV
Protein: Probable Rho-GTPase-activating protein 6 (O43027)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Interaction partners:
- Probable Rho-type GTPase-activating protein 4
- Probable Rho-type GTPase-activating protein 3
- 5'-AMP-activated protein kinase subunit beta
- Probable Rho-type GTPase-activating protein 2
- Cell division control protein 42 homolog
- Protein kinase domain-containing protein ppk9
- Multifunctional tryptophan biosynthesis protein
- SNF1-like protein kinase ssp2
- Rho guanine nucleotide exchange factor gef1
- GTP-binding protein rho2
Sequence:
MTLNPSTLNNGTLGDLKEHKDVVLSSNAQTDEKRFEEPSLEVGGSLAKVENGLSTSISSSASNLEGQQAPFFTKQNSCLSRFRELAQTYNIHEINLEEYVSQIKEVKQSLYSDDSVFNESKSSSPPDAHTDKYFTPCGSPTKLIHSTLLEERDTPSSLEHVSFYLQESAVSEVRFDKPSNNGPLGRSSLNLSSLSHELQTSQDSPSLSATNQLSSSDTLEPLQYPPSSFGSQRQFNASQDSPKRSPSKGSWSSILRRPSLTYSPKRQSTGLHRRSLTNYFKFPHRNAHQHNAIAHNPSVFGKPIGDLTSDPTNLCKFTFPTPECAPPSLLLPHIFAQCVHFLSLNALHVPGIFRISGSGPVIKAITEYFYSPPHFWLDETSEIFKRIGFPSYIDIAAVLKRYIMLLPGGLFTHKDILNLLVPLYVDSSRVKVPIDIRNEMAALCFSQIDSYVRFSILCSLLALLHQIATRTQELENGMENTKDSTLMKPEALGIIFGPLLLGNSSTDLSKSCPSGNVNDLMRFETEKARVEAKIVEGLIIHWPEVLLKINSLDIPNCFSDVGLTDQVAIFTPAVPKEDSPEQIPENVNASEESYPNVKHISKLPLINDSSDNESGNQENDDAVANESTKVVVDNQQPQPKISTVSDTAVPSMSFANNISSRSVISAATDSKPSTRTSPPFVNNTKPIVAKSPVTVTASSETNKKSQKINKKASPRVSLWTKLFGKFRSNKKKS
Protein: Protein COS10 (P52924)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Subcellular location: Membrane; Multi-pass membrane protein.
Interaction partners:
Sequence:
MGEEIRLLSSKGLETHSSFCLPEDIFRNRLTWLCSEIRNSGFWIWSLSWLPLAVWWGMASTWFYPLLTSVVLILALIAILPVVQIQYSKYTLSNQLTQLSKEIIKSAPGAYSADWDAVAIHFNSYLYENKAWKTAHFFFNGTDCQEAFRKTILEPAVLRRQNEDPRFSSIEILVPYTEDAVQVYFTKVNAQWRLIHGKKECKLTMLENVKLPKETYRCKLAWSCQRIRISFSPLDFLPDMSDFFICANLSPACLVSYWLIDIFFRMIDDFQNIRPKSMKVDDKMQYLSDIINEQGASPEKWDTIARKTNTRLFEKRVWKNEEFFFDGTDCQAFFERNFSSLLFSKKSASPRSLNVELWKYIQEAQLSCNYEPLP
Protein: Retinol dehydrogenase 5 (EC 1.1.1.209) (EC 1.1.1.315) (EC 1.1.1.53) (11-cis retinol dehydrogenase) (11-cis RDH) (11-cis RoDH) (9-cis retinol dehydrogenase) (Cis-retinol dehydrogenase) (O55240)
Organism: Mus musculus (Mouse)
Function: Catalyzes the oxidation of cis-isomers of retinol, including 11-cis-, 9-cis-, and 13-cis-retinol in an NAD-dependent manner. Has no activity towards all-trans retinal (By similarity). Plays a significant role in 11-cis retinol oxidation in the retinal pigment epithelium cells (RPE). Also recognizes steroids (androsterone, androstanediol) as its substrates (By similarity).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:10739682, ECO:0000269|PubMed:11279029}; Multi-pass membrane protein {ECO:0000255}; Lumenal side {ECO:0000269|PubMed:10739682, ECO:0000269|PubMed:11279029, ECO:0000269|PubMed:16223484}.
Interaction partners:
- Retinoid isomerohydrolase
- Lecithin retinol acyltransferase
- Retinal dehydrogenase 2
- Retinol dehydrogenase 11
- Retinaldehyde dehydrogenase 3
- Aldehyde dehydrogenase 1A1
- Retinol dehydrogenase 10
- Aldehyde dehydrogenase, cytosolic 1
- Retinol dehydrogenase 12
- Diacylglycerol O-acyltransferase 1
Sequence:
MWLPLLLGALLWAVLWLLRDRQSLPASDAFIFITGCDSGFGRLLALQLDQKGFQVLAGCLTPSGAEDLQQMASSRLHTTLLDITDPQNVQQVAKWVKTRVGETGLFGLVNNAGVAGIIGPTPWLTQDDFQRVLSVNTLGPIGVTLALLPLLQQARGRVVNITSVLGRIAANGGGYCVSKFGLEAFSDSLRRDMAPFGVQVSIVEPGFFRTPVTNLESLESTLKACWARLPPAIQAHYGEAFLDTYLRVQRRIMNLICDPELTKVTSCLEHALTARHPRTRYSPGWDAKLLWLPASYLPARVVDAVLTWILPRPAQSVS
Protein: Cysteine proteinase inhibitor 6 (AtCYS-6) (PIP-M) (PRLI-interacting factor M) (Q8H0X6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Specific inhibitor of cysteine proteinases. Probably involved in the regulation of endogenous processes and in defense against pests and pathogens (By similarity).
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
- Cathepsin B-like protease 2
- Cathepsin B-like protease 1
- Cathepsin B-like protease 3
- AT1g27100/T7N9_16
- At5g45880
- RING-type E3 ubiquitin transferase
- Allergen, putative
- Cysteine proteinase inhibitor 3
Sequence:
MMRSRFLLFIVFFSLSLFISSLIASDLGFCNEEMALVGGVGDVPANQNSGEVESLARFAVDEHNKKENALLEFARVVKAKEQVVAGTLHHLTLEILEAGQKKLYEAKVWVKPWLNFKELQEFKPASDAPAITSSDLGCKQGEHESGWREVPGDDPEVKHVAEQAVKTIQQRSNSLFPYELLEVVHAKAEVTGEAAKYNMLLKLKRGEKEEKFKVEVHKNHEGALHLNHAEQHHD
Protein: GTP-binding protein Rheb (EC 3.6.5.-) (Ras homolog enriched in brain) (Q62639)
Organism: Rattus norvegicus (Rat)
Function: Activates the protein kinase activity of mTORC1, and thereby plays a role in the regulation of apoptosis. Stimulates the phosphorylation of S6K1 and EIF4EBP1 through activation of mTORC1 signaling. Has low intrinsic GTPase activity.
Subcellular location: Endomembrane system {ECO:0000250|UniProtKB:Q15382}; Lipid-anchor {ECO:0000250|UniProtKB:Q15382}; Cytoplasmic side {ECO:0000250|UniProtKB:Q15382}. Lysosome membrane {ECO:0000250|UniProtKB:Q15382}; Lipid-anchor {ECO:0000250|UniProtKB:Q15382}; Cytoplasmic side {ECO:0000250|UniProtKB:Q15382}. Golgi apparatus membrane {ECO:0000250|UniProtKB:Q15382}; Lipid-anchor {ECO:0000250|UniProtKB:Q15382}; Cytoplasmic side {ECO:0000250|UniProtKB:Q15382}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q15382}; Lipid-anchor {ECO:0000250|UniProtKB:Q15382}; Cytoplasmic side {ECO:0000250|UniProtKB:Q15382}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q15382}. Note=Farnesylation is required for recruitment to lysosomal membranes, where it activates the mTORC1 complex. {ECO:0000250|UniProtKB:Q15382}.
Interaction partners:
- Serine/threonine-protein kinase mTOR
- Tuberin
- Regulatory-associated protein of mTOR
- Hamartin
- Target of rapamycin complex subunit LST8
- AKT1 substrate 1
- BCL2 interacting protein 3
- DEP domain-containing mTOR-interacting protein
- TBC1 domain family member 7
- Eukaryotic translation initiation factor 4E-binding protein 1
Sequence:
MPQSKSRKIAILGYRSVGKSSLTIQFVEGQFVDSYDPTIENTFTKLITVNGQEYHLQLVDTAGQDEYSIFPQTYSIDINGYILVYSVTSIKSFEVIKVIHGKLLDMVGKVQIPIMLVGNKKDLHMERVISYEEGKALAESWNAAFLESSAKENQTAVDVFRRIILEAEKIDGAASQGKSSCSVM
Protein: Synaptojanin-1 (EC 3.1.3.36) (Synaptic inositol 1,4,5-trisphosphate 5-phosphatase 1) (p150) (O18964)
Organism: Bos taurus (Bovine)
Function: Phosphatase that acts on various phosphoinositides, including phosphatidylinositol 4-phosphate, phosphatidylinositol (4,5)-bisphosphate and phosphatidylinositol (3,4,5)-trisphosphate. Has a role in clathrin-mediated endocytosis (By similarity). Hydrolyzes PIP2 bound to actin regulatory proteins resulting in the rearrangement of actin filaments downstream of tyrosine kinase and ASH/GRB2.
Subcellular location: Cytoplasm, perinuclear region {ECO:0000269|PubMed:9199318}.
Interaction partners:
- Inositol polyphosphate-4-phosphatase type I A
- phosphatidylinositol-3,4-bisphosphate 4-phosphatase
- Amphiphysin
- PIP5K1A protein
- Phosphatidylinositol 4-kinase beta
- Phosphatidylinositol-3-phosphatase SAC1
- Phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN
- Phosphatidylinositol-4-phosphate 5-kinase type 1 gamma
- Phosphatidylinositol 4-kinase type 2
- phosphoinositide 5-phosphatase
Sequence:
MAFSKGFRIYHKLDPPPFSLIVETRHKEECLMFESGAVAVLSSAEKEAIKGTYSKVLDAYGLLGVLRLNLGDIMLHYLVLVTGCMSVGKIQESEVFRVTSTEFISLRVDSSDEDRISEVRKVLNSGNFYFAWSASGVSLDLSLNAHRSLQEHTTDNRFSWNQSLHLHLKHYGVNCADWLLRLMCGGVEIRTIYAAHKQAKACLISRLSCERAGTRFNVRGTNDDGHVANFVETEQVVYLDDSVSSFIQIRGSVPLFWEQPGLQVGSHRVRMSRGFEANAPAFDRHFRTLKNLYGKQIIVNLLGSKEGEHMLSKAFQSHLKASEHAADIQMVNFDYHQMVKGGKAEKLHSVLKPQVQKFLDYGIFHFDGSEVQRCQSGTVRTNCLDCLDRTNSVQAFLGLEMLTKQLEALGLAEKPQLVTRFQEVFRSMWSVNGDSISKIYAGTGALEGKAKLKDGARSVSRTIQNNFFDSSKQEAIDVLLLGNTLNSDLADKARALLTTGSLRVSEQTLQSASSKVLKSMCENFYKYSKPKKIRVCVGTWNVNGGKQFRSIAFKNQTLTDWLLDAPKLAGIQEFQDKRSKPMDIFPIGFEEMVELNAGNIVNASTTNQKLWAAELQKTISRDNKYVLLASEQLVGVCLFVFIRPQHAPFIRDVAVDTVKTGMGGATGNKGAVAIRMLFHTTSLCFVCSHFAAGQSQVKERNDDFLEIARKLSFPMGRLLFSHDYVFWCGDFNYRIDLPNEEVKELIRQQNWDSLIAGDQLINQKNAGQIFRGFLEGKVTFAPTYKYDLFSDDYDTSEKCRTPAWTDRVLWRRRKWPFDRSAEDLDLLNASFQDESKILYTWTPGTLLHYGRAELKTSDHRPVVALIDIDIFEVEAEERQNIYKEVIAVQGPPDGTVLVSIKSSLPENNFFNDALIDELLQQFTNFGEVILIRFVEDKMWVTFLEGSSALNVLNLNGKELLGRTITITLKSPDWIKTLEEEMSLEKINVPLPSSTSSTLLGEDAEVTADFDMEGDVDDYSAEVEEILPQHLQPSSSSALARPPVLHPGPVPASHLPYRRGPVPSLPVRPSRAPSRTPGPPASQSSPVDTLPATQLQQKDSSQTLEPKRPPPPRPVAPPARPAPPQRPPPPSGARSPAPARERVWSTRKAQERPRRDNLGGSQLPPQGGLPGPGLAGHSAARPIIPPRAGVISAPESHGRVSAGRLTPESQRKTXEVLKGPALLPEPLKPQAALPVPPSLAPPSQEMQEPLIAVAAPLAQSALQPSLETPPQPPPRSRSSHSLPSDAPAAAAGATIRVTGEKQTGVSAVRLDCPLKSDPFEDLSLN
Protein: Patched-related protein 18 (Patched domain-containing protein 18) (Q9XWL9)
Organism: Caenorhabditis elegans
Function: Transporter, which promotes the endocytosis-mediated degradation of hedgehog-related proteins such as grl-7 in order to establish the capacity of progenitor cells to maintain quiescence in arrested L1 stage larvae.
Subcellular location: Apical cell membrane {ECO:0000269|PubMed:33872306}; Multi-pass membrane protein {ECO:0000255}. Note=Localizes to the apical cell membrane during the 3-fold stage during embryogenesis. {ECO:0000269|PubMed:33872306}.
Interaction partners:
- Calcineurin-like phosphoesterase domain-containing protein
- G_PROTEIN_RECEP_F1_2 domain-containing protein
- Ground-like domain-containing protein
- Ground-like domain-containing protein
- Ground-like domain-containing protein
- Ground-like domain-containing protein
Sequence:
MKSISQCLGNVSLWIEQQTHDMFYWVGLKIADYPKWTLFITTIWALLMAGGVVRFKEVNNVRDHFSATNSPSRYEYRVAREFFQELGSPFHVVVAMQAADGGSLLRPKYIDKALEIEDFLQYKLKGSFGNQSYSYSDFCGTQCETSDAVSIFLSMFRDQQIKKTAHVKLTYPSMDVFGHRVYLANNIFQVKINNRSSIIEESKLVAINFHAIYNNETMYEIMKEWEQKLFAYTLSTENDPLIRVYVTSEGLVSEEVRRTGILAMPLMGVTFLIILAFTILTTLKRDPVKSKPFEAFLGVICPILSLCASFGHLFWMGFEYLPIVTVVPFLILSIGVDDVFIFIHAWHRTPYKHSVRDRMAETLADAGPSISITSLTNLLSFAIGIFTPTPAIYTFCVFISTAVIYDYIYQIFFFSAVLVLSGEREEQRKNAYLWWKDVPLPEEPTGKQKKETIVSRVLGKVLDFWVDFIMAKWSKFLIGAIMITYWIFMARGVMEIAVGLSSEKLFLDDSPLLPLVRLQTNVIFKEGGQVAVFVNNPGNMSEPDAVPEIMRILRRFEVANNSVGAASTHMWLLPYLPYVGEQEHGSIEFKYRYLPEFFKLTEFRRWSHFVNLGNHQDCLSEKPSCLQKFVFSTGFHDAVSWSDRLALLENWREMASEYQHLNLTIYEDFSMYSDQLLTIVPVTQSTVFCALICMIMILTLFTPSPVTIVTSTAAVLSINLGVFGCLVYMNIDLDPISMTTLLMAIGFSVDFVAHITWHYYKGDFHSKRARIRHALAGIAWPMFQAGTSTMLAITVLALVHAYMVQVFVKVVVLVIFLGMFHGLVVLPIVFSALPFTKTSGPQKKKVAPLQMHEAGPIPKKEEPKVIKVNGEEDEEDEKTTKEEPVEKSVRSAERA
Protein: BTB/POZ domain-containing adapter for CUL3-mediated RhoA degradation protein 3 (hBACURD3) (BTB/POZ domain-containing protein KCTD10) (Potassium channel tetramerization domain-containing protein 10) (Q9H3F6)
Organism: Homo sapiens (Human)
Function: Substrate-specific adapter of a BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complex. The BCR(BACURD3) E3 ubiquitin ligase complex mediates the ubiquitination of target proteins, leading to their degradation by the proteasome (By similarity).
Subcellular location: Nucleus {ECO:0000269|PubMed:19125419}.
Interaction partners:
- Cullin-3
- UBX domain-containing protein 1
- UBX domain-containing protein 7
- FAS-associated factor 1
- BTB/POZ domain-containing adapter for CUL3-mediated RhoA degradation protein 1
- BTB/POZ domain-containing adapter for CUL3-mediated RhoA degradation protein 2
- E3 ubiquitin-protein ligase RBX1
- DNA polymerase delta subunit 2
- BTB/POZ domain-containing protein KCTD17
- Ubiquitin carboxyl-terminal hydrolase 25
Sequence:
MEEMSGESVVSSAVPAAATRTTSFKGTSPSSKYVKLNVGGALYYTTMQTLTKQDTMLKAMFSGRMEVLTDSEGWILIDRCGKHFGTILNYLRDGAVPLPESRREIEELLAEAKYYLVQGLVEECQAALQNKDTYEPFCKVPVITSSKEEQKLIATSNKPAVKLLYNRSNNKYSYTSNSDDNMLKNIELFDKLSLRFNGRVLFIKDVIGDEICCWSFYGQGRKIAEVCCTSIVYATEKKQTKVEFPEARIYEETLNILLYEAQDGRGPDNALLEATGGAAGRSHHLDEDEERERIERVRRIHIKRPDDRAHLHQ
Protein: Thiazole synthase (EC 2.8.1.10) (Q72AA3)
Organism: Nitratidesulfovibrio vulgaris (strain ATCC 29579 / DSM 644 / CCUG 34227 / NCIMB 8303 / VKM B-1760 / Hildenborough) (Desulfovibrio vulgaris)
Subcellular location: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00443}.
Interaction partners:
- ThiH protein
- ThiH protein, putative
- Thiamine biosynthesis protein ThiS
- ThiF family protein
- Phosphomethylpyrimidine synthase
- ThiamineS protein
- Thiamine biosynthesis protein ThiS
- Thiamine-phosphate synthase
- 1-deoxy-D-xylulose-5-phosphate synthase
- hydroxymethylpyrimidine kinase
Sequence:
MTHDTRHDDTFVLGGQALESRLFIGTGKYGTDALIPAVADASGSQVITVALRRVDLGNPKGNVLAHIPAHMRLLPNTSGARTVDEAVRIARLARAAGCGDWIKIEIISDSRYLLPDGYATARATEILAAEGFTVLPYMNPDLYVARDLENAGAAAIMPLGAPIGTNRGLRTREMIGILIEEMSLPIVVDAGIGKPSEACDAMEMGAAACLVNTAIASAGDPVAMARAFGEAVRAGRRAFLARAGRVLDGRAEASSPLTGFLGGQA
Protein: Xanthine dehydrogenase 2 (AtXDH2) (EC 1.17.1.4) (F4JLI5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Key enzyme involved in purine catabolism. Catalyzes the oxidation of hypoxanthine to xanthine and the oxidation of xanthine to urate. Regulates the level of ureides and plays a role during plant growth and development and senescence.
Interaction partners:
- Uricase
- Xanthine dehydrogenase 1
- Hypoxanthine phosphoribosyltransferase
- Cyclic pyranopterin monophosphate synthase, mitochondrial
- GTP 3',8-cyclase, mitochondrial
- Uric acid degradation bifunctional protein TTL
Sequence:
MEQNEFMEAIMYVNGVRRVLPDGLAHMTLLEYLRDLGLTGTKLGCGEGGCGSCTVMVSSYDRESKTCVHYAVNACLAPLYSVEGMHVISIEGVGHRKLGLHPLQESLASSHGSQCGFCTPGFVMSMYALLRSSKNSPSEEEIEECLAGNLCRCTGYRPIIDAFRVFAKSDDALYSGLSSLSLQDGSNICPSTGKPCSCGSKTTSEAATCNEDRFQSISYSDIDGAKYTDKELIFPPELLLRKLAPLKLGGNEGITWYRPVSLQNLLELKANFPDAKLLVGNTEVGIEMRLKRLQYPVLISAAQVPELNALNVNDNGIEVGSALRLSELLRLFRKVVKERPAHETSACKAFIEQLKWFAGTQIRNVACIGGNICTASPISDLNPLWMASRAEFRIINCNGDVRSIPAKDFFLGYRKVDMGSNEILLSVFLPWTRPLEYVKEFKQAHRRDDDIAIVNGGMRVFLEEKGQQLFVSDASIVYGGVAPLSLRARNTEELLIGKNWNKCLLQDALKVIQSDVLIKEGAPGGMVEFRKSLTLSFFFKFFLWVTHHVNNVNPTIETFPPSHMSAVQLVPRFSRIGKQDYETVKQGTSVGLPEVHLSARMQVTGEAEYTDDTPLPPCTLHAALVLSKVPHARILSVDDSAAKSSSGFVGLFLAKDVPGNNMIGPIVADEELFATDVVTCVGQVIGVLVADTHENAKTAARKVDVRYQELPAILSIKEAINAKSFHPNTERRLRKGDVELCFQSGQCDRIIEGEVQMGGQEHFYLEPNGSLVWTIDGGNEVHMISSTQAPQQHQKYVSHVLGLPMSKVVCKTKRLGGGFGGKETRSAFIAAAASVPSYLLNRPVKLILDRDVDMMITGHRHSFVGKYKVGFTNEGKILALDLEIYNNGGNSMDLSLSNLERAMFHSDNVYEIPHVRIVGNVCFTNFPSNTAFRGFGGPQGMLITENWIQRIAAELDKIPEEIKEMNFQVEGSITHYFQSLQHCTLHQLWKELKVSSNFLKTRREADEFNSHNRWKKRGVAMVPTKFGISFTTKFMNQAGALVHVYTDGTVLVTHGGVEMGQGLHTKVAQVAATAFNILLSSVFVSETSTDKVPNASPTAASASSDMYGAAVLDACEQIIARMEPVASKHNFNTFSELASACYFQRIDLSAHGFHIVPELEFDWVSGKGNAYRYYTYGAAFAEVEIDTLTGDFHTRKADIMLDLGYSLNPTIDIGQIEGAFVQGLGWVALEELKWGDAAHKWIKPGSLLTCGPGSYKIPSINDMPFQLNVSLLKGNPNAKAIHSSKAVGEPPFFLAASAFFAIKEAIKAARSEVGLTNWFPLETPATPERIRMACFDEFSAPFANSDFCPKLSV
Protein: Cyclin-L1 (Cyclin-L) (Cyclin Ania-6a) (Q52KE7)
Organism: Mus musculus (Mouse)
Function: Involved in pre-mRNA splicing. Functions in association with cyclin-dependent kinases (CDKs). May play a role in the regulation of RNA polymerase II (pol II). Inhibited by the CDK-specific inhibitor CDKN1A/p21.
Subcellular location: [Isoform 1]: Nucleus speckle {ECO:0000269|PubMed:11683997}. Nucleus, nucleoplasm {ECO:0000250|UniProtKB:Q9UK58}. Note=Found in nuclear intrachromatin granules clusters (IGC), also called nuclear speckles, which are storage compartments for nuclear proteins involved in mRNA processing.; SUBCELLULAR LOCATION: [Isoform 2]: Nucleus {ECO:0000269|PubMed:11683997}. Cytoplasm {ECO:0000269|PubMed:11683997}.
Interaction partners:
- Cyclin-dependent kinase 19
- Cyclin-dependent kinase 9
- Cyclin-dependent kinase 11B
- Cyclin-dependent kinase 12
- Negative elongation factor E
- RNA polymerase-associated protein LEO1
- Parafibromin
- FACT complex subunit SSRP1
- Cyclin-T1
- Retinoblastoma-associated protein
Sequence:
MASGPHPTSTAAAAAAAAASASSAAPSAGGSSSGTTTTTTTTTGGILIGDRLYSEVSLTIDHSLIPEERLSPTPSMQDGLDLPSETDLRILGCELIQAAGILLRLPQVAMATGQVLFHRFFYSKSFVKHSFEIVAMACINLASKIEEAPRRIRDVINVFHHLRQLRGKRTPSPLILDQNYINTKNQVIKAERRVLKELGFCVHVKHPHKIIVMYLQVLECERNQTLVQTAWNYMNDSLRTNVFVRFQPETIACACIYLAARALQIPLPTRPHWFLLFGTTEEEIQEICIETLRLYTRKKPNYELLEKEVEKRKVALQEAKLKAKGLNLDGTPALSTLGGFSPASKPSSPREVKAEEKSPVSINVKTVKKEPEDRQQASKSPYNGVRKDSKRSRTSRSASRSRSRTRSRSRSHSPRRHYNNRRSRSGTYSSRSRSRSRSHSESPRRHHNHGSPHLKAKHTREDLKSSNRHGHKRKKSRSRSQSKTRDHSDVTKKHRHERGHHRDRRERSRSFERSHKGKHHGGSRSGHGRHRR
Protein: Small ribosomal subunit protein uS2 (Q383K0)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496, ECO:0000256|HAMAP-Rule:MF_03015}.
Interaction partners:
- 40S ribosomal protein S13, putative
- 40S ribosomal protein S14
- 40S ribosomal protein S18, putative
- 40S ribosomal protein S23, putative
- Small ribosomal subunit protein uS4
- 40S ribosomal protein S15, putative
- 40S ribosomal protein S5, putative
- Small ribosomal subunit protein uS5
- Ribosomal protein S19, putative
- 40S ribosomal protein S15a, putative
Sequence:
MTSVSSGAKVLRMKESDVQKLLAMHCHLGTKNSSSAMKKYIHGRTSDGTNIIDIHMTWEKLILAARVIAAVENPQDVTVCSTRLFGQRAIFKFSQLVGTSFLGGRFIPGTFTNQIQKKFMQPRVLVVTDPRTDHQALREASLVNIPVIAFCDTDAPLEFVDIAIPCNNRGRHSISMMYWLLAREVLRLRGTIPRSVPWEVKVDLFFYRDPEEALKQEEATAAAEVHEEADEGYGWVERDNTWEQ