wanglab/gogpt-training-data huggingface dataset:
Protein: DNA polymerase epsilon subunit 3 (Q22798)
Organism: Caenorhabditis elegans
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Probable DNA polymerase epsilon subunit 2
- Transcription factor CBF/NF-Y/archaeal histone domain-containing protein
- DNA polymerase epsilon catalytic subunit
- Bromodomain adjacent to zinc finger domain protein 1A
- Chromatin-remodeling complex ATPase chain isw-1
- Probable DNA polymerase delta small subunit
- Replication factor C subunit 1
- DNA polymerase
- Nuclear transcription factor Y subunit nfyc-1
- DNA polymerase delta catalytic subunit
Sequence:
MSSNDVDQNDDRIAQMMMPAAIVTRLMKEDNISASKDARDVIARAAAVFLINLSDVSAQSARDQKHKTISGDDVVKGLRELENTSIHNHCKSANDKWKVISQQKALARKNPVESSSVNAEMDDDIIDDTPVDDSLMN
Protein: Methionine aminopeptidase 2 (MAP 2) (MetAP 2) (EC 3.4.11.18) (Peptidase M) (Q38C98)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03175}.
Interaction partners:
- Methionine aminopeptidase
- 60S ribosomal protein L35, putative
- 60S ribosomal protein L5, putative
- 60S ribosomal protein L17, putative
- 40S ribosomal protein S15a, putative
- 40S ribosomal protein S18, putative
- Small ribosomal subunit protein uS5
- 40S ribosomal protein S15, putative
- 40S ribosomal protein S14
- Large ribosomal subunit protein uL5
Sequence:
MPPKGGGAGSKKQQGGKKCKDDEADFDAQLAKALQEVQVSKDKQGGDANKKAQKGKQRTSKQESNGEANDNNDASDPKVVSTADHPDNPYPQVAEGMKRQTWPEPTIPVSQQFARGNFPVGIICEHPGEVNAYRYSSEEKRAMEHATEEQVQDLRCAAEVHRQVRRYAQSFIKPGISLLSMTDRIEKKLEELIEKDGLNRGQAFPTGCSLNHVAAHYTPNTGDKCVLMYDDVMKVDFGTQINGRIIDCAWTVAFKDEYEPLLTAVKEATYEGVKQAGIDVRLCDVGAAIQEVMESYEVELNGKVYPVKSIRNLSGHTIAPYVIHGGKSVPIVRGGEATRMEEGELFAIETFGSTGRGFVQEDMECSHYMMVPGGEKTQVRSDKAQQLLRHIHKTYNTLAFARKWLDRDGHDRHLLNLNQLVEAGAVNKYPPLCDIRGCYTAQLEHTLILKPTAKEILSKGDDY
Protein: MIOREX complex component 4 (Mitochondrial organization of gene expression protein 4) (Q12467)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of MIOREX complexes, large expressome-like assemblies of ribosomes with factors involved in all the steps of post-transcriptional gene expression.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:14562095}. Mitochondrion membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MTVLYTSASLKKMKCLAFNMGMNCVRTVSHARSGGAKFGGRNVFNIFDSKTPDSVRIKAFKNTIYQSAMGKGKTKFSAMEINLITSLVRGYKGEGKKNAINPLQTNVQILNKLLLTHRLTDKDILEGMNLAAGPVNVAIPRDITPQEEKKKVELRNRKAENMDLHPSRKMHIKELLHSLNLDMCNDEEVYQKISLYLQKNEESRTSVGASQQNHVDIDINSLKRYLQNIEKKARQKSAIDKQKKNQARIYQWNTQSFSEIVPLSAGNILFKREPNRLWKRLQNGISVFLGSNGGGKKSKTTKKVLQGNNILLHSLENNKDMTLSNNFDHSVFNINFTDLFGVINASGSPPDRVLNEINEIELKGWKCVGNLYDNNKIVVFQSSNPLLEDTKIPQKSFTNSKRFLISLSALLASFFAYYRYRLSQRQESKK
Protein: CDC42 effector protein 4 (J3KRZ9)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MPILKQLVSSSVHSKRRSRADLTAEMISAPLGDFRHTMHVGRAGDAFGDTSFLNSKAGEPDGESLDEQPSSSSSKRSLLSRKFRGSKRSQSVTRGEREQRDMLGSLRDSALFVKNAMSLPQLNEKEA
Protein: ZNF468 protein (Q6P514)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MNVARFLIKKQPLHITIDFILERNLTNGRNVTKVFSCKSNLKTHKKIHIEEKPYRGKVCDKVFAYNAYLAKHTRIHTGEKLIISVMSVARPLVKIHTL
Protein: Prothoracicotropic hormone, isoform G (A0A0S0WMK2)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MAMALLSLTNKGIASQYASDEGLDEMVGLRSLEHRAEEQQPDRSTSKMLSALFGFSPSTPHPTEMAMVMPHQLPPMYYNDFYEDLVTTKRNDVHSAGCDCKVTNELVDLGGLHFPRFLMNAVCESGAGRDLAKCSHGSNCRPLEYKVKVLAQTSQSDHPYSWMNKDQPWQFKTVTVTAGCFCTK
Protein: Nuclear factor 1 (A0A8I5ZYT8)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|RuleBase:RU000690}.
Interaction partners:
Sequence:
MHERARARGRRTRRWGCRRGHRSSGSLGLQPRTGRSAGWGGRVGGGRAGGGSAGGAGSSPRASPRASPRASPPAVASPHSAMDEFHPFIEALLPHVRAFAYTWFNLQARKRKYFKKHEKRMSKDEERAVKDELLGEKAEVKQKWASRLLAKLRKDIRPECREDFVLAVTGKKAPGCVLSNPDQKGKMRRIDCLRQADKVWRLDLVMVILFKGIPLESTDGERLVKAAACAHPVLCVQPHHIGVAVKELDLYLAYFVRERDAEQSSSPRTGVGSDQEDSKPITLDTTDFQESFVTSGVFSVTELIQVSRTPVVTGTGPNFSLGELQGHLAYDLNPASAGMRRTLPSTSSSGSKRHKSGSMEEDVDTSPGGDYYTSPNSPTSSSRNWTEDMEGGISSPVKKTEMDKSPFNSPSPQDSPRLSSFTQHHRPVIAVHSGIARSPHPSSALHFPATPILPQTASTYFPHTAIRYPPHLNPQDPLKDLVSLACDPATQQPGPPALRPARPLQTVPLWD
Protein: TBC1 domain family, member 9B (With GRAM domain) (A1L3A9)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MWLSPEEVLVANALWVTERANPFFVLQRRRGHGRGGGLTGLLVGTLDVVLDSSARVAPYRILHQTQDSQVYWTVACGSSRKEITKHWEWLENNLLQTLSIFDSEEDITTFVKGKIHGIIAEENKNLQPQGDEDPGKFKEAELKMRKQFGMPEGEKLVNYYSCSYWKGRVPRQGWLYLTVNHLCFYSFLLGKEVSLVVQWVDITRLEKNATLLFPESIRVDTRDQELFFSMFLNIGETFKLMEQLANLAMRQLLDSEGFLEDKALPRPIRPHRNISALKRDLDARAKNECYRATFRLPRDERLDGHTSCTLWTPFNKLHIPGQMFISNNYICFASKEEDACHLIIPLREVTIVEKADSSSVLPSPLSISTKSKMTFLFANLKDRDFLVQRISDFLQKTPSKQPGSIGSRKASVVDPSTESSPAPQEGSEQPASPASPLSSRQSFCAQEAPTASQGLLKLFQKNSPMEDLGAKGAKEKMKEESWHIHFFEYGRGVCMYRTAKTRALVLKGIPESLRGELWLLFSGAWNEMVTHPGYYAELVEKSTGKYSLATEEIERDLHRSMPEHPAFQNELGIAALRRVLTAYAFRNPTIGYCQAMNIVTSVLLLYGSEEEAFWLLVALCERMLPDYYNTRVVGALVDQGIFEELTRDFLPQLSEKMQDLGVISSISLSWFLTLFLSVMPFESAVVIVDCFFYEGIKVILQVALAVLDANMEQLLGCSDEGEAMTMLGRYLDNVVNKQSVSPPIPHLRALLSSSDDPPAEVDIFELLKVSYEKFSSLRAEDIEQMRFKQRLKVIQSLEDTAKRSVVRAIPVDIGFSIEELEDLYMVFKAKHLASQYWGCSRTMAGRRDPSLPYLEQYRIDASQFRELFASLTPWACGSHTPLLAGRMFRLLDENKDSLINFKEFVTGMSGMYHGDLTEKLKVLYKLHLPPALSPEEAESALEAAHYFTEDSSSEALPQEEQEGSGSEERGEEKGTSSPDYRHYLRMWAKEKEAQKETIKDLPKMNQEQFIELCKTLYNMFSEDPMEQDLYHAIATVASLLLRIGEVGKKFSARTGRKPRDCATEEDEPPAPELHQDAARELQPPAAGDPQAKAGGDTHLGKAPQESQVVVEGGSGEGQGSPSQLLSDDETKDDMSMSSYSVVSTGSLQCEDLADDTVLVGGEACSPTARIGGTVDTDWCISFEQILASILTESVLVNFFEKRVDIGLKIKDQKKVERQFSTASDHEQPGVSG
Protein: Transcriptional regulator Myc (c-Myc) (P06646)
Organism: Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri)
Function: Transcription factor that binds DNA in a non-specific manner, yet also specifically recognizes the core sequence 5'-CAC[GA]TG-3'. Activates the transcription of growth-related genes.
Subcellular location: Nucleus.
Interaction partners:
Sequence:
NSSLASKNYDYDYDSIQPYFYVDNEDEDFYHQQPGQLQPPAPSEDIWKKFELLPTPPLSPSRPSLSSIFPSTADQLEMVTEFLGDDVVNQSFICDADYSQTFLKSIIIQDCMWSGFSATAKLEKVVSERLASLQTARKDSAVGDNAECPTRLNANYLQDPNTSASECIGPNTSASECIGPSVVFPYPITETPKPSKVAPPTDLALDTPPNSGSSSSSGSDSEDDDEEEDDEDEEEIDVVTVEKRQAVKRCDPSTSETRHHSPLVLKRCHVSTHQHNYAAHPSTRHEQPAVKRLRLENSSSRVLKQISSNRKCSSPRTSDTEDYDKRRTHNVLERQRRNELKLSFFALRDEIPDVANNEKAAKVVILKKATECIYSMQTDEQRLVNLKEQLRRKSEHLKQKLAQLQNSCLSSKRH
Protein: Follitropin subunit beta (Follicle-stimulating hormone beta subunit) (FSH-B) (FSH-beta) (Follitropin beta chain) (P01225)
Organism: Homo sapiens (Human)
Function: Together with the alpha chain CGA constitutes follitropin, the follicle-stimulating hormone, and provides its biological specificity to the hormone heterodimer. Binds FSHR, a G protein-coupled receptor, on target cells to activate downstream signaling pathways. Follitropin is involved in follicle development and spermatogenesis in reproductive organs.
Subcellular location: Secreted {ECO:0000269|PubMed:2494176}. Note=Efficient secretion requires dimerization with CGA. {ECO:0000269|PubMed:2494176}.
Interaction partners:
- Follicle-stimulating hormone receptor
- Glycoprotein hormones alpha chain
- Lutropin-choriogonadotropic hormone receptor
- Thyrotropin receptor
- Gonadotropin-releasing hormone receptor
- Glucagon-like peptide 1 receptor
- Vasoactive intestinal polypeptide receptor 2
- Adrenocorticotropic hormone receptor
- D
- Adenosine receptor A2a
Sequence:
MKTLQFFFLFCCWKAICCNSCELTNITIAIEKEECRFCISINTTWCAGYCYTRDLVYKDPARPKIQKTCTFKELVYETVRVPGCAHHADSLYTYPVATQCHCGKCDSDSTDCTVRGLGPSYCSFGEMKE
Protein: Nuclear pore complex protein (A1YK63)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus, nuclear pore complex {ECO:0000256|RuleBase:RU365072}. Nucleus membrane {ECO:0000256|RuleBase:RU365072}.
Interaction partners:
Sequence:
MADSPFPRSSRSGLLRTTLNSSMAPQNLSHSLLILEKSNAEQNERSLMEDTGDDLDRGKSRMDVLFPQFFDVLQAQGNGQEAFEVIQSLTQVCRGVVEQLELEIDHGMGGEQGARQRESMLTWLRQEINTWRLLHALFYDRILLQTDRQADDEMQDGPTLGGSEKEVIQQLYALNATLREYQLVVDWLEACYDRGEQQNPLHAHDRMMAWENTLFQLENLQGAAFGKGHKIVTRLDPDAPVREKRPLHALDEEDNLRLSRAIFELIRAGRVDDGLKLCKHFGQTWRAAILEGWRLHEDPNFEQNVSVLHEKLPIEGNPRRDIWKRCAWMLADSKNYDEYSRATAGVFSGHLGSLKTLLHSNWHDVLWAHLKVQIDIRVESEIRGCCLKNYQPMPDDYWNGRMTMEQIFEELNVAKDASVRDFAQSQLGIIQRHLILDTCGELIQHMVRWVEKDTSQQSPHQLRFMAHIVLFLRQIGRVEQERQAEKIVAAYVEALIARGEPQLIAYYTASLSNPLQVQLYSRFLEQVEQKRPRELAVDAALQAGLDVEQITRVTVQNIRLAHQPLGEFGEPQSGEISAIDQRKISALEWLIHLPEQRGELLWQANAMIRTYLASSKVECMRQTFRMVPADIVQQLVSLYGSVDNIPPREECCLKEYLCYKAYLSGVDSFVEWNRLQQNRPKKPQTSHAASSQDNFTERMASERKEQAHRSEVVRWEHKVKEQAKQTIELLYNVLMFPDKGWLVDPFIAKLPENAVQLNWDHRLLQMEKLRSICIPEIALFLNEVMFKSGDFAGCVRLADEISSENRQLYKVYTKHKLAELLAKIADASLELLNSKLDPWGYPITT
Protein: IST1 homolog (Q38BY2)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Vta1/callose synthase N-terminal domain-containing protein
- Uncharacterized protein
- SNF-7-like protein, putative
- Uncharacterized protein
- Vacuolar transport protein 4A, putative
- Katanin, putative
- Class-E vacuolar protein-sorting protein 24
- Charged multivesicular body protein 6
- Uncharacterized protein
- Vesicular protein trafficking mediator, putative
Sequence:
MSSFWSKKSTAFNPNKLKANLRMAITRLRMQQNKLVNGIKIQRRQVAELLALQKYESARVRVEQVLRDDVSIEGYEVLALFLDLLSNRVHLITNISDECVSGSSDNRKKGLALCPPELKESITSVLWAAAQLGNVVPELQNVSKCFEAKLGADFVAMSVSNAEFSVNQKIIERLGFNTPSNARCIEYLTNVATEYSIEGYDEQRLLDPSGLVPSVSTTENVGTSLGVDVDTTTLGSVIDPTGVPEGGIIRTPSGFLLPALTQARDELECRLLQLKRG
Protein: DNA annealing helicase and endonuclease ZRANB3 (Annealing helicase 2) (AH2) (Zinc finger Ran-binding domain-containing protein 3) [Includes: DNA annealing helicase ZRANB3 (EC 3.6.4.-); Endonuclease ZRANB3 (EC 3.1.-.-)] (Q5FWF4)
Organism: Homo sapiens (Human)
Function: DNA annealing helicase and endonuclease required to maintain genome stability at stalled or collapsed replication forks by facilitating fork restart and limiting inappropriate recombination that could occur during template switching events. Recruited to the sites of stalled DNA replication by polyubiquitinated PCNA and acts as a structure-specific endonuclease that cleaves the replication fork D-loop intermediate, generating an accessible 3'-OH group in the template of the leading strand, which is amenable to extension by DNA polymerase. In addition to endonuclease activity, also catalyzes the fork regression via annealing helicase activity in order to prevent disintegration of the replication fork and the formation of double-strand breaks.
Subcellular location: Nucleus {ECO:0000269|PubMed:22704558, ECO:0000269|PubMed:22705370, ECO:0000269|PubMed:22759634}. Chromosome {ECO:0000269|PubMed:22704558, ECO:0000269|PubMed:22705370, ECO:0000269|PubMed:22759634}. Note=Following DNA damage, recruited to sites of DNA damage and stalled replication forks by polyubiquitinated PCNA (PubMed:22704558, PubMed:22705370, PubMed:22759634). {ECO:0000269|PubMed:22704558, ECO:0000269|PubMed:22705370, ECO:0000269|PubMed:22759634}.
Interaction partners:
- Proliferating cell nuclear antigen
- Fanconi anemia group M protein
- Bifunctional 3'-5' exonuclease/ATP-dependent helicase WRN
- DNA repair protein RAD51 homolog 1
- F-box DNA helicase 1
- DNA replication ATP-dependent helicase/nuclease DNA2
- Structure-specific endonuclease subunit MUS81
- DNA-directed primase/polymerase protein
- RPA-related protein RADX
- Helicase-like transcription factor
Sequence:
MPRVHNIKKSLTPHISCVTNESDNLLDFLPDRLRAKLLPFQKDGIIFALKRNGRCMVADEMGLGKTIQAIGITYFYKEEWPLLIVVPSSLRYPWTEEIEKWIPELSPEEINVIQNKTDVRRMSTSKVTVLGYGLLTADAKTLIDALNNQNFKVVIVDESHYMKSRNATRSRILLPIVQKARRAILLTGTPALGRPEELFMQIEALFPQKFGRWTDYAKRYCNAHIRYFGKRPQWDCRGASNLNELHQLLSDIMIRRLKTEVLTQLPPKVRQRIPFDLPSAAAKELNTSFEEWEKIMRTPNSGAMETVMGLITRMFKQTAIAKAGAVKDYIKMMLQNDSLKFLVFAHHLSMLQACTEAVIENKTRYIRIDGSVSSSERIHLVNQFQKDPDTRVAILSIQAAGQGLTFTAASHVVFAELYWDPGHIKQAEDRAHRIGQCSSVNIHYLIANGTLDTLMWGMLNRKAQVTGSTLNGRKEKIQAEEGDKEKWDFLQFAEAWTPNDSSEELRKEALFTHFEKEKQHDIRSFFVPQPKKRQLMTSCDESKRFREENTVVSSDPTKTAARDIIDYESDVEPETKRLKLAASEDHCSPSEETPSQSKQIRTPLVESVQEAKAQLTTPAFPVEGWQCSLCTYINNSELPYCEMCETPQGSAVMQIDSLNHIQDKNEKDDSQKDTSKKVQTISDCEKQALAQSEPGQLADSKEETPKIEKEDGLTSQPGNEQWKSSDTLPVYDTLMFCASRNTDRIHIYTKDGKQMSCNFIPLDIKLDLWEDLPASFQLKQYRSLILRFVREWSSLTAMKQRIIRKSGQLFCSPILALEEITKQQTKQNCTKRYITKEDVAVASMDKVKNVGGHVRLITKESRPRDPFTKKLLEDGACVPFLNPYTVQADLTVKPSTSKGYLQAVDNEGNPLCLRCQQPTCQTKQACKANSWDSRFCSLKCQEEFWIRSNNSYLRAKVFETEHGVCQLCNVNAQELFLRLRDAPKSQRKNLLYATWTSKLPLEQLNEMIRNPGEGHFWQVDHIKPVYGGGGQCSLDNLQTLCTVCHKERTARQAKERSQVRRQSLASKHGSDITRFLVKK
Protein: Alpha-defensin 5 (Defensin-related cryptdin-5) (P28312)
Organism: Mus musculus (Mouse)
Function: Probably contributes to the antimicrobial barrier function of the small bowel mucosa.
Subcellular location: Secreted.
Interaction partners:
- T-cell surface glycoprotein CD4
Sequence:
MKTFVLLSALVLLAFQVQADPIHKTDEETNTEEQPGEEDQAVSISFGGQEGSALHEELSKKLICYCRIRGCKRRERVFGTCRNLFLTFVFCCS
Protein: Complement C1q subcomponent subunit C (P31722)
Organism: Rattus norvegicus (Rat)
Function: C1q associates with the proenzymes C1r and C1s to yield C1, the first component of the serum complement system. The collagen-like regions of C1q interact with the Ca(2+)-dependent C1r(2)C1s(2) proenzyme complex, and efficient activation of C1 takes place on interaction of the globular heads of C1q with the Fc regions of IgG or IgM antibody present in immune complexes.
Subcellular location: Secreted.
Interaction partners:
- Complement C1q subcomponent subunit A
- Complement C1q subcomponent subunit B
- Complement C1s subcomponent
- Complement C1r subcomponent
- Complement C4
- Plasma protease C1 inhibitor
- Complement C2
- Complement C4A
- Ig-like domain-containing protein.
- Calreticulin
Sequence:
MVVGTSCQPQHGLYLLLLLLALPLRSQANAGCYGIPGMPGLPGTPGKDGHDGLQGPKGEPGIPAIPGTQGPKGQKGEPGMPGHRGKNGPMGTSGSPGDPGPRGPPGEPGEEGRYKQKHQSVFTVTRQTAQYPAANGLVKFNSAITNPQGDYNTNTGKFTCKVPGLYYFVHHTSQTANLCVQLLLNNAKVTSFCDHMSNSKQVSSGGVLLRLQRGDEVWLAVNDYNGMVGTEGSDSVFSGFLLFPD
Protein: E3 ubiquitin-protein ligase ubr1 (EC 2.3.2.27) (N-end-recognizing protein) (N-recognin-1) (RING-type E3 ubiquitin transferase ubr1) (O60152)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Ubiquitin ligase protein which is a component of the N-end rule pathway. Recognizes and binds to proteins bearing specific N-terminal residues that are destabilizing according to the N-end rule, leading to their ubiquitination and subsequent degradation.
Interaction partners:
- Ubiquitin-conjugating enzyme E2 2
- ERAD-associated E3 ubiquitin-protein ligase doa10
- E3 ubiquitin-protein ligase ptr1
- Cell division cycle protein 48
- Probable ubiquitin fusion degradation protein C12B10.01c
- Ubiquitin conjugation factor E4
- Ubiquitin-conjugating enzyme E2 4
- Polyubiquitin
Sequence:
MLQDESSRSLPRSALIRRRLSLFLQSHALMYSFLWSESAKKSLLNEVFSALLGYDHTLWNTLLPERPTIDASFLLRRAQGHSEGDEYRHGTCESKCGHIFRKGEVFYRCKTCSVDSNSALCVKCFRATSHKDHETSFTVSAGSGGCCDCGNAAAWIGDVSCKIHSHEEDATISNDMIDEIPEKLENSIQTTIDCVLDFVLDVFSCSPENLKKMPTLESILQDEKTSRLSENKYGDIDDSCNMYSLVLWNDEKHSFKQFYEQITTALELPNNVFGKKMANIINDIGRACIVTETNIKELLKIGQKLAQINLAVSIRSMRDIFREESCAVLLEWLADIAGSSICGKRNYFSSVICKELVRPWNCGLHNSDLTFRLSLRSLALPEIVAIDSPDIFLNEDHINSSGPSDTSSHMLETDESSIHSRHWYPSNSLPDVLSYASRVRFDYFFLYDLKLWKSLRYKLQELYLGYFITQPGFKEIMGARIAISYRRLAELFLLLDREPEHSVIFFSMQIFTVADVAKLLVTEYDFLTTINATLYTFFTYKKLNTPNYVDQHAMIRTDSAAFHSRRYIHIFHHIQFMLSIPCVAEIVREDLKFLKQYADFFNLFQGMCPYTRAVSQHVEWENDSWMYVLNVSLQVAKLCRHVGNVFMELNTNKLANAINYLISLILYPKARNESWTNTESLTTGITVDERGNSKLIEYDIALQPVSFHHPLHWLLVYLLSFYVERDNYKLLWTQLDLLAVTDHPLRVCAWLSQMRAKLWIRNGTTLRDQAHHYRNLSFHEYTFDLDVLLLQLTLTYGDPDAILPSFISRFQLEDQMYGRFFVPHKHYDVSQVTIMMEEFLLLLISIVCNTAVLDHWDITRRIEYGIAHILCFRPLPYSEITKRTCEHLLEHKQFESTLKKVATFRNAEGINDSGSFTLKDEYFDYVDPFNIHYSRNQREEAENILRRRYSKQHSKHLESVVYEEYHPILHSNITIPILQSDSFVGILWHTIVYAYIYPYDQGKLEGLVNTALHACLLVLMSEKGSEPIFSKKICENRFPVVEGLQEYCNSPDVTLFSVLCQMKNHRNFVYVKEKISLIMKILKSEVPLLYEPVYAETLSISSSKIVQSLSDAEQQEQHLAKVRMAKERQARIMEQFRMQQNKFLENHALFEASDCEMDEADEFSVTSSVSTKLFLDPPIDTCLLCQEELKDKRPYGTLVFVLRSSVLRLFPADDANYVSEVLDIPDSLDHEIQERPFGLAGKRKKVLDSTEAYDYDNYYYEKKGNELHQLKDSFNGFPPDQLDRGLHATGCGHFMHIDCFKNHIATVTLATRANPYRNHPHNLSMKEFLCPLCKALCNTIFPILWRPKEEINFQEAGVLTAPLKNWLVSKTFSFNKDLNQQLLDIETSPSEHTQSYNLNLLDVLQHTLRDSLKDIYTLNTGADNSSDNVEENADNLFQSSVLDHVHFKSVVNNEVPADERLAISDDIFELYRRLDDVIDLNSSLYSDDFIPVNGKLHNVVKLFSYSLCQVEASTRGHIKCSSIPADIWVHNLGKNQQVFLRILSESIKTYTLLCAHDSQKRIGGSIQEFEFISFCQQKRIFGRLLPSLDSPVTKSITDDRVEPLLVKDTFREFAEASVSGLLSCDESFHYLTQLYYTADIVRNLWILLSQRNSLLKCMESVEFEAFDYEQLKGFEHLVIQIWKSLRVDGAGLINFDCCTEDDLNNPHLLFTLYKLLERFSLIFLRKCALLWYCRYGVSFETQPNLNFQNSELSRLQTKMHIPGVIELSNHLCLTASSTEWSLIKHWCNFFTETGPLCDFPRAYYPGIYELVSLPYELDKVFELLLARRCSKCLTEPMEPAICLFCGKLLCFQSHCCSFNGIGECNLHMQQCASDIGIFLIVKKCAILYLNPPVGSFSVAPFLDAYGETDLGLRRGRSQYLSQKRYDETVRTMWLNGSIPSYIARQLDANPDTGGWETL
Protein: UDP-glucuronosyltransferase 1A8 (UGT1A8) (EC 2.4.1.17) (UDP-glucuronosyltransferase 1-8) (UDPGT 1-8) (UGT1*8) (UGT1-08) (UGT1.8) (UDP-glucuronosyltransferase 1-H) (UGT-1H) (UGT1H) (Q9HAW9)
Organism: Homo sapiens (Human)
Function: UDP-glucuronosyltransferase (UGT) that catalyzes phase II biotransformation reactions in which lipophilic substrates are conjugated with glucuronic acid to increase the metabolite's water solubility, thereby facilitating excretion into either the urine or bile. Essential for the elimination and detoxification of drugs, xenobiotics and endogenous compounds. Catalyzes the glucuronidation of endogenous steroid hormones such as androgens and estrogens. Produces dihydrotestosterone (DHT) diglucuronide from the DHT after two subsequent glucoronidation steps. Also catalyzes the glucuronidation of the isoflavones genistein, daidzein, glycitein, formononetin, biochanin A and prunetin, which are phytoestrogens with anticancer and cardiovascular properties. Involved in the glucuronidation of the AGTR1 angiotensin receptor antagonist caderastan, a drug which can inhibit the effect of angiotensin II. Also metabolizes mycophenolate, an immunosuppressive agent.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000305|PubMed:17179145}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
- UDP-glucuronosyltransferase 1A6
- UDP-glucuronosyltransferase 1A3
- UDP-glucuronosyltransferase 1A9
- UDP-glucuronosyltransferase 1A1
- UDP-glucuronosyltransferase 1A10
- UDP-glucuronosyltransferase 1A7
- UDP-glucuronosyltransferase 1A4
- Cytochrome P450 3A4)
- UDP-galactose translocator
- Cytochrome P450 1A1
Sequence:
MARTGWTSPIPLCVSLLLTCGFAEAGKLLVVPMDGSHWFTMQSVVEKLILRGHEVVVVMPEVSWQLGKSLNCTVKTYSTSYTLEDLDREFMDFADAQWKAQVRSLFSLFLSSSNGFFNLFFSHCRSLFNDRKLVEYLKESSFDAVFLDPFDACGLIVAKYFSLPSVVFARGIACHYLEEGAQCPAPLSYVPRILLGFSDAMTFKERVRNHIMHLEEHLFCQYFSKNALEIASEILQTPVTAYDLYSHTSIWLLRTDFVLDYPKPVMPNMIFIGGINCHQGKPLPMEFEAYINASGEHGIVVFSLGSMVSEIPEKKAMAIADALGKIPQTVLWRYTGTRPSNLANNTILVKWLPQNDLLGHPMTRAFITHAGSHGVYESICNGVPMVMMPLFGDQMDNAKRMETKGAGVTLNVLEMTSEDLENALKAVINDKSYKENIMRLSSLHKDRPVEPLDLAVFWVEFVMRHKGAPHLRPAAHDLTWYQYHSLDVIGFLLAVVLTVAFITFKCCAYGYRKCLGKKGRVKKAHKSKTH
Protein: Mannose-1-phosphate guanyltransferase (EC 2.7.7.13) (ATP-mannose-1-phosphate guanylyltransferase) (CASRB1) (GDP-mannose pyrophosphorylase) (O93827)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Function: Involved in cell wall synthesis where it is required for glycosylation. Involved in cell cycle progression through cell-size checkpoint (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Psa2p
- Phosphomannomutase
- Dolichol-phosphate mannosyltransferase subunit 1
- Chitobiosyldiphosphodolichol beta-mannosyltransferase
- Dolichol phosphate-mannose biosynthesis regulatory protein
- Dolichol-phosphate mannosyltransferase subunit 3
- Gal102p
- T-complex protein 1 subunit zeta
- Mannose-6-phosphate isomerase
- Dipeptidyl peptidase 3
Sequence:
MKGLILVGGYGTRLRPLTLTLPKPLVEFGNRPMILHQIEALAAAGVTDIVLAVNYRPEVMVSTLKKYEEEYGVSITFSVEEEPLGTAGPLKLAEEVLKKDDSPFFVLNSDVICDYPFKELADFHKAHGAAGTIVATKVDEPSKYGVIVHDRDTPNLIDRFVEKPVEFVGNRINAGLYILNPSVIDLIEMRPTSIEKETFPILVEQKQLYSFDLEGYWMDVGQPKDFLSGTCLYLTSLSKKHPEKLCKEKYVHGGNVLIDPTAKIHPSALIGPNVTIGPNVVVGEGARIQRSVLLANSQVKDHAWVKSTIVGWNSRIGKWARTEGVTVLGDDVEVKNEIYVNGAKVLPHKSISSNVEKESIIM
Protein: Protein PIN-LIKES 5 (Auxin efflux carrier-like protein 5) (Q9SHL8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in cellular auxin homeostasis by regulating auxin metabolism. Regulates intracellular auxin accumulation at the endoplasmic reticulum and thus auxin availability for nuclear auxin signaling.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:22504182}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Auxin efflux carrier component 5
- Auxin efflux carrier component 8
- Auxin efflux carrier component 6
- Auxin efflux carrier component 4
- Auxin efflux carrier component 7
- Auxin efflux carrier component 3
- Auxin efflux carrier component 2
Sequence:
MGFWSLLEVASMPVIQVLFMSLVGAFMASDRCKLFPVEARNSMNKVVFVLFAPALMFANLAQTVTLEDIISWWFMPVNMGLTFLIGGLLGWLVVKILKPPPYLEGLIVATCSAGNMGNLPIILVPAICDEDKSPFGNRSVCRTVGLSYASFSMALGGFYIWTYTFRLIKGSAMKVQAIEESEKIAIKSSNSDLEADHKTHLLGAPEDKENKVVKEKTGFWRKGVDFLHEILEELLAPPTLGAIIGFIFGAVRWLRNLIIGDDAPLRIVQSTAKLLGDGTIPCMTIILGGNLIQGLRSSAVKPMVVLGIVCVRYIAMPIIGIGIVLTAANLGFLPADPLFQYVLMLQFTLPPAMNIGTMTQLYNVAQDECSVLMLWTYLVAILALTVWSTIFLHLLV
Protein: Dynein axonemal assembly factor 3 (Q32NQ7)
Organism: Xenopus laevis (African clawed frog)
Function: Required for the assembly of axonemal inner and outer dynein arms. Involved in preassembly of dyneins into complexes before their transport into cilia (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}. Dynein axonemal particle {ECO:0000269|PubMed:30561330}.
Interaction partners:
Sequence:
MAAAAGRRMGPSWWGFSPALDLQVHCLQGTIQHLTSSDGLPELNILLVGGGDGRHLLKTICQASRWPHRKLKFFIIESDLELLARHMLFLSLALEHPEQMGLQEKSELFLELFGNSLIRSKTANYLQEKSELFIQCVTDPDYQQCVMPFLNLSSIKFKERDELEDIFKFWRIADPKLFPIDKYWDGKNRRHLGTRYDSRKGAYDWDLSMKLHDRGAGVINSREYNYWREKGVAFMNREGVYDVPNKTLASQMVVPQSSGKVLTRGYWGDITTSPYVAFGIETEEKSLLETANGVHVKSAQEIALHNIISLFHELATGKVYSVPASGQAEAELVKPVGDYKTNGDQTAAETIEEKAEAEDTKQSKYKGFITLNNVEIHFLPLSWVNELHCKGRFTNFFNLLYFSSSMVHLLKPEYKVIAASKATLVLELTKFMVDLQADKVQSYVSIVTKLAQGAGFTSDEPIDWKTHYIARFERGDDSVELQTAQ
Protein: Nucleotidyltransferase family protein (F4JH01)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- At3g56320
- DExH-box ATP-dependent RNA helicase DExH9
- Protein RRP6-like 2
- Zinc finger C3H1 domain protein
- Pentatricopeptide repeat-containing protein At3g03580
- Polyadenylate-binding protein-interacting protein 13
- Polyadenylate-binding protein-interacting protein 11
- At5g59460)
- Zinc finger CCCH domain-containing protein 41
- UTP:RNA uridylyltransferase 1
Sequence:
MENRHLPSKFFSSASSMAQNQLIDSLTSHISLYHSHSSSSSMANTIPNPRSAILRWFSSLSVHQRLSHLTVVDPKFVQILLQMLGYIRTKGPCSFIILPDLPSSSDLPSLCFKKSRGLISRVSESNESERFVFDSTRLFGSGEGERAQDCSCSVNSLDSVVMAEEFLTNVDRFVETMDVLSDGAFLRGEESDLGSNWVELEWLKAKGYYSMEAFVANRLEVSMRLAWLNTNSGKRRGIKLKEKLNAAAAAANSYWRKKACVDWWQNLDAATHKKIWTCLFGKSAKSVIYEILREANQAQQGEMWLFNFASARKGRTDTSAVSFCDMILEPNSVPRKPITVASNLSGLYVLQEFASLLILCQNGLVPVHSVFFSSMGTITTLVDCILRKLRGFLMVISIDSVKSELLDDNTHKCSPSSSSNQKLGSTNRKQKGKTRNMKKPTPEAKSDKNVNLSTKNGKKDQAKLEFNKSREAIECKKVPTASTMINDPEASAATMEVVPGLVARKGRTKKKRKEKNKSKKCTSLENNGEVNKSVVNSSAIVKASKCDSSCTSANQHPQEYINAQIIEEHGSFSCERNRSGTCASVNGAANCEYSGEEESHSKAETHVISSDLSSVDPAGGPSCENVNPQKSCCRGDRKEKLTMPNERSRTLDEGESHRIHHQRREAGYGFASSSSEFVSYEWPAVAPMYFSHVSSHLPTATDRLHLDVGHNLHPYVRQPFVSTVQHARNPSIEGSHKQVLSRPMPMSLDWPPMVHSNCGLTTAFTCNYDSGILVDIPEQKNKHELGNECENNWMLEEDFEVHTVSGVDYNQYFGGGVMYWNPSDHLGTGFSRPPSLSSDDSSWAWHEAEMKRSVDDMVAFSSSYSANGLDSPTAASFCSPFHPLGPPNQPLGYVVPGNEISTKILQAPPTTIEGAGEEEVSGTLASLSGDVEGNSGDSLPYPILRPIIIPNMSKSEYKRSYDTKSPNVPPTRREHPRIKRPPSPVVLCVPRAPRPPPPSPVSNSRARRGFPTVRSGSSSPRHWGMRGWFHDGVNWEEPRGAEIVLPWRNKSLAVRPIIQPLPGALLQDHLIAMSQLGRDQEHPDVAFPLQPPELLNCPMQGESLSLIHGILNDEIDSFCKQVAAENMARKPYINWAIKRVTRSLQVLWPRSRTNIFGSSATGLSLPSSDVDLVVCLPPVRNLEPIKEAGILEGRNGIKETCLQHAARYLANQEWVKTDSLKTVENTAIPIIMLVVEVPCDLICSIQSPKDGPDCITVDQDSNGNTEMVGFEDSAAANSLPTNTGNLAIAKSVRLDISFKTPSHTGLQTTQLVKDLTEQFPAATPLALVLKQFLADRTLDQSYSGGLSSYCLVLLITRFLQHEHHLGRSINQNLGGLLMDFLYFFGNVFDPRQMRVSVQGSGIYRNRERGYSIDPIHIDDPLFPTNNVGRNCFRIHQCIKAFSEAYSVLENELTCITSTSDSCGKQQLHNLLPKIIPSIISS