wanglab/gogpt-training-data huggingface dataset:
Protein: ATP-dependent 6-phosphofructokinase (ATP-PFK) (Phosphofructokinase) (EC 2.7.1.11) (Phosphohexokinase) (Q90YA3)
Organism: Gallus gallus (Chicken)
Subcellular location: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03184}.
Interaction partners:
Sequence:
MGAGKAIAVLTSGGDAQGMNAAVRAVVRVGIYTGAKVYFVHEGYQGLVDGGDNLKEATWESVSMMLQLGGTVIGSARCQDFRTREGRLKAARNLVKRGITNLCVIGGDGSLTGADTFRAEWSSLLAELLKTGGITAEEAKKSSHLNIVGMVGSIDNDFCGTDMTIGTDSALHRIMEIVDAITTTAQSHQRTFVLEVMGRHCGYLALITSLACGADWVFIPESPPEDGWEDHLCRPTETRLGGSRLNIIIVAEGAIDRHGKAITSDDVKDLVVKRLGYDTRVTILGHVQRGGTPSAFDRILGSRMGVEAVMALLEGTPDTPACVVSLSGNQAVRLPLMECVQVTKDVTTAMNERRFDDAVKLRGRSFQNNWNVYKLLAHIRPPSTKSGHTLAVLNVGAPAAGMNAAVRSTVRIGLIHGHRMLAVHDGFEGLALGKVEDISWDMVGGWTGLGGSKLGTKRTLPKKYFEEISATISTFGIHGLIIIGGFEAFMGSLELMDGRAKFEELCIPICVIPATVSNNVPGSDFSIGADTALNTITTTCDRIKQSAAGTKRRVFIIETMGTWPPWQGGYCGYLAAGADAAYIFEEHFSIRDLQINVEHLTEKMKTTVKRGLVLRNEHCNENYTTDFIYNLYTEEGKGIFDCRKNVLGHMQQGGAPTPFDRNFGTKMGAKSVAWITGKIKECSRHGRIFANTADSACLLGMRKRSLVFQPLTELKEQTDFQHRIPKEQWWLKLRPILKILAKYNIELDTSEKALMEHVRQKRISQESNI
Protein: Uncharacterized protein (Q57ZK7)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MIFYSPFSFLSNMRMPLVIHMAPAVMRRFTGSRLIGPRCCHIATDSHVFFQLYGRHMEPMNETVPLSPSPPLKLEVSNNSSLFTSQLPAWSKALKELSAQLYAAPHSGFRRRSAIHALEVLNNALSLPHERRMPYCQSFWHKALAICGNIDEGEDIRSAALLATVLYYGDKHKRVLAFASNVQWLREKRAMSVLREDTQYILRLCIVYVLSSSFVGASFRPDMVECVKMHAENALRVMRGGEALETAREYRVFLYALDWYVAHCGNIDARDFIRRTFDPLVSDRLRPFIFRTDEGVPVEAFKKVSPASILRMGERCRAEGNTKLLRQLFTEVKHREDVDDRYRLFKLSSSLGNMLSLMSDVDSRTQSDIVACCGTSLSHEALAKIGGSSRNCSAVLRVLWNIGGEEAYFASRQVLFHRSPEEALAFQNECGDVLLADRSLVWETALRSMSESIGRGDINWRETLPTALRLLSDAGKNSVFFQLLRESHREDETASLMTASALGQATRRSGQWWRALDVVDMIAACDPPRTTAEDMFLQDACLQTIYALRDAKRWKEALAFYTSFASIALPPIHRLFCSVICGMPPSSPWEAALTVAQTYGEVPEKFLRTLRCARTPDAVMCASTEGAPLGLGTSSLKSRRFILQGFAEGGHWHHALQCVLQGAEGDVDFSSCVSLLRAAQRTSLGSLPGTFFSVLPDCVWGSAGLLRLCLLAAEAHGIMGSLCDALEKHESHEIATEYLSLTRFLIDGRLPPDDKPLSNRYVIYRILMSPLPSSSPAKIRVKWTKDALAAFESARHGGMKAFVQSYFRLHPSCVPKKLNRENSKTFALRSVMPQGSLQECNTLVAVLPRMLAVADKPSGTSTHAYARAVAQRARVGPMHTLAYLLSSSSSGLILLLSSSIPTKAVRLEMRIFLRVCPLGPSSIPLLSTTFYTSYKMEVVAASLPEVSVTVEATCSSDTDGLMAGSLYRLKESVSAEGWGICGVETDEAAAEEGLHVAALTLRLLHDECEGERVMLFETTNVPAWLRQACDE
Protein: Ubiquitin-conjugating enzyme E2 G2 (EC 2.3.2.23) (E2 ubiquitin-conjugating enzyme G2) (Ubiquitin carrier protein G2) (Ubiquitin-protein ligase G2) (P60605)
Organism: Mus musculus (Mouse)
Function: Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes 'Lys-48'-linked polyubiquitination. Involved in endoplasmic reticulum-associated degradation (ERAD). Required for sterol-induced ubiquitination of 3-hydroxy-3-methylglutaryl coenzyme A reductase and its subsequent proteasomal degradation.
Subcellular location: Endoplasmic reticulum {ECO:0000269|PubMed:11278356}. Lipid droplet {ECO:0000250|UniProtKB:P60604}.
Interaction partners:
- E3 ubiquitin-protein ligase AMFR
- Lipid droplet-regulating VLDL assembly factor AUP1
- Ubiquitin-conjugating enzyme E2 G1
- E3 ubiquitin-protein ligase synoviolin
- E3 ubiquitin-protein ligase MARCHF6
- Ubiquitin-conjugating enzyme E2 J1
- Ubiquitin-like modifier-activating enzyme 1
- Ubiquitin-conjugating enzyme E2 Q1
- Ubiquitin-like modifier-activating enzyme 6
- Protein sel-1 homolog 1
Sequence:
MAGTALKRLMAEYKQLTLNPPEGIVAGPMNEENFFEWEALIMGPEDTCFEFGVFPAILSFPLDYPLSPPKMRFTCEMFHPNIYPDGRVCISILHAPGDDPMGYESSAERWSPVQSVEKILLSVVSMLAEPNDESGANVDASKMWRDDREQFYKIAKQIVQKSLGL
Protein: RE05851p (Q9W5A7)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- IP19013p
- IP19005p
- Uncharacterized protein, isoform B
- Chorion protein c at 7F
- Chorion protein S36
- FI16876p1
- Uncharacterized protein
- Uncharacterized protein
- IP19120p
- Mucin 4B, isoform B
Sequence:
MLKAAKIPLFFALLGAVCIQAVVVGPQPLHNNNRNGYRYNGPAHKYLPSEESHSHGSPLDSSHQHDQQGPSNAYNSHHYPAQEQHGQGAPEHDHQQKEVDSWQTALSQQQHESFGNQQNHQNAYNEGPVYQHYQGFNHQQHYGLSQQQQHESYGQEHYQQSPNQLQHHQSQHANEYAYEPAHFQQQQQHHEIQGHKQHQQRKEHWNFVQEQQPQNHEPWQSSHGFQQHQQQHSNRFESQLPLREDLWQPIRELDLEKLPSAEAHASSHKTVAAPGRDVKLVPSYTLSSDFEHDRFIGLDSTDTRLLTQSLPDAYRKQLFSSPPEPSSLAQGHNQQHKPGSAAYGGSHGPSLGESTSDFLQMQSHSYQLPSTFTTHTEWTQDKEQHQHNPQQQATGNRQYSASAFAVSPSYLHASEASQPPKNSLPHPSRDFQPPYY
Protein: Farnesyl pyrophosphate synthase (FPP synthase) (FPS) (EC 2.5.1.10) ((2E,6E)-farnesyl diphosphate synthase) (Cholesterol-regulated 39 kDa protein) (CR 39) (Dimethylallyltranstransferase) (EC 2.5.1.1) (Farnesyl diphosphate synthase) (Geranyltranstransferase) (Q920E5)
Organism: Mus musculus (Mouse)
Function: Key enzyme in isoprenoid biosynthesis which catalyzes the formation of farnesyl diphosphate (FPP), a precursor for several classes of essential metabolites including sterols, dolichols, carotenoids, and ubiquinones. FPP also serves as substrate for protein farnesylation and geranylgeranylation. Catalyzes the sequential condensation of isopentenyl pyrophosphate with the allylic pyrophosphates, dimethylallyl pyrophosphate, and then with the resultant geranylpyrophosphate to the ultimate product farnesyl pyrophosphate (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Hydroxymethylglutaryl-CoA synthase, cytoplasmic
- S-adenosylmethionine-dependent nucleotide dehydratase RSAD2
- Diphosphomevalonate decarboxylase
- Isopentenyl-diphosphate Delta-isomerase 1
- Squalene synthase
- Geranylgeranyl pyrophosphate synthase
- Squalene monooxygenase
- Isopentenyl-diphosphate delta-isomerase 2
- Protein farnesyltransferase subunit beta
- All trans-polyprenyl-diphosphate synthase PDSS1
Sequence:
MNGNQKLDAYNQEKQNFIQHFSQIVKVLTEKELGHPEIGDAIARLKEVLEYNALGGKYNRGLTVVQAFQELVEPKKQDAESLQRALTVGWCVELLQAFFLVSDDIMDSSLTRRGQICWYQKPGIGLDAINDALLLEASIYRLLKFYCREQPYYLNLLELFLQSSYQTEIGQTLDLMTAPQGHVDLGRYTEKRYKSIVKYKTAFYSFYLPIAAAMYMAGIDGEKEHANALKILMEMGEFFQVQDDYLDLFGDPSVTGKVGTDIQDNKCSWLVVQCLLRASPQQRQILEENYGQKDPEKVARVKALYEALDLQSAFFKYEEDSYNRLKSLIEQCSAPLPPSIFMELANKIYKRRK
Protein: LP07267p1 (Q7YXW0)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
KLLALLAVLCLSQVIGAERIVNCYWGTWANYRSGNGKFDVSNIDAGLCTHLSYSFFGINDNGEIQSLDTWLDYDLGFINQAISLKNQNSNLKVLAVVGGWNEGSTKYSSMSGDWYKRQNFINSALNLLRNHGFDGLDLDWEYPNQRGGNWNDRANFVTLLREIKEAFAPYGYELGIAVGAGESLASASYEIANIAQQVDFINVMTYDFAMASDGQTGFNAPQWAVENAINFWLSQGAPANKLVLGVGTYGRSFQLSDSSQNWPGAPCRGEGSAGSYTGSTGYLGYNEICQNNWHTVFDYDNAAPYAYSGDQWVSFDNVLSVQYKMDFALSKGLAGAMIWSLETDDYRGQCGETYPLLKTINRKLRW
Protein: Neprilysin-2 (EC 3.4.24.11) [Cleaved into: Neprilysin-2, soluble form] (A0A0B4K692)
Organism: Drosophila melanogaster (Fruit fly)
Function: Metalloendoprotease which cleaves peptides such as tachykinin peptide TK-2 at the amino side of hydrophobic residues. Functions in female fertility, embryogenesis and memory formation. Required in females for normal patterns of egg laying, probably due to its function in sperm retention and preventing sperm displacement by rival ejaculates. Also required for normal patterns of hatching due to its important role in early embryonic development. Required in the dorsal paired medial neurons for the proper formation of middle-term memory. Also required in the mushroom body neurons where it functions redundantly with neprilysins Nep3 and Nep4 in normal long-term memory formation.
Subcellular location: Cell membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}. Secreted {ECO:0000269|PubMed:15554877, ECO:0000269|PubMed:17157960}. Note=A secreted form exists that is probably produced by proteolytic cleavage (Probable). In embryos, adult Malpighian tubules and testes, detected in the soluble fraction but is not detected in the membrane fraction (PubMed:15554877, PubMed:17157960). {ECO:0000269|PubMed:15554877, ECO:0000269|PubMed:17157960, ECO:0000305|PubMed:15554877, ECO:0000305|PubMed:17157960}.
Interaction partners:
- Insulin-degrading enzyme
- Angiotensin-converting enzyme
- Angiotensin-converting enzyme
- Angiotensin-converting enzyme
- Angiotensin-converting enzyme
- Angiotensin-converting enzyme
Sequence:
MQTVIQNPNWWRRRNKLEKSLLVSLGIMFVVLATGFGLWIGKVLRTSPPSNPQATALHGDSTTINQVPTGTASKGKSGDSGDVCLTQECIHTASTVLRKMKPEVEPCDNFYEFACGTYLEEENIPDDKVSISTFSVISDKLQEQLKDIITAERPETEPKHFRLPNLLYKACMNKTLIETLGPEPITRVAERLGGWPLIKGDSWNADDSWTWQEQVKKFRTAGFSMDYIIDFSIGVDLQNSTKRLIDLDQSSLALSREYLVKGFNETLVTAYYKYMVDIAVLFGANRDLAKTELLLSLEFEMALANISWPNEKRRNSSELYNLRTPAQLQAAYPYVQWVDYMNALLPEGLNVAEDEMINLSVPSFFEDLGKLLAKTPKRVIANYMFWRIHGFSVGFLSEEFRKRQLQYATALSGRQEQEARWKECVDIATSSMDEVCEDDFDSLGISVGSLYVGKHFHKDSKANALEMVNEIRNVFNDILDEVNWMDAKTKKEAKLKLHSMATHIGYPDEMLDNEKLAAYYAKLDIDPDKYFESFLGMNIFGTDYSFNKLRLPVNKTDWVRHARPAIVNAFYSSLENSIQFPAGILQGHFFNAQRPKYMNFGAIGYVIGHEITHGFDDQGRQFDVKGNLRDWWHPDTQKAYLAKAKCIIEQYGNYTERATGLNLNGINTQGENIADNGGVKESYIAYRRWAEKHGPEAKLPGLDYTPEQMFWVAAGQTWCAKYRKESLKMRITTGVHSPSEFRVLGSLSNMKDFAKDFHCPEGSPMNPVQKCEVW
Protein: Bone morphogenetic protein 8B (BMP-8B) (P55105)
Organism: Mus musculus (Mouse)
Function: Induces cartilage and bone formation. May be the osteoinductive factor responsible for the phenomenon of epithelial osteogenesis. Plays a role in calcium regulation and bone homeostasis (By similarity). Involved in the generation of primordial germ cells; this function involves Bmp4 in a synergistic manner though separate receptor complexes seem to be involved. Required for the initiation and maintenance of spermatogenesis. Signaling protein involved in regulation of thermogenesis and energy balance. Proposed to increase the peripheral response of brown adipose tissue (BAT) to adrenergic stimulation while acting centrally in the hypothalamus to increase sympathetic output to BAT.
Subcellular location: Secreted {ECO:0000250}.
Interaction partners:
- Bone morphogenetic protein receptor type-1A
- Activin receptor type-1
- Bone morphogenetic protein 8A
- Bone morphogenetic protein receptor type-2
- Bone morphogenetic protein receptor type-1B
- Chordin
- Activin receptor type-2B
- Activin receptor type-2A
- Noggin
- Neuroblastoma suppressor of tumorigenicity 1
Sequence:
MAARPGLLWLLGLALCVLGGGHLSHPPHVFPQRRLGVREPRDMQREIREVLGLPGRPRSRAPVGAAQQPASAPLFMLDLYRAMTDDSGGGTPQPHLDRADLIMSFVNIVERDRTLGYQEPHWKEFHFDLTQIPAGEAVTAAEFRIYKEPSTHPLNTTLHISMFEVVQEHSNRESDLFFLDLQTLRSGDEGWLVLDITAASDRWLLNHHKDLGLRLYVETEDGHSIDPGLAGLLGRQAPRSRQPFMVGFFRANQSPVRAPRTARPLKKKQLNQINQLPHSNKHLGILDDGHGSHGREVCRRHELYVSFRDLGWLDSVIAPQGYSAYYCAGECIYPLNSCMNSTNHATMQALVHLMKPDIIPKVCCVPTELSAISLLYYDRNNNVILRRERNMVVQACGCH
Protein: ER membrane protein complex subunit 9 (Protein FAM158A) (Q9Y3B6)
Organism: Homo sapiens (Human)
Function: Part of the endoplasmic reticulum membrane protein complex (EMC) that enables the energy-independent insertion into endoplasmic reticulum membranes of newly synthesized membrane proteins. Preferentially accommodates proteins with transmembrane domains that are weakly hydrophobic or contain destabilizing features such as charged and aromatic residues. Involved in the cotranslational insertion of multi-pass membrane proteins in which stop-transfer membrane-anchor sequences become ER membrane spanning helices. It is also required for the post-translational insertion of tail-anchored/TA proteins in endoplasmic reticulum membranes. By mediating the proper cotranslational insertion of N-terminal transmembrane domains in an N-exo topology, with translocated N-terminus in the lumen of the ER, controls the topology of multi-pass membrane proteins like the G protein-coupled receptors. By regulating the insertion of various proteins in membranes, it is indirectly involved in many cellular processes (Probable).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000305|PubMed:32459176}; Peripheral membrane protein {ECO:0000305|PubMed:32459176}; Cytoplasmic side {ECO:0000269|PubMed:22119785}.
Interaction partners:
- ER membrane protein complex subunit 6
- ER membrane protein complex subunit 4
- ER membrane protein complex subunit 2
- ER membrane protein complex subunit 3
- ER membrane protein complex subunit 5
- Endoplasmic reticulum membrane protein complex subunit 7
- ER membrane protein complex subunit 10
- ER membrane protein complex subunit 1
- ER membrane protein complex subunit 8
Sequence:
MGEVEISALAYVKMCLHAARYPHAAVNGLFLAPAPRSGECLCLTDCVPLFHSHLALSVMLEVALNQVDVWGAQAGLVVAGYYHANAAVNDQSPGPLALKIAGRIAEFFPDAVLIMLDNQKLVPQPRVPPVIVLENQGLRWVPKDKNLVMWRDWEESRQMVGALLEDRAHQHLVDFDCHLDDIRQDWTNQRLNTQITQWVGPTNGNGNA
Protein: Protein qua-1 (G5EC21)
Organism: Caenorhabditis elegans
Function: Required for cuticle shedding and normal alae morphology and localization, and subsequently larval development.
Subcellular location: Cytoplasmic vesicle {ECO:0000269|PubMed:16502424}. Secreted {ECO:0000269|PubMed:16502424}. Secreted, extracellular space, extracellular matrix {ECO:0000305|PubMed:16502424}. Note=Secreted by the underlying hypodermis. {ECO:0000305|PubMed:16502424}.
Interaction partners:
- Apple domain-containing protein
- SSD domain-containing protein
- MAM domain-containing protein
- C-type lectin domain-containing protein 180
- Papilin
- Uncharacterized protein
- Apple domain-containing protein
- Copper transport protein
- Molting protein mlt-10
- SUppressor of Pkc-3
Sequence:
MRRLSAILPILLLSNFWPTVESLNYKCHNDQILVVQSFGNDTIRMHCQRLDLCGYQKLKCDYDELQPQCGGKLNFVSHVNQKGSTAPVEHTCCNLFNPRSHHSIPTHIGNDCFIYELPDGSSNGKKVDPAPADDAPYAVLKNPAEIPEQFDGVTGYRLRLFLLKNKSPPTLLVKGIERRLDGYRVTICRPRCTSYDKVVNDNEGAEDGEWKAISWSSWSSSSWSTWARHAFNKAAAEGGEAAERIRTRMPIGEKTVAGAAGATGAAGSDKSNINIHVESNGNNNNSFEGGRSSSEKSDGQLNREISGSSEAGAGGKGGAGADGAAGSGAGAGAGAGTNGNINITVHTDGKSGGNAVAVANANVTVNGAGGVSTTGTGAQTGNESGLGGSAGTDKAGGKKGGHGDSGDSGNNKNKDNGKGKGKGKNDEEDEEDNGDEDGNGKGGNGGNPKGEWDDGDGDEDDDGTDGGSKESGNNGKGKGKGSGDGDGNRNGNGDGNGRPKGDGNIKINIHSPDDNDLLEKDENGPNGKGGAGNGNGDGDKDNNGKGNGTGDGDGDGNGNGNGLTGDGNGTGDGDNNESGNGNGDGSDKNSGAGAGTKPENREGGDGNGNGTGDGNGDGNDNGNGSKGLGTGSGDGKGEGNKSGTPGKSDGKEDGAGSNGSGNGKEGDGNKSGGSGKGGAGNGKSGDGSGDGKNNGNGGTGDGKDKNGKGSGSGDNDKSGTRAAGKGNAEGNGKGNGNDGKGSGSGDGSGAGGKGDKSDSESGNEADGKDGKKNEGAGGEAAAGSGGANKGGSDGDDDDVDVTDVEVGTKPLTGTKLEELLAKLPNETADGNATGDGNEFGTVQTGAKHNAESSASGIPLVQARSNTVNGGAPVPPAPGSGATGSGTSGSGTSESVTNGSGATESGSTGSGTTGTGTSGTGSSGTGASAARTSSIAGDAPQAAVLADTPGAAGAAGGGRSNCFSADSLVTTVTGQKRMDELQIGDYVLVPSSGNVLKYEKVEMFYHREPKTRTNFVVLYTKSGRKLSLTGRHLLPVAECSQVEQYTMNPDGIDVAMRESKYAEKARKGECVLSIDESGEVIADEIVRVGRMTNVGIYSPMTVEGSLIVDGVLSSCFSHLESHSAHKLIFDFIYYVYNAFGLLNTNHVDLQPIPTFVSFAQYLSKTVLPFS
Protein: Transporter (Q334I2)
Organism: Rattus norvegicus (Rat)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- Neutral amino acid transporter B
- b
- Y+L amino acid transporter 1
- Amino acid transporter
Sequence:
MDRLKCPSFFKCRQKEKVTASSENFHVGENDENQERGNWSKKSDYLLSMVGYAVGLGNVWRFPYLTYTNGGGAFLIPYAIMLALAGLPLFFLECSLGQFASLGPVSVWRILPLFQGVGITMVLISIFVTIYYNVIIAYSLYYLFASFQSVLPWANCSSSWADDNCSRQPIVTGCRVSTDTGGDMFMNISWVNSNNFTCLNGSEVFRPGQLPSEQYWDKVTLRRSSGMDETGVIVWYLALCLLLAWIIVGAALFKGIKSSGKVVYFTALFPYVVLLILLIRGATLEGASKGISYYIGAQSNFTKLREAEVWKDAATQIFYSLSVAWGGLVALSSYNKFNNNCYSDAIIVCLTNCLTSVFAGFAIFSILGHMAHISGKEVSQVVKSGFDLAFIAYPEALAQLPGGPFWSILFFFMLLTLGLDSQFASIETITTTIQDLFPKAMKRMRVPITLGCCLILFLLGLVCVTQAGIYWVHLIDHFCAGWGILIAAILEIAGIIWIYGGNRFIEDIEMMIGAKRWLFWLWWRACWFVITPILLSAILVWSLVKFHRPNYADIPYPDWGVALGWCMIIFCIIWIPIMAIIKIVRAEGNILQRIIKCCRPASNWGPYLEKHRGERYKDMAEPAKETDHEIPTISGTRKPE
Protein: Stromal cell-derived factor 1 (C-X-C motif chemokine 12) (Q6T7C0)
Organism: Gallus gallus (Chicken)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
MDLRALALLAFALAVISLSEEKPVSLTYRCPCRFFESNVARANIKHLKILSTPNCSLQIVARLKSNSKQVCIDPKLKWIQEYLEKALNK
Protein: Synaptotagmin-15 (Chr10Syt) (Synaptotagmin XV) (SytXV) (Q9BQS2)
Organism: Homo sapiens (Human)
Function: May be involved in the trafficking and exocytosis of secretory vesicles in non-neuronal tissues.
Subcellular location: [Isoform 1]: Cell membrane {ECO:0000250}; Single-pass type III membrane protein {ECO:0000250}.; SUBCELLULAR LOCATION: [Isoform 2]: Cell membrane {ECO:0000250}; Single-pass type III membrane protein {ECO:0000250}.; SUBCELLULAR LOCATION: [Isoform 4]: Cell membrane {ECO:0000250}; Single-pass type III membrane protein {ECO:0000250}.
Interaction partners:
Sequence:
MAEQLALVIGGTIGGLLLLLLIGASCCLWRRFCATLTYEELPGTPAMATTAASSGQRDRPCQPHARTQLSRPPAVPFVVPPTLQGRDWVPLHSGEWADAPWDPCPASELLPHTSSGGLGDACMVGAINPELYKFPEDKSETDFPDGCLGRLWFSVEYEQEAERLLVGLIKAQHLQAPSETCSPLVKLYLLPDERRFLQSKTKRKTSNPQFDEHFIFQVSSKTITQRVLKFSVYHVDRQRKHQLLGQVLFPLKNETLVGDCRRVIWRDLEAESLEPPSEFGDLQFCLSYNDYLSRLTVVVLRAKGLRLQEDRGIVSVFVKVSLMNHNKFVKCKKTSAVLGSINPVYNETFSFKADATELDTASLSLTVVQNMEGDKSQQLGRVVVGPYMYTRGRELEHWDEMLSKPKELVKRWHALCRTTEP
Protein: DNA-directed RNA polymerase II subunit Rpb4 (RNA polymerase II subunit D) (Q9VEA5)
Organism: Drosophila melanogaster (Fruit fly)
Function: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Associates with POLR2G.
Subcellular location: Nucleus {ECO:0000269|PubMed:12482983}. Chromosome {ECO:0000269|PubMed:19921261}.
Interaction partners:
- Transcriptional adapter 2A
- DNA-directed RNA polymerase II subunit RPB7
- RNA-binding protein 9, isoform J
- DNA-directed RNA polymerase II subunit RPB11
- DNA-directed RNA polymerases I, II, and III subunit RPABC1
- DNA-directed RNA polymerase II subunit RPB3
- DNA-directed RNA polymerase II subunit RPB9
- DNA-directed RNA polymerases I, II, and III subunit RPABC5
- DNA-directed RNA polymerases I, II, and III subunit RPABC3
- DNA-directed RNA polymerases I, II, and III subunit RPABC4
Sequence:
MSFMNPVDMVDEDAADLQFPKEFENAETLLISEVHMLLDHRKRQNESADEEQEFSEVFMKTYAYTDSFRKFKNKETIMSARSLLMQKKLHKFELAALGNLCPEAPEEAKALIPSLEGRFEDEELRQILDDIGTKRSLQY
Protein: Bacterial RNA polymerase inhibitor (Gene product 2) (Gp2) (P03704)
Organism: Escherichia phage T7 (Bacteriophage T7)
Function: Acts as an inhibitor of bacterial RNA polymerase by interacting with RpoC subunit and thus preventing promoter recognition by RpoE. Non-DNA-binding transcription factor that plays a role in the transcriptional switch that abolishes transcription of the viral early genes (class I) by the host RNA polymerase but allows transcription of late genes (class II and class III) by T7 RNA polymerase.
Interaction partners:
Sequence:
MSNVNTGSLSVDNKKFWATVESSEHSFEVPIYAETLDEALELAEWQYVPAGFEVTRVRPCVAPK
Protein: Ubiquitin-conjugating enzyme E2 13 (EC 2.3.2.23) (Q95XX0)
Organism: Caenorhabditis elegans
Function: Involved in protein ubiquitination, but has no ubiquitin ligase activity on its own. The uev-1-ubc-13 heterodimers catalyze the synthesis of non-canonical 'Lys-63'-linked polyubiquitin chains. Involved in sorting Lys-63-linked polyubiquitinated maternal membrane proteins for degradation by targeting to multivesicular bodies. May be involved in the ubiquitination and growth of intracellular polyglutamine protein aggregates. May have a role in AMPA-type glutamate receptor trafficking in neurons.
Interaction partners:
- Ubiquitin-conjugating enzyme E2 variant 1
- Ubiquitin thioesterase otubain-like
- Ubiquitin-ribosomal protein eL40 fusion protein
- Polyubiquitin-A
- E1 ubiquitin-activating enzyme
- E3 ubiquitin-protein ligase CHIP
- Ubiquitin-conjugating enzyme E2 1
- Ubiquitin-like domain-containing protein
- Ubiquitin-like domain-containing protein
- E3 ubiquitin-protein ligase ZNRF1
Sequence:
MAGQLPRRIIKETQRLLADPVPGISANPDESNARYFHVMIAGPDDSPFAGGVFKLELFLPEEYPMAAPKVRFMTKIYHPNIDKLGRICLDILKDKWSPALQIRTVLLSIQALLSAPNPEDPLATDVAEQWKTNEAEAIKTAKQWTMNYAQA
Protein: Tryptophan decarboxylase 2 (EC 4.1.1.-) (Q7XHL3)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Involved in serotonin biosynthesis. Catalyzes the decarboxylation of L-tryptophan to tryptamine, which is converted to serotonin by tryptamine 5-hydroxylase. May play a minor role in serotonin biosynthetis during senescence. Accumulation of serotonin attenuates leaf senescence.
Interaction partners:
- Serotonin N-acetyltransferase 1, chloroplastic
- Serotonin N-acetyltransferase 2, chloroplastic
- histidinol-phosphate transaminase
- Aspartate aminotransferase
- Aspartate aminotransferase
- Amine oxidase
- Tryptophan aminotransferase-related protein 1
- Tryptophan aminotransferase-related protein 2
- Aspartate aminotransferase
- Aspartate aminotransferase, cytoplasmic
Sequence:
MEGVGGGGGGEEWLRPMDAEQLRECGHRMVDFVADYYKSIEAFPVLSQVQPGYLKEVLPDSAPRQPDTLDSLFDDIQQKIIPGVTHWQSPNYFAYYPSNSSTAGFLGEMLSAAFNIVGFSWITSPAATELEVIVLDWFAKMLQLPSQFLSTALGGGVIQGTASEAVLVALLAARDRALKKHGKHSLEKLVVYASDQTHSALQKACQIAGIFSENVRVVIADCNKNYAVAPEAVSEALSIDLSSGLIPFFICATVGTTSSSAVDPLPELGQIAKSNDMWFHIDAAYAGSACICPEYRHHLNGVEEADSFNMNAHKWFLTNFDCSLLWVKDRSFLIQSLSTNPEFLKNKASQANSVVDFKDWQIPLGRRFRSLKLWMVLRLYGVDNLQSYIRKHIHLAEHFEQLLLSDSRFEVVTPRTFSLVCFRLVPPTSDHENGRKLNYDMMDGVNSSGKIFLSHTVLSGKFVLRFAVGAPLTEERHVDAAWKLLRDEATKVLGKMV
Protein: Protein ZIP2 (Zipping up meiotic chromosomes protein 2) (P53061)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Required for initiation of meiotic chromosome synapsis. Involved in synaptonemal complex formation, a structure that tethers a pair of homologous chromosomes along their lengths and plays a central role in recombination and homolog segregation during meiosis. Required for the normal localization of MSH4 to chromosomes.
Subcellular location: Nucleus. Chromosome. Note=localizes to a meiosis specific chromosomal structure called the synaptonemal complex (SC) formed during meiotic prophase.
Interaction partners:
- Sporulation-specific protein 16
- Synaptonemal complex protein ZIP1
- Sporulation-specific protein 22
- Chromosome stability protein 9
- Meiotic recombination protein DMC1
- Homologous-pairing protein 2
- Protein RED1
- Meiotic nuclear division protein 1
- Pachytene checkpoint protein 2
- MutS protein homolog 4
Sequence:
MIIERWEVKLSKCNQNVGGYSVLSGNLKENIKLGRRAQKYLKELRNLQLKPLKIGGYENCGTINGEEYFLEVIHITSGRQKIDVAVGKTWNVTNIENDNKEELQYELFKEKLKVGKQDMLFFSWMKSLSVQLNAPLHQKMTEHGLADDNTRLEWFNIPLLRRSQYRKKVPYPSLRQMSSVLEVQCSTLTEEKLNFCVGFSDKPLSEWKPQIFEQTYNRYRLQRISPEKSFKYKSRCSKYNFKTSSQSWVVKVPEHDQQLNTFEKRYDELFDAQFNKLEFFKIRMKKLKKNKPIEKKNYKIWCLEKEDLKDLVWDPLKRICNHSRYAIFEHVTINREAYSIKPLRLTFQKLDSGSLDLIDNQKKTFGSIKLAMSMPDVKKTENQSIEESERHDETAIETQEFDENDCLSSKADINTSLAPQKRSFIDNELMSMLVTKKKIKKDKDVSDTGISSTSYLINSGTYANSHIEIPTSNSVYNGKEDCSFNNYSVKHSILEEDIENKCIAVNENKVIENQKVIQSLCKNSHLDLIEQSYFGECDFIINHSTCVYKIQASRFMQLRNNGSLHYDKAVNDLLTEFQRVIIIVEFSEIIQDVDPDLFWKIKLYLLNSRVDVFFIHETTDFFIDWMKYFIARWAFSYNDEKEKNIANADILLDLGFNILLVRKIFQTYSLEEFFMAIIKEESKAVKMLTVSQMTRLKKLLTLEW
Protein: Adenylyl cyclase-associated protein (Q9ZWM6)
Organism: Gossypium hirsutum (Upland cotton) (Gossypium mexicanum)
Interaction partners:
- Vegetative cell wall protein gp1-like
- 66 kDa stress protein-like
- 66 kDa stress protein
- 66 kDa stress protein-like
- 66 kDa stress protein-like
- Actin-depolymerizing factor 2-like
- Actin depolymerizing factor 2
- Actin-related protein 2
- Actin-related protein 2
- Uncharacterized protein ycf45-like isoform X1
Sequence:
MEAKLIERLEAAVARLESLSAGGISDRGLPDGVDEVSSDPSVLAFDDLMDQYAARVSAAAEKIGGQVLDVTKLVLEAFSVQKKLLIEIKQTQKPDMAGLVEFLKPLNEVILKVNAMTEGRRSDFFNHLKSAGDSLSALAWIAYTGKDCGMSMPIAHVEESWQMAEFYNNKVLVEYRNKDQIHVEWAKALKELYLPGLRDYVKSHYPLGPVWSASGKKASSAPPKAPPPGAPAPPPPPPASLFSSEPSQPSSSNPKQGMSAVFQEISSGNVSAGLKKVTADMKTKNRTDRTGVVSASGKETRSSSPSFSKAGPPKLELQMGRKWAVENQIGRKNLVIDDCDAKQSVYIYGCKDSVLQIQGKVNNITIDKCTKMGVVFKDVVAACEVVNCNGVEVQCQGSAPTISVDNTSGCQLYLSKDSLGTSITSAKSSEINVLVPTGPDGDWGEHSLPQQYIHVFKDGQFETTPVSHSGA
Protein: Vesicle transport v-SNARE N-terminal domain-containing protein (Q57YW6)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Endomembrane system {ECO:0000256|ARBA:ARBA00046280}; Single-pass type IV membrane protein {ECO:0000256|ARBA:ARBA00046280}.
Interaction partners:
- Vesicle-associated membrane protein, putative
- Syntaxin 5
- Vacuolar protein sorting 33, putative
- Pep3/Vps18/deep orange beta-propeller domain-containing protein
- Vacuolar assembly protein vps41, putative
- RING-type domain-containing protein
- Vacuolar protein sorting complex subunit, putative
- Syntaxin, putative
- Vacuolar protein sorting-associated protein 45, putative
- Syntaxin, putative
Sequence:
MSSDLLREYENDFNETLKEANDVASRLQESLQRSGVSYQAPPAAGPQSRSQQCHSLQQSLTRLRELITNMSYESNEVEPASAKEEVKRRLEDYRGKLVALEKQLSRLRQESREADRTDLLGNGREMGDDGGSMEEHARMLGTTTKLKEGTGALQKAEALLHGTNELGLETLSVVRGQTETMKHIHGVVIDVDDDVTESRRIVHRMQQVARKQKLIMAGVIGMLVFTFLIIVFWK