wanglab/gogpt-training-data huggingface dataset:
Protein: Delta-9 acyl-lipid desaturase 1 (EC 1.14.19.-) (O65797)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in delta-9 desaturation of fatty acids (Probable). Involved in the production of very-long-chain fatty acids (VLCFAs). May desaturate chloroplastic monogalactosyl diacylglycerol (MGDG) and alter chloroplast membrane fluidity, which is required to prime a cold acclimation response.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:23175755}; Multi-pass membrane protein {ECO:0000255}. Plastid, chloroplast membrane {ECO:0000305|PubMed:27062193}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Sphingolipid delta
- F1K23.9
- Delta
- Delta
- Putative glutaredoxin-C12
- Acid phosphatase-like protein
- Cellulase
- At2g16660/T24I21.7
- Protein NRT1/ PTR FAMILY 4.7
- Tropinone reductase homolog At2g29300
Sequence:
MSLSASEKEENNKKMAADKAEMGRKKRAMWERKWKRLDIVKAFASLFVHFLCLLAPFNFTWPALRVALIVYTVGGLGITVSYHRNLAHRSFKVPKWLEYFFAYCGLLAIQGDPIDWVSTHRYHHQFTDSDRDPHSPNEGFWFSHLLWLFDTGYLVEKCGRRTNVEDLKRQWYYKFLQRTVLYHILTFGFLLYYFGGLSFLTWGMGIGVAMEHHVTCLINSLCHVWGSRTWKTNDTSRNVWWLSVFSFGESWHNNHHAFESSARQGLEWWQIDISWYIVRFLEIIGLATDVKLPSESQRRRMAMVR
Protein: Extracellular sulfatase (EC 3.1.6.-) (Q7ZVU8)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Endoplasmic reticulum {ECO:0000256|PIRNR:PIRNR036665}. Golgi apparatus, Golgi stack {ECO:0000256|ARBA:ARBA00004348, ECO:0000256|PIRNR:PIRNR036665}. Cell surface {ECO:0000256|PIRNR:PIRNR036665}.
Interaction partners:
Sequence:
MAVGWRPATLLLVFILTFICLSDGSTYLSGQRQRSRLQRDRRNVRPNMILILTDDQDIELGSMQAMNKTKRIMMQGGTHFSNAFATTPMCCPSRSTILTGKYVHNHHTYTNNENCSSPSWQAHHEPHTFAVHLNNSGYRTAFFGKYLNEYNGSYVPPGWREWVALVKNSRFYNYTLCRNGIREKHGTQYPKDYLTDVITNDSINFFRMSKRMYPHRPVMMVLSHAAPHGPEDAAPQYSSAFPNASQHITPSYNHAPNPDKHWILRYTGPMKPVHMQFTNMLQRRRLQTLLSVDDSVEKVYNMLVETGELDNTYIIYMSDHGYHIGQFGLVKGKSMPYEFDIRIPFYVRGPNVEAGAINPHIVLNTDLAPTLLDMAGIDIPQDMDGKSILKLLETERPVNSFTRFHSYKKAKLWRDSFLVERGKPLHKLADGKEVEQNSLPKYQRVRDLCQRAEHQTPCEQPGQKWQCIEDGTGMPRLYKCKGMAGLYAPRALGLMAANRGQISAAHSGSDYCDCEPTASLKRKKALTKKKLKNKKSVPRNRWARSVPYNLDSNVYTLDLEKGYRPLNLNTSLMLGSKQAVYGQNEEYSGMGPTEDNFNSLTPPAALKVTYRCSILMNDTVKCDGGLYKSLQAWKDHKLHIEHEIGTLQTKIKNLREVKGHLKEVRPKECECNKNMYQYSSRALFKLKSAQTHSVKMTSKDKKQWLMKEQKRRKKLRKLLKRLRNNDTCSMPGLTCFTHDNQHWQTAPFWTMGPFCACTSANNNTYWCLRTINETHNFLFCEFATGFLEYFDLNTDPYQLMNGVSTLDRDAVNHMHQQLMKLRSCKGHKECNQETGGKERNTLYDYRPLHRRKRPKVKKASSKSMGQIWEGWVG
Protein: Serine/threonine-protein phosphatase 2A 55 kDa regulatory subunit B (X1WDS4)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- Protein phosphatase 2
- Protein phosphatase 2, regulatory subunit A, beta a
- Serine/threonine-protein phosphatase
- Extra spindle pole bodies-like 1, separase.
- NRDE-2, necessary for RNA interference, domain-containing
- Serine/threonine-protein kinase CHK1
- Serine/threonine-protein phosphatase 2A 55 kDa regulatory subunit B delta isoform
- ATR serine/threonine kinase
- S-phase kinase-associated protein 1
- Serine/threonine-protein phosphatase
Sequence:
MDGHGDGQSRWCLSQVKGAVDDDVAEADIISAVEFNHSGELLATGDRGGRIVIFQQEQENKSLPQCRAEYNVYSTFQSHEPEFDYLKSLEIEEKINKIRWLPQKNAAHFLLSTNDKTIKLWKISERDKRPEGYNLKEEDGRYRHPSSLTTLRVPVFQPMDLMVEASPRRVYANAHTYHINSISVNSDNETYLSADDLRVNLWHLDYTDRSFNIVDIKPANMEELTEVITASEFHPLQCNTFVYGSSKGSVRLCDMRASALCDQHSKLFEEPEDPSTRSFFSEIISSISDVKFSHSGRYMMTRDYLTLKIWDLHMESHPVETYQVHGYLRSKLCSLYENDCIFDKFECCWRGDDSEVMTGSYNNFFRMFEREGQRDVTLEASWENGSPGCPLKSWRVSTGSRRKRNEIGVDCLDFSRKILYTSWHPQENIVALATVNNLYLFQEKLN
Protein: SART-1 family protein DOT2 (Protein DEFECTIVELY ORGANIZED TRIBUTARIES 2) (Protein MERISTEM-DEFECTIVE) (Q9LFE0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Plays a role in root, shoot and flower development. Probably required for normal root and shoot meristem organization and maintenance and the proper expression of PIN and PLT genes. Involved in leaf vasculature patterning.
Subcellular location: Nucleus {ECO:0000269|PubMed:19000164}.
Interaction partners:
- Protein STABILIZED1
- RNA-binding motif protein 25
- Sm-like protein LSM5
- Sm-like protein LSM2
- 110 kDa U5 small nuclear ribonucleoprotein component CLO
- Sm-like protein LSM4
- Sm-like protein LSM8
- Small nuclear ribonucleoprotein Sm D2
- 109 kDa U5 small nuclear ribonucleoprotein component GFL
- Thioredoxin-like protein 4B
Sequence:
MEVEKSKSRHEIREERADYEGSPVREHRDGRRKEKDHRSKDKEKDYDREKIRDKDHRRDKEKERDRKRSRDEDTEKEISRGRDKEREKDKSRDRVKEKDKEKERNRHKDRENERDNEKEKDKDRARVKERASKKSHEDDDETHKAAERYEHSDNRGLNEGGDNVDAASSGKEASALDLQNRILKMREERKKKAEDASDALSWVARSRKIEEKRNAEKQRAQQLSRIFEEQDNLNQGENEDGEDGEHLSGVKVLHGLEKVVEGGAVILTLKDQSVLTDGDVNNEIDMLENVEIGEQKRRNEAYEAAKKKKGIYDDKFNDDPGAEKKMLPQYDEAATDEGIFLDAKGRFTGEAEKKLEELRKRIQGQTTHTFEDLNSSAKVSSDYFSQEEMLKFKKPKKKKQLRKKDKLDLSMLEAEAVASGLGAEDLGSRKDGRRQAMKEEKERIEYEKRSNAYQEAIAKADEASRLLRREQVQPFKRDEDESMVLADDAEDLYKSLEKARRLALIKKEEAGSGPQAVAHLVASSTNQTTDDNTTTGDETQENTVVFTEMGDFVWGLQRENDVRKPESEDVFMEEDVAPKAPVEVKEEHPDGLTEVNDTDMDAAEDSSDTKEITPDENIHEVAVGKGLSGALKLLKDRGTLKEKVEWGGRNMDKKKSKLVGIVDDDGGKESKDKESKDRFKDIRIERTDEFGRTLTPKEAFRLLSHKFHGKGPGKMKEEKRMKQYQEELKLKQMKNSDTPSQSVQRMREAQAQLKTPYLVLSGHVKPGQTSDPQSGFATVEKDVPGSLTPMLGDRKVEHFLGIKRKSEPGNSDTPPKRPKP
Protein: Very long chain fatty acid elongase 3 (EC 2.3.1.199) (3-keto acyl-CoA synthase ELOVL3) (Cold-inducible glycoprotein of 30 kDa) (ELOVL fatty acid elongase 3) (ELOVL FA elongase 3) (Elongation of very long chain fatty acids protein 3) (Very long chain 3-ketoacyl-CoA synthase 3) (Very long chain 3-oxoacyl-CoA synthase 3) (Q9HB03)
Organism: Homo sapiens (Human)
Function: Catalyzes the first and rate-limiting reaction of the four reactions that constitute the long-chain fatty acids elongation cycle. This endoplasmic reticulum-bound enzymatic process allows the addition of 2 carbons to the chain of long- and very long-chain fatty acids (VLCFAs) per cycle. Condensing enzyme that exhibits activity toward saturated and unsaturated acyl-CoA substrates with higher activity toward C18 acyl-CoAs, especially C18:0 acyl-CoAs. May participate in the production of saturated and monounsaturated VLCFAs of different chain lengths that are involved in multiple biological processes as precursors of membrane lipids and lipid mediators.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000255|HAMAP-Rule:MF_03203, ECO:0000269|PubMed:20937905}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_03203}.
Interaction partners:
- Very long chain fatty acid elongase 1
- Very-long-chain 3-oxoacyl-CoA reductase
- Very long chain fatty acid elongase 7
- Acyl-CoA wax alcohol acyltransferase 1
- Lipid transferase CIDEA
- Mitochondrial brown fat uncoupling protein 1
- Histone-lysine N-methyltransferase PRDM16
- Type II iodothyronine deiodinase
Sequence:
MVTAMNVSHEVNQLFQPYNFELSKDMRPFFEEYWATSFPIALIYLVLIAVGQNYMKERKGFNLQGPLILWSFCLAIFSILGAVRMWGIMGTVLLTGGLKQTVCFINFIDNSTVKFWSWVFLLSKVIELGDTAFIILRKRPLIFIHWYHHSTVLVYTSFGYKNKVPAGGWFVTMNFGVHAIMYTYYTLKAANVKPPKMLPMLITSLQILQMFVGAIVSILTYIWRQDQGCHTTMEHLFWSFILYMTYFILFAHFFCQTYIRPKVKAKTKSQ
Protein: Rab-GAP TBC domain-containing protein (Q389W8)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Rab3 GTPase-activating protein catalytic subunit
- Nuclear migration protein nudC
- Nuclear movement protein, putative
- CS domain-containing protein
Sequence:
MSVALDENTVSIPLWPVNGVPTRSTGQILQATLTGKETPRFTLTFFDPQNPTTLYACTSSSLVYAFFLNKNVVRLFIALECAITAMTCFSCSGSSLFVCATGDNSLVWVDCASGRIVKRMKTPHQHAVNMIRLSHVIGDHRSIVTASRESLAVWDVARMACRMCSNGKSTKEKREFLSIHTGRQSLLTVERFGRVTMWEPSTLSPSKSIMLAMQPRASAFCQKCLAIGGPGPLVGLLEVEGLTPIGCVQLSTAPVATRSLFIINDTLLACELTSGTVVFVVIGNYTVSFSLDAPHTGAVPRKMTSFSLSGPSFAAFAQGEKLTIFHLPTARQHYVHRERLGGGYSDSTLPARLHSFVQGKSNAYREGASRTSKKCARDENPGSDVELPRPNLRPADKDVNKWVKVKALPAGVQDEVKSTKGSAGGRVEPLERTGKDRKVEKGIGPRPKGGVELSLRPSLDEESRKANMNHLQQLLLRYGLFPDTYRAVTWRFLLQLPDKRFTASQYAQLASKGTHPSAHILMKPFRLANDGVQTSMEKALSVLVWHVPMFAAIHFLPMVVYPFLHPFEGDVQSVVEVVLVFLSNWGKEFFQFYPQQPVALTTLLDRLLRAEDAELHRHLSMSGVLVEEWGWEPLRSIYSDTVKPAEWLQVLDHTFFNEPLWFFLFHIRWMISIRSDIMKFRDQREIMNSILTTHDVDVNRIIGETYRLQARCPRGELTNPYSKLETLANYAYPTLWKYNEENVERKLNDMKLLQEQIERSKASSQEIAKICDQLAQADVLEEVYVRKQQAEAAARVSAKADSWKGEVAREMERQYTRDMEKMLRLRQMRQQIEQSGRLEVLNEELECANIQVDHLHEIRQREATHWTLADQLSEQELLHLEEAARNRLKGAKKAVESGTVGAERSPVTDGGEFGAVKSRMTTATPDVVSVVRPLSASPGEQQLTYDLGNPMNVYRALQNSAAREMVGRRIPSETGGKRVQRSYDDTHVAEVVSTVGATFQRQHGDHLIAAFGKASDSRSERGAALYDNLLPPGASPSETQTLCSSDLNRHTTEHRQTSESYEPSSAATVLLRPQDPGAYRLQRCSR
Protein: PAX-interacting protein 1 (PAX transactivation activation domain-interacting protein) (Q9U370)
Organism: Caenorhabditis elegans
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- JmjC domain-containing protein
- Retinoblastoma-binding protein homolog 5
- PHD-type domain-containing protein
- Set1/Ash2 histone methyltransferase complex subunit ash-2
- WD repeat-containing protein wdr-5.1
- BRCT domain-containing protein
- Protein hsr-9
- Serine/threonine-protein kinase ATM
- WD repeat-containing protein wdr-5.3
- Structural maintenance of chromosomes protein 6 homolog smc-6
Sequence:
MADPLSKEEDIQHRPDSPPLGLLDPSRIQNPLANDQLHQVPQQQNPSGFVMPEQPRQQPPPQTWQRTPTMSPANIFQGDSGSGTPGSQRSSTGTPNHQMGNPPQHQQQQFFHGESPAHSQGTPMTPQSAGMPGSNCGTPQSAGGPPTSVPYDYQQAQMQQQQHAQAMAAAAAAQQQQQQHLQQQQYAQNPQQMHDSPYRQHQMMQMHQHPGHPSQYPPGYPQQQAAQWQQQMYARQAAAQAQAQAQAQAQAQAQQRAAAQRVPVPYPPGAYPPGMPGPMTPGYPAQAPAAPRTTPGSAGPGTGPPGTPQRPQYPQGTNPQPQQAQFTYPPTQQMTPTGQPPGYPGMPGTPTFSSPAHQMFRQGQPTAPPGMRQYISPQAGQQQPTPGTPHRFAPPGPSGTTSSPHFAPGAPGADLRSPSLMSPNQQSQQHTPVLPRSLHNEMTSHGMRPIALPSQPLPQTQGTPQPILSASSLPPQSAGATQFVYRPQQPNQMNTMNQMNQMHHDVNPFPIQMNVDPELYLTGIHFHCFDSEKLFEDKLDRKNLEFMIKYHGGDIEFEASKFHERIHQITHVLVDSCRNTNVMTSLEHRKRIVSIQWIIDVMERERVELPWRIAHLPPPFNENFRPYLGKLFSLSGFDSSERAAISFMAEMMGAKITPFLARQNDLLIAKQPADKVTRAQEWKVPVVNFQWIADAYVCDEASPQKRPNVENPRYQLENPVMTNVNTSPNHIEGASQEFGAMMSCWKSQTIIADQAYEKARQNRKTLQNNTFFFPSKRLSDQAVAPTEDEIKSSRARLDEIKTHWEEHQEKMKDTPLSKEFYRVREPQARVSAWFGEGIDDEALTILKKKLEFLGGECVEKIRDATHVILISGRRSLVLLESIIRGKNIMDPEWIVDSYKQKMWLDTLDYFLHDKELEKEFAYNCKRSVLRARNKPVFEDIEFHVTRFVEPNQNDLVRLIELGGGNVHSEKPDPKYLAKCVETEQPFIIISCENDARFLSYLAGSKLPIYNVDLVLFAMLRQQIEPLPQYRIPIPIVVKTPVFRQPPPYTAPPKDQEPAASLASEPTRAADVLSENS
Protein: Uncharacterized protein (Q57ZN6)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Uncharacterized protein
- T. brucei spp.-specific protein
- Uncharacterized protein
- EF-hand domain-containing protein
Sequence:
MESDDGQVHSQVFEPQDVQLEEVEERSLVVGSEPTVYSSEDVQSVLVNVPVGGPPSRGPLSEFHSVEEISASSERSRDVARSAIVNRLVSPLPTSPLKDRSVVEISEEQIRLFADESHFPPPPSNISIRTSRSERAPSSSHAVSRFVSSPSPLRQVVRRYVSPQRHIDTPLINRRASTPIRRLSTPCDRRLVSPVDTPDFRERRGRLNPQARMSPTLVVASSSLPEDESSADSLVIVPTYNRKKRRVCGGRSFPTLYNISSLLVQFDGVWASSDDEEETSRNIAGSVALRRAAGRYRNSPSPITPVASGAVLARQRCRTGPLIEALQSVRNEKDMLMIMEKEQRDRRKITKAYVRLLREMLLWCAVKHATVLARGGPGAQSCKLRSQAGAVGRANSVPTRTSSSRRGERVRTCPIQRMSPLRTPREEIRPPLLSCGAQLETDVPVVGQGGRSRNDFSSHSQEKEKKGPSAGTYQSVSGAPAGSWGVFDSPVQGGRQGSFSRPSPDRLCSTSMDRSYEIWEVKAQLRSVVSEELGKRILVIGAESAAFQFIVHYHRIELTAFQREPIYLQEACQRRSIVSEAKNQLRMISDRGSNMGILGHLNWVEEWAQRLLTLIESERYVRQIELYQAEGHEREEIQRVFSLGLKSLTEYRECEAKRRRCRLEMKDIALCENLAREKLVAEEIQSRAALHLTYSAIPSSVVASGSDRRVGVPRRGAQKGSCGEHSHISPRGTEDPSRCYDRSLVTEPESHASTTQDGSAFTSALSAAMCSRNTSNNRALSDSDTPNEVVFFEWDPTSNTLTRTSNNNFTSFNTSTGTTTATVRAPSTGTVAVVRCDRSKSLPEATGSVSKVSSPSPQFPVAGSSTSRVDKSGSFVSAPLRGSAAAARDQVSEIPRKAGHSGRRSSSAVLKSCKTARRNDKTPLSGSGRRPSRVPNAARADGGKTNRDIFKRPINPVEEAEATFSLANRHIVPCSLKAAVARRGGSTCCFNQFSGEPFPDLRSTTQRPYNDDIIYSNSSRGFSEIDFGELSSAGEEEVKVRGDTAAKVHCGVSGTPLQSVTTVTISLDSDDAEDGGHGGQGNSNAAAVSDDRVEVGSITTEFIFESVRDEDDDVDPFSMRTVGKGSNSDSAAGKNVGPSLMGSSKAPFESAERSPTSTPMPRQESRRLLSHRSKSQETLTIPDVSLSTMHDETIGSGFKGEAAGRASLRSGCSSSPRFGESTLSASTALNTDEAGNKKRSCKGGPSRGSSRRPAVNRPKVPPGYLRPTAGWKRQSEEKVWQQLFSEARAKHRVSASRPAPINPRCPRDYKSDRKAIKVARVPYEEGPGVWSDYEEPRQPYGPIKVPSDARYGRKPEGRCVGGQSGAATIISPVRRRDAVWRFKAEGSCCHRSTSSLRDAKLSRDESSNALTNEGTALDEEDMDALKGIVRRASTTSHRTVASVASTPKKACGSSFYSSRSVTPSYIEAFYKLDLEAAKRYGFLISSHSGPVLQSTTPSKGGKKRITKGKHLPQPPTESSSSELKLSPDANSEERLLSTTTTHTSMSHILYSPRSKHHC
Protein: Regulatory protein zeste (O44203)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MVNKQYSATDLEAFMKIAANWQNSNHNLLEGVDIKTEMTQYMNSPSMNMYKKRERTQNWNHQEKKYLLDLCRKDMRIIENKRLDAGLTAVKNKAWKIIHQKFSNQFGTDRTCNRLKEQWRRMKACTRNEILDYNNRLARFGAEVADRKKPSPFTFEVWDFMQEAKKACKSEALDGIDYSKIPLALEEGFEYREDYKFNPEDHDMDDSRTPPQELCDVDIKEEENNETFNETFNHHHLNQSDILGSGERLSVSPNHSISRNGIHEAESPATISTSNVLDSSGAYMAGGGDMSGFQANFNMNNISATLEALNALRSGQFPSAAAAAAAAIHQHQAQAQAQVAMHHQHNNNNNNNNNEDDEDSMKPQSKRQRTSSGSMLGSEDQAPVLAPSVPASSDSQALERSGSSNGLTMPGTAVSTNANSSSSNNNNFELRMFMEMQSKEHMMRMKILEVQLQAAKHSRDLVEINKTLALQKLQLELASKRLPS
Protein: Phospholipid-transporting ATPase VB (EC 7.6.2.1) (ATPase class V type 10B) (P4-ATPase flippase complex alpha subunit ATP10B) (O94823)
Organism: Homo sapiens (Human)
Function: Catalytic component of a P4-ATPase flippase complex, which catalyzes the hydrolysis of ATP coupled to the transport of glucosylceramide (GlcCer) from the outer to the inner leaflet of lysosome membranes. Plays an important role in the maintenance of lysosome membrane integrity and function in cortical neurons.
Subcellular location: Late endosome membrane {ECO:0000269|PubMed:25947375, ECO:0000269|PubMed:32172343}; Multi-pass membrane protein {ECO:0000255}. Lysosome membrane {ECO:0000269|PubMed:25947375, ECO:0000269|PubMed:32172343}; Multi-pass membrane protein {ECO:0000255}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:25947375}; Multi-pass membrane protein {ECO:0000255}. Note=Exit from the endoplasmic reticulum requires the presence of TMEM30A, but not TMEM30B.
Interaction partners:
- Cell cycle control protein 50A
- Phospholipid-transporting ATPase VA
- Phospholipid-transporting ATPase VD
- Phospholipid-transporting ATPase IH
- Phospholipid-transporting ATPase IA
- Phospholipid-transporting ATPase IC
- Cell cycle control protein 50B
Sequence:
MALSVDSSWHRWQWRVRDGFPHCPSETTPLLSPEKGRQSYNLTQQRVVFPNNSIFHQDWEEVSRRYPGNRTCTTKYTLFTFLPRNLFEQFHRWANLYFLFLVILNWMPSMEVFHREITMLPLAIVLFVIMIKDGMEDFKRHRFDKAINCSNIRIYERKEQTYVQKCWKDVRVGDFIQMKCNEIVPADILLLFSSDPNGICHLETASLDGETNLKQRCVVKGFSQQEVQFEPELFHNTIVCEKPNNHLNKFKGYMEHPDQTRTGFGCESLLLRGCTIRNTEMAVGIVIYAGHETKAMLNNSGPRYKRSKIERRMNIDIFFCIGILILMCLIGAVGHSIWNGTFEEHPPFDVPDANGSFLPSALGGFYMFLTMIILLQVLIPISLYVSIELVKLGQVFFLSNDLDLYDEETDLSIQCRALNIAEDLGQIQYIFSDKTGTLTENKMVFRRCTIMGSEYSHQENAKRLETPKELDSDGEEWTQYQCLSFSARWAQDPATMRSQKGAQPLRRSQSARVPIQGHYRQRSMGHRESSQPPVAFSSSIEKDVTPDKNLLTKVRDAALWLETLSDSRPAKASLSTTSSIADFFLALTICNSVMVSTTTEPRQRVTIKPSSKALGTSLEKIQQLFQKLKLLSLSQSFSSTAPSDTDLGESLGANVATTDSDERDDASVCSGGDSTDDGGYRSSMWDQGDILESGSGTSLEEALEAPATDLARPEFCYEAESPDEAALVHAAHAYSFTLVSRTPEQVTVRLPQGTCLTFSLLCTLGFDSVRKRMSVVVRHPLTGEIVVYTKGADSVIMDLLEDPACVPDINMEKKLRKIRARTQKHLDLYARDGLRTLCIAKKVVSEEDFRRWASFRREAEASLDNRDELLMETAQHLENQLTLLGATGIEDRLQEGVPDTIATLREAGIQLWVLTGDKQETAVNIAHSCRLLNQTDTVYTINTENQETCESILNCALEELKQFRELQKPDRKLFGFRLPSKTPSITSEAVVPEAGLVIDGKTLNAIFQGKLEKKFLELTQYCRSVLCCRSTPLQKSMIVKLVRDKLRVMTLSIGDGANDVSMIQAADIGIGISGQEGMQAVMSSDFAITRFKHLKKLLLVHGHWCYSRLARMVVYYLYKNVCYVNLLFWYQFFCGFSSSTMIDYWQMIFFNLFFTSLPPLVFGVLDKDISAETLLALPELYKSGQNSECYNLSTFWISMVDAFYQSLICFFIPYLAYKGSDIDVFTFGTPINTISLTTILLHQAMEMKTWTIFHGVVLLGSFLMYFLVSLLYNATCVICNSPTNPYWVMEGQLSNPTFYLVCFLTPVVALLPRYFFLSLQGTCGKSLISKAQKIDKLPPDKRNLEIQSWRSRQRPAPVPEVARPTHHPVSSITGQDFSASTPKSSNPPKRKHVEESVLHEQRCGTECMRDDSCSGDSSAQLSSGEHLLGPNRIMAYSRGQTDMCRCSKRSSHRRSQSSLTI
Protein: Kinesin-like protein KIF6 (Q6ZMV9)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000305}.
Interaction partners:
- Kinesin-associated protein 3
Sequence:
MVKQTIQIFARVKPPVRKHQQGIYSIDEDEKLIPSLEIILPRDLADGFVNNKRESYKFKFQRIFDQDANQETVFENIAKPVAGSVLAGYNGTIFAYGQTGSGKTFTITGGAERYSDRGIIPRTLSYIFEQLQKDSSKIYTTHISYLEIYNECGYDLLDPRHEASSLEDLPKVTILEDPDQNIHLKNLTLHQATTEEEALNLLFLGDTNRMIAETPMNQASTRSHCIFTIHLSSKEPGSATVRHAKLHLVDLAGSERVAKTGVGGHLLTEAKYINLSLHYLEQVIIALSEKHRSHIPYRNSMMTSVLRDSLGGNCMTTMIATLSLEKRNLDESISTCRFAQRVALIKNEAVLNEEINPRLVIKRLQKEIQELKDELAMVTGEQRTEALTEAELLQLEKLITSFLEDQDSDSRLEVGADMRKVHHCFHHLKKLLNDKKILENNTVSSESKDQDCQEPLKEEEYRKLRDILKQRDNEINILVNMLKKEKKKAQEALHLAGMDRREFRQSQSPPFRLGNPEEGQRMRLSSAPSQAQDFSILGKRSSLLHKKIGMREEMSLGCQEAFEIFKRDHADSVTIDDNKQILKQRFSEAKALGESINEARSKIGHLKEEITQRHIQQVALGISENMAVPLMPDQQEEKLRSQLEEEKRRYKTMFTRLKALKVEIEHLQLLMDKAKVKLQKEFEVWWAEEATNLQVNSPAVNSLDHTKPFLQTSDSQHEWSQLLSNKSSGGWEVQDQGTGRFDVCDVNARKILPSPCPSPHSQKQSSTSTPLEDSIPKRPVSSIPLTGDSQTDSDIIAFIKARQSILQKQCLGSN
Protein: At3g08670 (Serine/arginine repetitive matrix-like protein) (Q9C9Y9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MNRNLRESLAGGRNIPAISQFRRGNNNNSNNISQNGFSRDSDENLDLFSKIRRSFPLASSDELPDVSAKLGRLSVGSKIAPKGKDDLLSSAEGGKNDYDWLLTPPGTPLGNDSHSSLAAPKIASSARASSASKASRLSVSQSESGYHSSRPARSSSVTRPSISTSQYSSFTSGRSPSSILNTSSASVSSYIRPSSPSSRSSSSARPSTPTRTSSASRSSTPSRIRPGSSSSSMDKARPSLSSRPSTPTSRPQLSASSPNIIASRPNSRPSTPTRRSPSSTSLSATSGPTISGGRAASNGRTGPSLSRPSSPGPRVRNTPQQPIVLADFPLDTPPNLRTSLPDRPISAGRSRPVGGSSMAKASPEPKGPITRRNSSPIVTRGRLTETQGKGRFGGNGQHLTDAPEPRRISNVSDITSRRTVKTSTTVTDNNNGLGRSFSKSSLDMAIRHMDIRNGKTNGCALSTTTLFPQSIRPASSKIQPIRSGNNHSDSISSNGTENGNEANEGRRLMGKLSDMDMYESSRYDALLLKEDVKNTNWLHSIDDRSSDHGLMFDNGGFELLPEPFAPL
Protein: RFX-like transcription factor daf-19 (Abnormal dauer formation protein 19) (Q09555)
Organism: Caenorhabditis elegans
Function: Probable transcription factor. May regulate some genes of ciliated sensory neurons. May activate the expression of the shared components of sensory cilia, but not the cell-type-specific expression. Together with transcription factor atf-7, involved in regulation of the serotonergic response of ADF neurons to pathogenic food.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00858, ECO:0000269|PubMed:12954713}.; SUBCELLULAR LOCATION: [Isoform c]: Nucleus {ECO:0000269|PubMed:20923979}.
Interaction partners:
- Serine/threonine-protein kinase ATR
- Intraflagellar transport protein 88 homolog
- Intraflagellar transport protein 52 C-terminal domain-containing protein
- Serine/threonine-protein kinase chk-2
- non-specific serine/threonine protein kinase
- Intraflagellar transport protein che-13
- B9 domain-containing protein 1
- Intraflagellar transport protein osm-1
- Cytoplasmic dynein 2 light intermediate chain 1
- WD_REPEATS_REGION domain-containing protein
Sequence:
MTNEEPVPSTSSVLSAAEKNVKIETPSRKRKGLDIDALWRKKFKDVENQKSPEKSEKSEKTIKEEPLETHPSGERKLRSASKDSKSLSKETHNTISTRSSSSGTPRKKMEPEDVKPNIKMLKKSLPVSFQCSNLNDGTVGDASVMLDPTKISLHSSSVAYGEESQDEMEVIQHSTDDPNGTREEFDYNQIEYGNAVTPNGTYTLYAPDSNYAPYYQYSNNMQSSPQDNAPYLVPAPQSPVSIDDADSINLPNNQRASPATVNWLFENYEIGEGSLPRCELYDHYKKHCAEHRMDPVNAASFGKLIRSVFHNLKTRRLGTRGNSKYHYYGIRLKDSSTLHSMQHPQPQIIQNTYTPPMQLPQRDAYADTVNQVAAIKYMDVEIPDKRARKDNSSSSSSCRDSVSPCMDLPAQQTIQHTPVHSVIPSTQQPAPLHNNNVVSYVVTESDKAAMGKIDLPIVPFPDKDALMATIGFRKLGVGEEELNSLIDIYEILCREILALIKNIDFASVEDTWSKFWSGNFGVDRDHISALCTLDQVQDYIIEVDLALYQTIVDTLIPNVLLSELSTGMTQTCRTFAKNIDVYLRKSLMLANLGEFFVKKKIQAIKYLQQGLKRYTSLNHLAHASRGVLMKPEQVQQMYQDYIRVDINTVHQQAGWICGCDSVMVHHVNNAFKHNLQRMSAMEVWAEWLESIVDQVLAKYHDKPANVIANVGKQFLLNWSFYTSMIIRDLTLRSAMSFGSFTLIRLLADDYMYYLIESKIAKAGKQQLITVIRADKDWPLTTNPQEYIVVANDNDEDLDLEKAGLL
Protein: Torsin-1A (Dystonia 1 protein) (Torsin ATPase-1A) (EC 3.6.4.-) (Torsin family 1 member A) (O14656)
Organism: Homo sapiens (Human)
Function: Protein with chaperone functions important for the control of protein folding, processing, stability and localization as well as for the reduction of misfolded protein aggregates. Involved in the regulation of synaptic vesicle recycling, controls STON2 protein stability in collaboration with the COP9 signalosome complex (CSN). In the nucleus, may link the cytoskeleton with the nuclear envelope, this mechanism seems to be crucial for the control of nuclear polarity, cell movement and, specifically in neurons, nuclear envelope integrity. Participates in the cellular trafficking and may regulate the subcellular location of multipass membrane proteins such as the dopamine transporter SLC6A3, leading to the modulation of dopamine neurotransmission. In the endoplasmic reticulum, plays a role in the quality control of protein folding by increasing clearance of misfolded proteins such as SGCE variants or holding them in an intermediate state for proper refolding. May have a redundant function with TOR1B in non-neural tissues.
Subcellular location: Endoplasmic reticulum lumen {ECO:0000269|PubMed:29053766}. Nucleus membrane {ECO:0000269|PubMed:14970196, ECO:0000269|PubMed:29053766}; Peripheral membrane protein {ECO:0000305}. Cell projection, growth cone {ECO:0000250}. Cytoplasmic vesicle membrane {ECO:0000250}. Cytoplasmic vesicle, secretory vesicle {ECO:0000250}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle. Cytoplasm, cytoskeleton. Note=Upon oxidative stress, redistributes to protusions from the cell surface (By similarity). Peripherally associated with the inner face of the ER membrane, probably mediated by the interaction with TOR1AIP1. The association with nucleus membrane is mediated by the interaction with TOR1AIP2. {ECO:0000250}.
Interaction partners:
- Tumor necrosis factor receptor superfamily member 25
- Torsin-1A-interacting protein 2
- THAP domain-containing protein 1
- Torsin-1A-interacting protein 1
- Epsilon-sarcoglycan
- HLA class II histocompatibility antigen DQ alpha chain
- Protein-glutamine gamma-glutamyltransferase 2
- Torsin-1B
- Tubulin beta-4A chain
- Tumor necrosis factor receptor superfamily member 10A
Sequence:
MKLGRAVLGLLLLAPSVVQAVEPISLGLALAGVLTGYIYPRLYCLFAECCGQKRSLSREALQKDLDDNLFGQHLAKKIILNAVFGFINNPKPKKPLTLSLHGWTGTGKNFVSKIIAENIYEGGLNSDYVHLFVATLHFPHASNITLYKDQLQLWIRGNVSACARSIFIFDEMDKMHAGLIDAIKPFLDYYDLVDGVSYQKAMFIFLSNAGAERITDVALDFWRSGKQREDIKLKDIEHALSVSVFNNKNSGFWHSSLIDRNLIDYFVPFLPLEYKHLKMCIRVEMQSRGYEIDEDIVSRVAEEMTFFPKEERVFSDKGCKTVFTKLDYYYDD
Protein: Endolysin (EC 4.2.2.n2) (Lysis protein) (Lysozyme) (Transglycosylase) (P03706)
Organism: Escherichia phage lambda (Bacteriophage lambda)
Function: Endolysin with transglycosylase activity that degrades host peptidoglycans and participates with the holin and spanin proteins in the sequential events which lead to the programmed host cell lysis releasing the mature viral particles. Once the holin has permeabilized the host cell membrane, the endolysin can reach the periplasm and break down the peptidoglycan layer.
Subcellular location: Host cytoplasm {ECO:0000255|HAMAP-Rule:MF_04109}. Note=The endolysin is cytoplasmic, but can reach the periplasmic space with the help of the holins which disrupt the host cell membrane. {ECO:0000255|HAMAP-Rule:MF_04109, ECO:0000305|PubMed:24113139}.
Interaction partners:
Sequence:
MVEINNQRKAFLDMLAWSEGTDNGRQKTRNHGYDVIVGGELFTDYSDHPRKLVTLNPKLKSTGAGRYQLLSRWWDAYRKQLGLKDFSPKSQDAVALQQIKERGALPMIDRGDIRQAIDRCSNIWASLPGAGYGQFEHKADSLIAKFKEAGGTVREIDV
Protein: Interleukin-12 receptor subunit beta-1 (IL-12 receptor subunit beta-1) (IL-12R subunit beta-1) (IL-12R-beta-1) (IL-12RB1) (IL-12 receptor beta component) (CD antigen CD212) (P42701)
Organism: Homo sapiens (Human)
Function: Functions as an interleukin receptor which binds interleukin-12 with low affinity and is involved in IL12 transduction. Associated with IL12RB2 it forms a functional, high affinity receptor for IL12. Associates also with IL23R to form the interleukin-23 receptor which functions in IL23 signal transduction probably through activation of the Jak-Stat signaling cascade.
Subcellular location: Membrane; Single-pass type I membrane protein.
Interaction partners:
- Interleukin-23 receptor
- Non-receptor tyrosine-protein kinase TYK2
- Interleukin-12 receptor subunit beta-2
- Interleukin-23 subunit alpha
- Interleukin-12 subunit beta
- Tyrosine-protein kinase JAK2
- Signal transducer and activator of transcription 4
- Interleukin-27 receptor subunit alpha
- Signal transducer and activator of transcription 3
- Interleukin-12 subunit alpha
Sequence:
MEPLVTWVVPLLFLFLLSRQGAACRTSECCFQDPPYPDADSGSASGPRDLRCYRISSDRYECSWQYEGPTAGVSHFLRCCLSSGRCCYFAAGSATRLQFSDQAGVSVLYTVTLWVESWARNQTEKSPEVTLQLYNSVKYEPPLGDIKVSKLAGQLRMEWETPDNQVGAEVQFRHRTPSSPWKLGDCGPQDDDTESCLCPLEMNVAQEFQLRRRQLGSQGSSWSKWSSPVCVPPENPPQPQVRFSVEQLGQDGRRRLTLKEQPTQLELPEGCQGLAPGTEVTYRLQLHMLSCPCKAKATRTLHLGKMPYLSGAAYNVAVISSNQFGPGLNQTWHIPADTHTEPVALNISVGTNGTTMYWPARAQSMTYCIEWQPVGQDGGLATCSLTAPQDPDPAGMATYSWSRESGAMGQEKCYYITIFASAHPEKLTLWSTVLSTYHFGGNASAAGTPHHVSVKNHSLDSVSVDWAPSLLSTCPGVLKEYVVRCRDEDSKQVSEHPVQPTETQVTLSGLRAGVAYTVQVRADTAWLRGVWSQPQRFSIEVQVSDWLIFFASLGSFLSILLVGVLGYLGLNRAARHLCPPLPTPCASSAIEFPGGKETWQWINPVDFQEEASLQEALVVEMSWDKGERTEPLEKTELPEGAPELALDTELSLEDGDRCKAKM