wanglab/gogpt-training-data huggingface dataset:
Protein: Tyrosine-protein phosphatase non-receptor type 1 (EC 3.1.3.48) (CPTP1) (Protein-tyrosine phosphatase 1B) (PTP-1B) (O13016)
Organism: Gallus gallus (Chicken)
Function: May play an important role in CKII- and p60c-src-induced signal transduction cascades. May regulate the EFNA5-EPHA3 signaling pathway which modulates cell reorganization and cell-cell repulsion. May also regulate the hepatocyte growth factor receptor signaling pathway through dephosphorylation of MET (By similarity).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}.
Interaction partners:
- Insulin receptor substrate 1.
- Tyrosine-protein kinase receptor
- Proto-oncogene tyrosine-protein kinase Src
- Insulin receptor substrate 4.
- Catenin beta 1
- Cadherin-2
- Tyrosine-protein kinase JAK2
- Uncharacterized protein.
- Growth factor receptor-bound protein 2
- Tyrosine-protein kinase.
Sequence:
MEIEKEFHRLDQAASWAAIYQDIRHEASDFPCKVAKHPRNKNRNRYRDVSPFDHSRIKLNQGDNDYINASLIKMEEAQRSYILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRVMEKGSIKCAQYWPRKEEKEMFFEDTNLKLTLISEDIKSYYTVRQLELENLTTQETREILHFHYTTWPDFGVPESPASFLNFLFKVRESGSLNPEYGPVVVHCSAGIGRSGTFCLVDTCLLLMDKRKDPSSVDVKQVLLEMRKYRMGLIQTADQLRFSYLAVIEGAKFIMGDASVQEQWKELSNEDLDPPPEHTPPPPRPPKRTSEMHNGRMHEHAEFFPKHQVVEEEIRCSVSTAEETVSDGRVFSSVPLITDSTSQDTEIRRRTVGENLHVTAHKEESKSESVEEDDENMMTTWKPFLVNICMFTFLTAGAYLCYRVCFH
Protein: Dpr-interacting protein zeta, isoform A (Dpr-interacting protein zeta, isoform B) (FI03417p) (Q9VLF0)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Defective proboscis extension response 16, isoform C
- Defective proboscis extension response 6, isoform F
- Defective proboscis extension response 13, isoform B
- Defective proboscis extension response 20
Sequence:
MLPPSWHLIGALLVLAATAGDSTNKIILPQILNGGGGGGGVGTAQGKHPSGSKTVATGVVPNFGGAAGNGAGGGGPVAGSGTGSTVVGSNGVIVAGGGANVPTSNLNIVVEEPEFTEYIENVTVPAGRNVKLGCSVKNLGSYKVAWMHFEQSAILTVHNHVITRNPRISVTHDKHDRHRTWYLHINNVHEEDRGRYMCQINTVTAKTQFGYLNVVVPPNIDDSLSSSDVIVREGANISLRCRASGSPRPIIKWKRDDNSRIAINKNHIVNEWEGDTLEITRISRLDMGAYLCIASNGVPPTVSKRIKVSVDFPPMLLIPHQLVGAPEGFNVTIECFTEAHPTSLNYWTRGEGPIIHDSHKYKVEATVGLPAYKTHMKLTIINVSSGDDGIYKCVAKNPRGETDGIIRLYVSYPPTTASSGIYSTDTHWGENGINNNYAYGGPDSTRSIYAQDKNTRYQSNLNEIGLSEQKSFLDKTQNPLLANGNANEADAESNGARGHNPSMAIAWLFVVIATLLLTIRSAVGSSHSLSLC
Protein: UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase (EC 6.3.2.13) (Meso-A2pm-adding enzyme) (Meso-diaminopimelate-adding enzyme) (UDP-MurNAc-L-Ala-D-Glu:meso-diaminopimelate ligase) (UDP-MurNAc-tripeptide synthetase) (UDP-N-acetylmuramyl-tripeptide synthetase) (P9WJL3)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Catalyzes the addition of meso-diaminopimelic acid to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate (UMAG) in the biosynthesis of bacterial cell-wall peptidoglycan.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00208}.
Interaction partners:
- UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-alanine ligase
- UDP-N-acetylmuramoylalanine--D-glutamate ligase
- UDP-N-acetylglucosamine--N-acetylmuramyl-
- UDP-N-acetylmuramate--L-alanine ligase
- Phospho-N-acetylmuramoyl-pentapeptide-transferase
- Probable peptidoglycan glycosyltransferase FtsW
- Diaminopimelate epimerase
- UDP-N-acetylglucosamine 1-carboxyvinyltransferase
- Cell division protein FtsQ
- D-alanine--D-alanine ligase
Sequence:
MSSLARGISRRRTEVATQVEAAPTGLRPNAVVGVRLAALADQVGAALAEGPAQRAVTEDRTVTGVTLRAQDVSPGDLFAALTGSTTHGARHVGDAIARGAVAVLTDPAGVAEIAGRAAVPVLVHPAPRGVLGGLAATVYGHPSERLTVIGITGTSGKTTTTYLVEAGLRAAGRVAGLIGTIGIRVGGADLPSALTTPEAPTLQAMLAAMVERGVDTVVMEVSSHALALGRVDGTRFAVGAFTNLSRDHLDFHPSMADYFEAKASLFDPDSALRARTAVVCIDDDAGRAMAARAADAITVSAADRPAHWRATDVAPTDAGGQQFTAIDPAGVGHHIGIRLPGRYNVANCLVALAILDTVGVSPEQAVPGLREIRVPGRLEQIDRGQGFLALVDYAHKPEALRSVLTTLAHPDRRLAVVFGAGGDRDPGKRAPMGRIAAQLADLVVVTDDNPRDEDPTAIRREILAGAAEVGGDAQVVEIADRRDAIRHAVAWARPGDVVLIAGKGHETGQRGGGRVRPFDDRVELAAALEALERRA
Protein: Uncharacterized protein (Q57Z82)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Uncharacterized protein
- Ribosomal protein L30 ferredoxin-like fold domain-containing protein
- Large ribosomal subunit protein mL46
- Uncharacterized protein
- Uncharacterized protein
- Uncharacterized protein
- Uncharacterized protein
- Large ribosomal subunit protein mL43
- LIM zinc-binding domain-containing protein
- 39S ribosomal protein L28
Sequence:
MLNRSRLRRVWLGGTAANTSLGRDVMPSTGKYINIVSPTDVAANISAGAMPPEANVAAALPVPRIQYSKWNRALRSDVYDELLKLPLRYKLHDFAKLCPPQRCQEEPEAVGVVGRDSAVGYLPPLGPADPLDTIPFFVHRSSNGVLPGKVFSMHPRNLMPAFYLRIQQVEGDMFRFEEELLKIFPTKKIFVRSHSIYVYNVALDGRMVLHHWLLGLGF
Protein: RNA exonuclease 4 (EC 3.1.-.-) (Exonuclease XPMC2) (Prevents mitotic catastrophe 2 protein homolog) (hPMC2) (Q9GZR2)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus, nucleolus {ECO:0000269|PubMed:10908561, ECO:0000269|PubMed:12429849}.
Interaction partners:
- Oligoribonuclease, mitochondrial
- tRNA
- ATP-dependent RNA helicase DDX55
- RNA-binding protein 34
- Suppressor of SWI4 1 homolog
- U3 small nucleolar ribonucleoprotein protein IMP4
- 60S ribosome subunit biogenesis protein NIP7 homolog
- Calcium-binding and coiled-coil domain-containing protein 2
- Activator of basal transcription 1
- rRNA-processing protein UTP23 homolog
Sequence:
MGKAKVPASKRAPSSPVAKPGPVKTLTRKKNKKKKRFWKSKAREVSKKPASGPGAVVRPPKAPEDFSQNWKALQEWLLKQKSQAPEKPLVISQMGSKKKPKIIQQNKKETSPQVKGEEMPAGKDQEASRGSVPSGSKMDRRAPVPRTKASGTEHNKKGTKERTNGDIVPERGDIEHKKRKAKEAAPAPPTEEDIWFDDVDPADIEAAIGPEAAKIARKQLGQSEGSVSLSLVKEQAFGGLTRALALDCEMVGVGPKGEESMAARVSIVNQYGKCVYDKYVKPTEPVTDYRTAVSGIRPENLKQGEELEVVQKEVAEMLKGRILVGHALHNDLKVLFLDHPKKKIRDTQKYKPFKSQVKSGRPSLRLLSEKILGLQVQQAEHCSIQDAQAAMRLYVMVKKEWESMARDRRPLLTAPDHCSDDA
Protein: Hemolysin transporter protein ShlB (P15321)
Organism: Serratia marcescens
Function: Interacts with the cell-bound hemolysin. Necessary for the extracellular secretion and activation of hemolysin.
Subcellular location: Cell outer membrane.
Interaction partners:
- Hemolysin
- Surface layer protein.
- LuxR-family transcriptional regulator.
- Serralysin
Sequence:
MIKKITALTLLVSTALSAETLPDSHMMQDMSMGESRRALQDSTREVNQLIEQRRYQQLKQQRLLAEPAAPALPQSAQCLPIAGVYLQGVTLLSPADLSALSGLPEQCISSNDINRLTRELTRLYVQKGYITARVQIVRPNSQGELGLSVTEGFIEKIEGGDRWVNSRLLFPGLEGKPLKLTELDQGLDQANRLQSNTTKLDILPGRQVGGSVIRLRNQHAKPWLITAGTDNYGQKSTGRWLARATATLDSPFGLSDFVSLNANSTLENPAHRYNRAYTLLYSLPYGAFTFSGFASFSSYENHQQLPHNVVKLHGQTQQYGLRSDYVFYRDHDQIDSLSGQLTYKRIDNYFESVRLEVSSPTLTLAELSASHLQILPNGVFSANLSVEQGMPWLGAGRHPSSVHLDSQFTKGKLFANLSQRLRLGDATYQLNNLFYGQYSRDPLPGVEWLSLTDRSAVRGFSRSTQSGDNGWYLQNTLSRSFNLGATTLTPRLGADVGRILPRQDNSGWRSSAGISTGATLRYQRALVDLEVSRGWILSNHATPEDPVQVLARFSYTF
Protein: GH11519p (Midline fasciclin, isoform B) (Midline fasciclin, isoform D) (Midline fasciclin, isoform L) (Midline fasciclin, isoform P) (Q9VGE9)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MLRLWACLLLLGSIQIQAVPFYGDSGYDTEFVPLEHQQQPQGRQETAATVPAQTPSGVEQKPFNVDTITTDVNSPNPAIFFQQSFPFFGNEFFNSFGGFGFGAAQEPWWKGPNVCTEKEEDETVASETEAEETVDTFGQERDGVTNVVRSPLFGQFQFSVNSCAEKPNKHVCTKIVNQNGKKKTLTLTRQCCYGYGRPRNADFTTPCEKIDIKDVEATASDMGAKQFLESARTAGELADMLGAGSGKKVTLFVPNDAAFMEYRGHHQQENNVEDAKAEASKPSIYKLHAVLGEVQLEDVPNEKLLQTELPDQKIRINSYQLPAALGLEPYRFAANCVPIEKHDKLSEQALVHTLGGVLKPLTKNLMDIIRERADMSIMRTVLEKTNLSAMLEDDKPVTIFVPTDAAFDKLEPHLRRALKEGRGCASNILKNHLLDLTFCSLATVPGAKTTAYNLLGEPLLLNRTHRAANQTGPTPIYINNLAKIIDADIMGTNGVLHVIDTILPTESALPMTSLMSQKNLTIFQRLLEASGYDDQFDDLDNVTIFAPTDKALQNTEWARMLKEQPELLNHNLDLLEFLNYHVVKPMIKTCDLSEKSLPTVAGSSVRLNLYSTHALFSDVMNRATVNCARLVHFDDESCGSVLHQVDRALAPPKNNMLKLLEANPNYSKFLELVRKANLTQLLSNDSRSLTLLVPKNDIFEELNESGEGSKPADPMALVKTHIVEDVVCCAGIIPTNWPFVRSIESISGQHLRITRDRRPKIENAGVTKCDVVATNGILHEINDIIVPRPQRQQQQRPQLIPPGAGYQPQGDFDVFF
Protein: Uncharacterized protein, isoform C (A0A0B4KF71)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MSLFRKPKKIQRRVFSSNADEEEDGASLDPDAEMEAPPPPIISGKREKEKSRKAIKPQEDNSKPKALLSFADDEDDGEVFQVRKSSHSKKVMRMLDKERRKKKREERAENSGHPGGENGSTQHLESSGGPSSGPPNSNSNPANAGRYKSASDQSKSKKSDNHMIQTEIRTDDFVVS
Protein: Shewanella-like protein phosphatase 1 (EC 3.1.-.-) (A0A509AQU3)
Organism: Plasmodium berghei (strain Anka)
Function: Phosphatase which plays an essential role in the development and differentiation of the ookinete and in the formation of ookinete micronemes.
Interaction partners:
- Mitogen-activated protein kinase
- Protein phosphatase PP2A regulatory subunit A, putative
- Protein SOC1
- Protein phosphatase inhibitor 3, putative
Sequence:
MIFKKALYILLFLYIAIVKKGESKPGSKHPFLFKNLVIDKKKLDSSYYNKYDNIKWNGKIIAIGDIHGDIESLKLILRHSKLIGENDNWIGDNVLLVQNGDVFDRGIYGPIIYNFLFKLQKEAIKKNSRVILIMGNHEQLNLCGYFNYVNPKEIEMFFHNDANYRYHSFVNPYGEYHKRLIRLPPMVKVNNIIFTHGGLNLLISKLSINDINLKTRLQIENNCKPIKYDSFQNYLSRDGVLWSDAMSRNVPYYEKEKCSELFQILDKYDAKYLVVGHTRQPSHQIGSYCNNHYFLIDTGMSLFTNYGQPYPNYLKIDDHKIKAVRLIVEKKKKCPHTEIQLNTPNKIKYCVQESQTNLNPVL
Protein: Clusterin (E7ETB4)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm, cytosol {ECO:0000256|ARBA:ARBA00004514}. Cytoplasm, perinuclear region {ECO:0000256|ARBA:ARBA00004556}. Cytoplasmic vesicle, secretory vesicle, chromaffin granule {ECO:0000256|ARBA:ARBA00004248}. Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00004240}. Mitochondrion membrane {ECO:0000256|ARBA:ARBA00004346}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004346}; Cytoplasmic side {ECO:0000256|ARBA:ARBA00004346}. Nucleus {ECO:0000256|ARBA:ARBA00004123}. Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
MMKTLLLFVGLLLTWESGQVLGDQTVSDNELQEMSNQGSKYVNKEIQNAVNGVKQIKTLIEKTNEERKTLLSNLEEAKKKKEDALNETRESETKLKELPGVCNETMMALWEECKPCLKQTCMKFYARVCRSGSGLVGRQLEEFLNQSSPFYFWMNGDRIDSLLENDRQQTHMLDVMQDHFSRASSIIDELFQDSLMPFSPYEPLNFHAMFQPFLEMIHEAQQAMDIHFHSPAFQHPPTEFIREGDDDRTVCREIRHNSTGCLRMKDQCDKC
Protein: Transcriptional regulator ATRX (EC 3.6.4.12) (ATP-dependent helicase ATRX) (X-linked nuclear protein) (A0A096LNW1)
Organism: Homo sapiens (Human)
Subcellular location: Chromosome, telomere {ECO:0000256|ARBA:ARBA00004574}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MTAEPMSESKLNTLVQKLHDFLAHSSEESEETSSPPRLAMNQNTDKISGSGSNSDMMENSKEEGTSSSEKSKSSGSSRSKRKPSIVTKYVESDDEKPLDDETVNEDASNENSENDITMQSLPKGTVIVQPEPVLNEDKDDFKGPEFRSRSKMKTENLKKRGEDGLHGIVSCTACGQQVNHFQKDSIYRHPSLQVLICKNCFKYYMSDDISRDSDGMDEQCRWCAEGGNLICCDFCHNAFCKKCILRNLGRKELSTIMDENNQWYCYICHPEPLLDLVTACNSVFENLEQLLQQNKKKIKVDSEKSNKVYEHTSRFSPKKTSSNCNGEEKKLDDSCSGSVTYSYSALIVPKEMIKKAKKLIETTANMNSSYVKFLKQATDNSEISSATKLRQLKAFKSVLADIKKAHLALEEDLNSEFRAMDAVNKEKNTKEHKVIDAKFETKARKGEKPCALEKKDISKSEAKLSRKQVDSEHMHQNVPTEEQRTNKSTGGEHKKSDRKEEPQYEPANTSEDLDMDIVSVPSSVPEDIFENLETAMEVQSSVDHQGDGSSGTEQEVESSSVKLNISSKDNRGGADCQEVPQDKDGYKSCGLNPKLEKCGLGQENSDNEHLVENEVSLLLEESDLRRSPRVKTTPLRRPTETNPVTSNSDEECNETVKEKQKLSVPVRKKDKRNSSDSAIDNPKPNKLPKSKQSETVDQNSDSDEMLAILKEVSRMSHSSSSDTDINEIHTNHKTLYDLKTQAGKDDKGKRKRKSSTSGSDFDTKKGKSAKSSIISKKKRQTQSESSNYDSELEKEIKSMSKIGAARTTKKRIPNTKDFDSSEDEKHSKKGMDNQGHKNLKTSQEGSSDDAERKQERETFSSAEGTVDKDTTIMELRDRLPKKQQASASTDGVDKLSGKEESFTSLEVRKVAETKEKSKHLKTKTCKKVQDGLSDIAEKFLKKDQSDETSEDDKK
Protein: Uncharacterized protein At1g03900 (Q681Q7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- AP-2 complex subunit mu
- AP-2 complex subunit sigma
- Calcium sensing receptor, chloroplastic
- AP-2 complex subunit alpha-2
- AP-2 complex subunit alpha-1
- Beta-adaptin-like protein C
- Beta-adaptin-like protein A
- Beta-adaptin-like protein B
- Clathrin heavy chain 1
- Clathrin heavy chain 2
Sequence:
MSFEEEEEEETFEHTLLVVREVSVYKIPPRTTSGGYKCGEWLQSDKIWSGRLRVVSCKDRCEIRLEDSNSGDLFAACFVDPGRRENSVEPSLDSSRYFVLRIDDGRGKYAFIGLGFAERNEAFDFNVALSDHEKYVRREKEKETGETSESDNHIDIHPAVNHRLKEGETIRINVKPKPTTNGTGMLSAALSGTGKPKPLALAPPPKAAGVTRSPLPPPPNDPVASRIASDGCKESRRNEPLSDLSQLKKNLPSTAGSGSSKSTGAASGWAAF
Protein: Endoplasmic reticulum chaperone BiP homolog (Heat shock 70 kDa protein D) (EC 3.6.4.10) (P20163)
Organism: Caenorhabditis elegans
Function: Endoplasmic reticulum chaperone that plays a key role in protein folding and quality control in the endoplasmic reticulum lumen (By similarity). Required for ER dynamics during the first embryonic cell divisions. Specifically, controls ER transition into sheet-like structures at the onset of mitosis, possibly by regulating homotypic membrane fusion.
Subcellular location: Endoplasmic reticulum lumen {ECO:0000250|UniProtKB:P11021}.
Interaction partners:
- Endoplasmin homolog
- Hypoxia up-regulated protein 1
- J domain-containing protein
- Chaperonin homolog Hsp-60, mitochondrial
- Serine/threonine-protein kinase/endoribonuclease ire-1
- Hypoxia up-regulated protein 1
- Armadillo-type protein
- DnaJ homolog dnj-20
- Thioredoxin domain-containing protein
- DnaJ homolog subfamily C member 10
Sequence:
MKVFSLILIAFVANAYCDEGASTEKEEKMGTIIGIDLGTTYSCVGVFKNGRVEIIANDQGNRITPSYVAFSGDQGERLIGDAAKNQLTINPENTIFDAKRLIGRFYNEKTVQQDIKHWPFKIVDKSNKPNVEVKVGSETKQFTPEEVSAMVLTKMKQIAESYLGHEVKNAVVTVPAYFNDAQKQATKDAGSIAGLNVVRIINEPTAAAIAYGLDKKDGERNILVFDLGGGTFDVSLLTIDSGVFEVLATNGDTHLGGEDFDQRVMEYFIKLYKKKSGKDLRKDNRAVQKLRREVEKAKRALSTQHQTKIEIESLFDGEDFSETLTRAKFEELNMDLFRATLKPVQKVLEDADMKKTDVHEIVLVGGSTRIPKVQQLIKDYFNGKEPSRGINPDEAVAYGAAVQAGVIGGVENTGDVVLLDVNPLTLGIETVGGVMTKLIGRNTVIPTKKSQVFSTAADSQSAVSIVIYEGERPMVMDNHKLGNFDVTGIPPAPRGVPQIEVTFEIDVNGILHVSAEDKGTGNKNKLTITNDHNRLSPEDIERMINDADKFAADDQAQKEKVESRNELEAYAYQMKTQIADKEKLGGKLTDEDKVSIESAVERAIEWLGSNQDASTEENKEQKKELESVVQPIVSKLYSAGGQGEQASEEPSEDHDEL
Protein: Leptin receptor overlapping transcript-like 1 (Q6FHL7)
Organism: Homo sapiens (Human)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MAGIKALISLSFGGAIGLMFLMLGCALPIYNKYWPLFVLFFYILSPIPYCIARRLVDDTDAMSNACKELAIFLTTGIVVSAFGLPIVFARAHLIEWGACALVLTGNTVIFATILGFFLVFGSNDDFSWQQW
Protein: P300/CBP acetyltransferase-related protein-like protein (F4I4I6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Probable mediator of RNA polymerase II transcription subunit 15c
- Seipin-3
- Histone acetyltransferase
- Uncharacterized protein At3g24150
- Mediator of RNA polymerase II transcription subunit 15a-like protein
- ATP-dependent DNA helicase Q-like 3
- Gb|AAF19561.1
- Mediator of RNA polymerase II transcription subunit 15a
- Glutamyl-tRNA
Sequence:
MDNDVFQIRRSMRDAIFVQLEKRNPLPNDDASKGKHLDAAKRLEEGLFKMAMTKEEYLNPSTLESRLTSLIKGRQLNKYKHQHADSSTLGTTITPTPGVSAEPTMQDNENRDQCETEIAENLKSVSLEP
Protein: ATP-sensitive inward rectifier potassium channel 12 (Inward rectifier K(+) channel Kir2.2) (IRK-2) (Inward rectifier K(+) channel Kir2.2v) (Potassium channel, inwardly rectifying subfamily J member 12) (Q14500)
Organism: Homo sapiens (Human)
Function: Inward rectifying potassium channel that is activated by phosphatidylinositol 4,5-bisphosphate and that probably participates in controlling the resting membrane potential in electrically excitable cells. Probably participates in establishing action potential waveform and excitability of neuronal and muscle tissues. Inward rectifier potassium channels are characterized by a greater tendency to allow potassium to flow into the cell rather than out of it. Their voltage dependence is regulated by the concentration of extracellular potassium; as external potassium is raised, the voltage range of the channel opening shifts to more positive voltages. The inward rectification is mainly due to the blockage of outward current by internal magnesium.
Subcellular location: Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}. Cell membrane {ECO:0000269|PubMed:21209095}. Cell membrane, sarcolemma, T-tubule {ECO:0000250|UniProtKB:P52188}.
Interaction partners:
- Inward rectifier potassium channel 4
- Inward rectifier potassium channel 2
- Potassium voltage-gated channel subfamily KQT member 1
- Potassium voltage-gated channel subfamily KQT member 2
- Potassium voltage-gated channel subfamily KQT member 5
- Potassium voltage-gated channel subfamily KQT member 4
- Potassium voltage-gated channel subfamily KQT member 3
- Guanine nucleotide-binding protein G
- ATP-sensitive inward rectifier potassium channel 14
- Inward rectifier potassium channel 18
Sequence:
MTAASRANPYSIVSSEEDGLHLVTMSGANGFGNGKVHTRRRCRNRFVKKNGQCNIEFANMDEKSQRYLADMFTTCVDIRWRYMLLIFSLAFLASWLLFGIIFWVIAVAHGDLEPAEGRGRTPCVMQVHGFMAAFLFSIETQTTIGYGLRCVTEECPVAVFMVVAQSIVGCIIDSFMIGAIMAKMARPKKRAQTLLFSHNAVVALRDGKLCLMWRVGNLRKSHIVEAHVRAQLIKPRVTEEGEYIPLDQIDIDVGFDKGLDRIFLVSPITILHEIDEASPLFGISRQDLETDDFEIVVILEGMVEATAMTTQARSSYLANEILWGHRFEPVLFEEKNQYKIDYSHFHKTYEVPSTPRCSAKDLVENKFLLPSANSFCYENELAFLSRDEEDEADGDQDGRSRDGLSPQARHDFDRLQAGGGVLEQRPYRRESEI
Protein: Eukaryotic translation initiation factor 5 (H0YLZ1)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MSVNVNRSVSDQFYRYKMPRLIAKVEGKGNGIKTVIVNMVDVAKALNRPPTYPTKYFGCELGAQTQFDVKNDRYIVNGSHEANKLQDMLDGFIKKFVLCPECENPETDLHVNPKKQTIGNSCKACGYRGMLDTHHKLCTFILKNPP
Protein: Lengsin (Glutamate-ammonia ligase domain-containing protein 1) (Q29RF4)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- tRNA wybutosine-synthesizing protein 3 homolog
- GMP synthase
- Gamma-crystallin N-A
- Grifin
- Crygmx protein
- Lens intrinsic membrane protein 2.2
- Crystallin, gamma MX,-like 2
- Delta-1-pyrroline-5-carboxylate synthase
- Isoamyl acetate-hydrolyzing esterase 1 homolog
- Crystallin, zeta
Sequence:
MQESEESKDTETVPDQVDGGSMSARKKDADPREKRLSSSEWDRKGTPVAISQSKVPISGPTNDPILISIGPPHHFPSVSSESQYQGFSREEDYINRHGWRRENVQYYPSNTEGGVPKQTMDELKSVLRESSLLSAKGQDEGRSYPPGQRVDCKPDQEPSRTFSTFKPYSEARRASRQRDRNWDSSGSSRTDGPPNRSSGMNSPTFQASDWGEVGTSQSDKERSQAHSFASQSFISDVERIKQQIARENLSFVRFEATDLHGVSRSKTVPARFFHEKAVYGIPMPRSYLELTLSPQINEVDHASAVNFSSDVLLVPDLSTFQILPWADQTARLICDPCTITGVPLRTSPRLIAKMMLGQLQSMGFSLHSSFTYECCIFGSPEHVGPKAVFFPATTLLSNNDQPFLQQLVKGMYNMGVDVESFSSANGPGQMEICFKPRFGMDAADNAYTFRTGIKEMARKYDYIATFFTYENIQNSGLLSHSLWDASGRRSLFHSGNGELSEIGRKWLSGLLHHSAALSCLLAPGISCRTQISKGKKDSKNHVYATCGCNDNSCDFNVKIHGGRETHIDNKLASAMANPYIVLAATIAAGLDGIKRNLNAEQVLSRAPNQQKQFVIPVKLDDALLALAEDSVICGALGEPFVQYFIAMKQIEMESQEDADRNEGLDYFI
Protein: Erythrocyte membrane protein 1, PfEMP1 (Q8I3E5)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
Sequence:
MGPKTRAPDYSSAPDAKHLLDMIGKDVHEKAKSEAKNYIEELKGDLNTANGRSSETRYTTDTCTLVKEYYTTRLGVNNERNPCKGLSGIIVERFSDTLGGQCTDHRIKGNNRNVTGGACAPYRRLHVCDKNMEKIPTSKTSTDTLLAEVCYAAKYEGDSISGRYRQHQLTNKGSQLCTVLARSFADIGDIVRGRDLYLGYDDKEKEKRDQLESKLKVIFGNIYGNLDKNNRYNDDTPEYYKLREAWWDANRAKVWEAITCDAPDNAKYFRGTCGGDDEKTGTQAIHKCRCTKSSGGKPGKNETDQVPTYFDYVPQFLRWFEEWAEDFCRKKKHKLKDVKTNCRNDEEQRYCSGNGFDCTKTIYKKGRIVIGEHCTKCSVWCRMYESWIDNQKKEFLKQKRKYKTEISGGDGGGSSRKKRVARSSSSSDDNGYESKFYKKLKEVGYQDVDSFLEKLNNEEICKKITDEKENIDFKTADNSLNKNINKEGTFYHSKYCEVCPGCGVERNGSGWEEKSGGTCDVKKPYKIRDDAPFNDINVLSFGDKGNEIKQKIDKFCKTQNGNSGKASSSGSGDCGTNIDSSLCEPWKCYKGEDVMKPEDDDDQQDYENMKNAGGLCILPNPKKHESEKKTADEPAEFQKTYNDFFYFWIRRFLNDSMYWRGKIGGCLKNKSEKCKNECNTNCDCFKKWIGKKKEEWDKIKKHFKTQDFGSKGFLGQFGYDEVLKYVLNIDELFKDIKDGYGNAKELEGIKKLLEEEERKNQVEAADGGASSGKDNTTIDKLLKHEEQDATKCKDCKPPEESLARAEVAGDNIPKKEDSDEEEEEEEEGTEGTGEVEENVEEDNTENKDQEDVSGEGSKEAEKEPTAKKDEAEKVCETVKSALTGDDLTKACQQKYQYGKEKFPNWKCIPSGDKTDTSSESESPPRQRRDTTSGVVTTAPSSAKSGDTTGSICVPPRRRKLYIGKIKEWAGIQLKSQVEGGGTGKQSSQLQQQQQQQQEQQQQQQQLKPQSPVASNSTLTTSAKQSPSNPRADDLRDAFIQSAAIETFFLWHRYKKIKEKEKKEKQEEAQGNVYTQTDENKNKDPQNELNGGKIPDGFLRQMFYTLADYKDILEGKNIVVDMLSGNDKDTMKKIQAKIDEILPKNGTSPGSSSGNDPESWWKNHGEHIWNAMVCALTYTDSEAKEQPPIQDKEVKKALLDKEGASNEPISQYQYKTVELKEESSDTKPQIASAPSDTPTLNNPKLTEFVEIPPFFRWLHEWGSDFCDKRARMLKNVKKACREKGDDEYKCSGDGHDCTKNGNLGHHKMLEDPNCPRCYEQCRKYRKWIDIKFEEFHNQKHKYQGEYDKLKVNSSVDYKKLQGYSTAADFLKELRHCKDGQTSEEKDNDNKIDFKEPLKTFGHSKYCEMCPSYEVNCNGRRARSGGNDQCTPVNGNGNTWDSVFEGISGNGENSTITVEMIDRRGPFIKEYSKDLKNSEQSKDSNDLFKTSRLFKGIRKQEWTCKYKGENMDLCKLNNFNKVIDLNDYTTFKVLLIYWLEDFIEGYYILKKRKVFEQCKENGGNKCSEESKKNCACVKVWVDQKKEEWDQIRTHFNNRNQRKGDDDMKSSVKKILDPLIYRMDLKNGKRKFDELTDFLKAYECKCVDNAGNSEKDVVECLLENLKTKATSCQTQHQPSGKPGQTCENPITPPDDEDLVLEEEQNPENMRPGFCPPQTPAQQEETDGTCDAVAPGAAKKAEEESGIPPAAEPEADKGPEQADTEKKVPPKAAPARPKDKKRPKRQPRNVLEHPAVIPALMSSTIMWSIGIGFAAFTYFYLKKKTKSTIDLLRVINIPKSDYDIPTKLSPNRYIPYTSGKYRGKRYIYLEGDSGTDSGYTDHYSDITSSSESEYEEMDINDIYVPRAPKYKTLIEVVLEPSGKNTTASGKNTPIDTQNDIQSDGIPSSKITDNEWNTLKDEFISNMLQSEQPNDVPNDYSSGDIPFNTQPNTLYFDKPEEKPFITSIHDRNLLSGEEYSYDMSTNTMDDPKYVSNNVYSGIDLINDSLNSGNQHIDIYDELLKRKENELFGTNHVKQTSIHSVAKPISDDPIHNQLNLFHTWLDRQRDMCQQWNNKEEVLDKLKEKWENETHSGDINSGIPSGKLSDTPSDNNIHSDIHPSDIPSGKQSDIPSDNNIHSDIPYVLNTDVSIQIHMDNPKPINQFTNMDTILEDLDKYNEPYYDVQDDIYYDVNDHDTSTVDTNAMDVPSKVQIEMDVNTKLVKEKYPIADVWDI
Protein: Coatomer subunit alpha (Q9W0B8)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm {ECO:0000256|PIRNR:PIRNR003354}. Golgi apparatus membrane {ECO:0000256|ARBA:ARBA00004255, ECO:0000256|PIRNR:PIRNR003354}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004255, ECO:0000256|PIRNR:PIRNR003354}; Cytoplasmic side {ECO:0000256|ARBA:ARBA00004255}. Cytoplasmic vesicle, COPI-coated vesicle membrane {ECO:0000256|ARBA:ARBA00004347}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004347}; Cytoplasmic side {ECO:0000256|ARBA:ARBA00004347}.
Interaction partners:
- Coatomer subunit beta'
- Coatomer subunit zeta
- Coatomer subunit beta
- Coatomer subunit epsilon
- Coatomer subunit delta
- Coatomer subunit gamma
- Protein transport protein SEC23
- ADP-ribosylation factor GTPase activating protein 3, isoform H
- Protein transport protein Sec31A
- Centromere/kinetochore protein zw10
Sequence:
MLTNFESKSARVKGLSFHPKRPWILVSLHSGVIQLWDYRMHTLLEKFDEHDGPVRGVAFHQQMPLFVSGGDDYKIKVWNYKQRRCIFTLLAHLDYVRTVAFHHEYPWILSASDDQTIRIWNWQSRNCICVLTGHNHYVMCAQFHPTEDQIVSASLDQTVRVWDISGLRKKNVAPGPGGLDDHLKGHPGATDLFGQADAVVKHVLEGHDRGVNWASFHPTLPLIVSGADDRLVKLWRMNEYKAWEVDTCRGHYNNVSSVLFHPRQDLILSNGEDRSIRVWDMTKRQCLFTFRRDNERFWILTAHPTLNLFAAGHDGGMVVFKLERERPAYAVHGNILYYVKERFLRKLDFTTTKDTVVMQLRPGKSPVYSMSYNPALNAVLICTRTNNLENSTYDLCQIPKDTESQSESDSKRSSGITAIWVARNRFAVLDRNQQLVIKNFKNEVTKKLPTFCEEIFYAGTGMLLIRDPEFVTLYEVQRLVSVGSIKLAKCRYVVWSPDMSLVALLCKHSVTICDRRLQYLCTVQENCRVKSGAWDESGVFIYTTSNHIKYAITNGDHGIIRTLDLPIYLTRVKGNQVFCLDRECRTRVLHIDPTEYKFKLALIQRKYDEVLHMVRNARLVGQSIIAYLQQKGYPEVALHFVKDEKTRFGLALECGNIEIALEAAKALDDKDCWDRLGQSALLQGNHQVVEMCYQRTKNFDKLSFLYLITGNLEKLKKMNKIAEIRKDVSAQYQGALLLGDVKERVNILKNCGQLSLAYLTAATHGFDELTESLGESITSQGNSLPEVNPNAQLLQPPVPIQQLETNWPLLSVSKGFFEGAMVTRAGSSATARQALNINADAALLDEHNGGGDGWGADADLGLDEDGDDEMHDALSNDGDGGAGGEEGAGWDVGDDDLVVPEELASKIKASALDSNYYAAPNKGLSPAQQWANNSPLVLDHVKAGSFETAFRLLHDQLGVVNFQPFKTLFLQNYACSRTSYTANPNLQSLSGYPLRNYSETNIKLQRPAVGIKLNDLVARLQAGYQLTTSGKFSEAVEKFHSILISIPLLVVDTKLDAAEAQQLLRICAEYIVGLKMETVRKGMPKSTLEEQKRLCEMAAYFTHCKLQPVHQILTLRTALNMFFKLKNYKTAASFARRLLELAPRPDVAQQVRKILQACEVNPVDEHQLQYEEFNPFTICGISWKPLYRGKPEVTCPFCSSSFDPQFKGNLCTVCEVSQIGKDSIGLRISNLQFR
Protein: Succinate--CoA ligase [ADP/GDP-forming] subunit alpha, mitochondrial (EC 6.2.1.4) (EC 6.2.1.5) (Succinyl-CoA synthetase subunit alpha) (SCS-alpha) (O19069)
Organism: Sus scrofa (Pig)
Function: Succinyl-CoA synthetase functions in the citric acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of either ATP or GTP and thus represents the only step of substrate-level phosphorylation in the TCA. The alpha subunit of the enzyme binds the substrates coenzyme A and phosphate, while succinate binding and specificity for either ATP or GTP is provided by different beta subunits.
Subcellular location: Mitochondrion {ECO:0000255|HAMAP-Rule:MF_03222}.
Interaction partners:
- Succinate--CoA ligase [GDP-forming] subunit beta, mitochondrial
- Succinate--CoA ligase subunit beta, mitochondrial
- Succinate dehydrogenase iron-sulfur subunit, mitochondrial
- 2-oxoglutarate dehydrogenase complex component E1
- Succinate dehydrogenase cytochrome b560 subunit, mitochondrial
- Succinate dehydrogenase flavoprotein subunit, mitochondrial
- 2-oxoglutarate dehydrogenase-like, mitochondrial
- ATP-citrate synthase
- Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex, mitochondrial
- 2-oxoadipate dehydrogenase complex component E1
Sequence:
MTAALVAAPAAATMASGSSGLAAARLLSRSFLLQQNGIRHCSYTASRKHLYVDKNTKVICQGFTGKQGTFHSQQALEYGTNLVGGTTPGKGGKTHLGLPVFNTVKEAKEQTGATASVIYVPPPFAAAAINEAIDAEVPLVVCITEGIPQQDMVRVKHRLLRQGKTRLIGPNCPGVINPGECKIGIMPGHIHKKGRIGIVSRSGTLTYEAVHQTTQVGLGQSLCVGIGGDPFNGTDFTDCLEIFLNDPATEGIILIGEIGGNAEENAAEFLKQHNSGPKSKPVVSFIAGLTAPPGRRMGHAGAIIAGGKGGAKEKITALQSAGVVVSMSPAQLGTTIYKEFEKRKML