wanglab/gogpt-training-data huggingface dataset:
Protein: Cyclin-dependent kinase 11B (EC 2.7.11.22) (Cell division cycle 2-like protein kinase 1) (CLK-1) (Cell division protein kinase 11B) (Galactosyltransferase-associated protein kinase p58/GTA) (PITSLRE serine/threonine-protein kinase CDC2L1) (p58 CLK-1) (P21127)
Organism: Homo sapiens (Human)
Function: Plays multiple roles in cell cycle progression, cytokinesis and apoptosis. Involved in pre-mRNA splicing in a kinase activity-dependent manner. Isoform 7 may act as a negative regulator of normal cell cycle progression.
Subcellular location: Cytoplasm. Nucleus.
Interaction partners:
- Matrix metalloproteinase-23
- Cyclin-L1
- SAP30-binding protein
- Matrix metalloproteinase-21
- Heat shock protein HSP 90-alpha
- Hsp90 co-chaperone Cdc37
- Pericentrin
Sequence:
MGDEKDSWKVKTLDEILQEKKRRKEQEEKAEIKRLKNSDDRDSKRDSLEEGELRDHRMEITIRNSPYRREDSMEDRGEEDDSLAIKPPQQMSRKEKAHHRKDEKRKEKRRHRSHSAEGGKHARVKEKEREHERRKRHREEQDKARREWERQKRREMAREHSRRERDRLEQLERKRERERKMREQQKEQREQKERERRAEERRKEREARREVSAHHRTMREDYSDKVKASHWSRSPPRPPRERFELGDGRKPGEARPAPAQKPAQLKEEKMEERDLLSDLQDISDSERKTSSAESSSAESGSGSEEEEEEEEEEEEEGSTSEESEEEEEEEEEEEEETGSNSEEASEQSAEEVSEEEMSEDEERENENHLLVVPESRFDRDSGESEEAEEEVGEGTPQSSALTEGDYVPDSPALSPIELKQELPKYLPALQGCRSVEEFQCLNRIEEGTYGVVYRAKDKKTDEIVALKRLKMEKEKEGFPITSLREINTILKAQHPNIVTVREIVVGSNMDKIYIVMNYVEHDLKSLMETMKQPFLPGEVKTLMIQLLRGVKHLHDNWILHRDLKTSNLLLSHAGILKVGDFGLAREYGSPLKAYTPVVVTLWYRAPELLLGAKEYSTAVDMWSVGCIFGELLTQKPLFPGKSEIDQINKVFKDLGTPSEKIWPGYSELPAVKKMTFSEHPYNNLRKRFGALLSDQGFDLMNKFLTYFPGRRISAEDGLKHEYFRETPLPIDPSMFPTWPAKSEQQRVKRGTSPRPPEGGLGYSQLGDDDLKETGFHLTTTNQGASAAGPGFSLKF
Protein: Polo kinase kinase 1 (Q7YZB2)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MSFITNLKKVFHLGGGEAKKKRLYNNIKMDTDPAEFWEMVGELGDGAFGKVYKAQHKEQKRFAAAKMCQLEDEENLSDHMVEIDILSEIKHPNIVELYEAFSIDDKLWMLIEYCDGGALDSIMVELEKPLTEPQIAYVCKHMTEGLTFLHRNKVIHRDLKAGNVLLTMEGGVKLADFGVSAKNKHTMQKHDTFIGTPYWMAPELVLCETFRDNPYDHKVDIWSLGITLIELAQMEPPNSEMSPMRVLLKIQKSEPPKLEQPSRWSKEFNDFLKKSLVKDPQVRPTTDVLMQHAFINRNLDAKPIKDLLLEYKAEVVEEVVDDETEEPRNSALQLDLDDDSASLQSQDIDKLPGTPTSILRDAKEQSQPSSSLPIAAAATAAAAATTTTKATTPDRPNHTKDDNAEAAAQQPPHTKVPAPAPPSSQQTPPPQVQQPPTPPAQPTAAVLQKKPEDVAAVAETSEKTESDKKHFVKKGKAPPPPSPLGLANAKPAASDSQTSPKKLATPEPTSPVTTAIEVAIGQEAMEPKPQPPSPTASSIVSVQSVASSSSSGSVSNAVLSSSTSLITINSDPPTPHHHQPLPPQPQHLILPNSLESVSQITVVTSTHPPVIIDNSVMPPQNEVIIVSNDMNKSTHLHESSTDDDFPSLDDSLGDATTPPHKQSSMILAVNEPAGVVPAPPSQPQTSSTVHARKLDESEVLIVSPSYADDDSAYNTASGSHSHDHSDHLMDTSHVSVVTVGDEGVKVKDSSNELVKRQPNGVGIVPEDVNIIVNRFKQEKRSPDSSLSENGSVRGRRGIEVLVGGSGGSDVDSIGTNTSQESRHETDHNNKQQYPAAALMPPPPPSLTNNHINETIDEEEEVVIRPKARVPAVVKSANAQGLTKEEIELRNLRKKTRKRTRKFEIDGVQMTTTTSRVIYGDDENGRIYDDHDFRKQELRELKLLQKQEKKQQTELHLKEQQAKEQQDRRFEQERSSLEKTYEADMDMLARQHKQLVEKTEQTQENELRSSSKRIRSEQEQELKIFRENLKQEIRLLKQEVDLFPKDKRKDEFKQRRSAMELDHEEKERAFLDSLKERHELLLRRLSEKHRDHLATINRNFLQQKQNAMRTREALLWELEEKQLHERHQLSKRHVKELCFMQRHQMIIRHEKELDQVKRMLQRKEEDMVKKQTMEKRALPKRIRAERKARDLMFRESLRISTNLDPEIERDRLKKFQEQEKKRYMQEERRFEVKHQKQLEELRATRESAIKELEQLQNEKRRALVEHEHSKLSEIDERLKGELREWREQLVPRKQRLEETFAQQLDEMETLYGGALIVSMPSDTLQRDHFTGSTRSSLSSYSEG
Protein: Citrate exporter 1 (G3Y4N5)
Organism: Aspergillus niger (strain ATCC 1015 / CBS 113.46 / FGSC A1144 / LSHB Ac4 / NCTC 3858a / NRRL 328 / USDA 3528.7)
Function: Transmembrane transporter that exports citrate across the cell membrane.
Subcellular location: Cell membrane {ECO:0000305|PubMed:30553933, ECO:0000305|PubMed:32990722}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MSSTTSSSRSDLEKVPVPQVTPRDSDSDKGSLSPEPSTLEAQSSEKPPHHIFTRSRKLQMVCIVSLAAIFSPLSSNIYFPALDDVSKSLNISMSLATLTITVYMIVQGLAPSFWGSMSDATGRRPVFIGTFIVYLVANIALAESKNYGELMAFRALQAAGSAATISIGAGVIGDITNSEERGSLVGIFGGVRMLGQGIGPVFGGIFTQYLGYRSIFWFLTIAGGVSLLSILVLLPETLRPIAGNGTVKLNGIHKPFIYTITGQTGVVEGAQPEAKKTKTSWKSVFAPLTFLVEKDVFITLFFGSIVYTVWSMVTSSTTDLFSEVYGLSSLDIGLTFLGNGFGCMSGSYLVGYLMDYNHRLTEREYCEKHGYPAGTRVNLKSHPDFPIEVARMRNTWWVIAIFIVTVALYGVSLRTHLAVPIILQYFIAFCSTGLFTINSALVIDLYPGASASATAVNNLMRCLLGAGGVAIVQPILDALKPDYTFLLLAGITLVMTPLLYVEDRWGPGWRHARERRLKAKANGN
Protein: FarB (C8VM39)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Interaction partners:
Sequence:
MTDSPVAPNPAVETDPKSKRKASSAGLSANSRPVKRRASKACCCCRARKVRCDVVENGSPCTNCRLDQVECVVTESKRRKKSRVDTEISNPQLSQSPAEILDDGALFGGLGDTQGIPHVAPTSPSQGSVDMEQGQHMPHLLYQSQVNRVDPGDRFRKRMAPNPLVPSSMPLSHVTSEIQQLLDPSFGSPRSSGIVLPDYIRGLPARLQKEDIDYLAMKGALTVPDVTLRNELLKAYIHYVHTYMPLLDLEDFLQTIVQNDGIRRMSLLLFQAVMFAGTAFIDLKHLQAAGYPSRKSARKSFFQRARLLYDFDYEVDRISLVQSLLLMTYWYETPDDQKDTWHWMGVSLSLAHTIGLHRDPANSRMDVRRQRMWKRIWWSTYTRDRLIALGMRRPMRVKDDDCDVPMLTLDDFEFHPFSPEIVSMVGNSEILQSVAHQRELASMFIEKAKLCLCVSHVLSAQYSVLSHKFGGTMETTMMLVPKKSAAETFEVRRCDQELEDWLAHLPSEIQYAPAAPAKLSEAQEVLHSHRALLKMVYLTTSSALHRPQVLPAVPFPSMDTELQDMSRNKVRFAAIEITNIAQDLHSLDLTRYFPTTGVTVLLPAVIIHLLDIKSSDQNVRMTSLQRFYQCMRILQRLREIYASADFATSFLEAAIRKAGIQLTVPPQELQKRSNNSGASRNTTLTPPPDSLAQKIPDLTYPKTGSMGGMTLNLVDEAQPAFASTPPPSDGSENGSTNNINPNYHRDAFRIPNIDDTEMSLSQLMDLANDAEVTQNDFDALINFDDAGADFFSSENGVENMTGDGNSKNFPFTFQDMVGFDSGNKSDAAASNGADAAQTEAPNLDMDLGLSLNA
Protein: Major S-layer protein (Cell surface glycoprotein) (Q8TSG7)
Organism: Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 / C2A)
Function: S-layer protein. The S-layer is a paracrystalline mono-layered assembly of proteins which coat the surface of the cell.
Subcellular location: Secreted, cell wall, S-layer {ECO:0000269|PubMed:19228054}. Cell membrane {ECO:0000305}.
Interaction partners:
- H
Sequence:
MKRFAALSLAALMLLTVFASAASAVDVIEIRGPVYNGSDIDDIIDTYGDGTILTMDATDFAAFYYDIDDNVTTETLSIEDVPDTEGNVIGEGGLIYETTIQEVEYEYYNPDAGWDNYSLMGFFAEKYIPINPDKADKLSKLILDSDDKYTIRTGEMLDLGEGYAIEAKQVDVDGEKVWLEFTKDGEFVDDEIISVSTADDEANTWDVELDDIEDEDDVIVLKVHVNQVFQGAVDSIAQIEGLWLIDYANAMTIESDDEFGNLDDVSIDGDTLTITNEDTFTLTRDDEEEIGEGLYFATADTPSNVLRFYAMKEITDPGTYEIRGQVASGFGDQSWDASSFAGFYYDIDDNVSTETLTVSDLDGNVIPEGGLVYTTTIADVDFEYYNPDAGWDQYPVMGFFAEEYIPINPDKADKIAKLVLDSDDKYTIRTGEMLDLGEGYAIEAKQVDVDGEKVWLEFTKDGEFVDDEIISVSTADDEANTWDVELDDIEDEDDVVVLKVHVNQVFQGAVDSIAQIEGLWLIDYANAMTIESDDEFGNLDDVSIDGDTLKISNEDTFTLTRDSEEEIGEGMYFMIADTSSSDLRYYPYVEKTIGEEVSGEEETPEETPTGEVTETEGEEETPTEVTETPTEGEPAPEETETTESEGTTPGFGFMFGLVGLLAVVYLVRRNN
Protein: Flavin adenine dinucleotide synthase (FAD synthase) (EC 2.7.7.2) (FAD pyrophosphorylase) (FMN adenylyltransferase) (P38913)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Catalyzes the adenylation of flavin mononucleotide (FMN) to form flavin adenine dinucleotide (FAD) coenzyme.
Subcellular location: Cytoplasm {ECO:0000305|PubMed:7799934}.
Interaction partners:
- Riboflavin kinase
- Adenylyl-sulfate kinase
- Low molecular weight phosphotyrosine protein phosphatase
- Mitochondrial FAD carrier protein FLX1
- Acid phosphatase PHO11
- Acid phosphatase PHO12
- Repressible acid phosphatase
- Constitutive acid phosphatase
- Probable acid phosphatase DIA3
- Sulfite reductase subunit beta
Sequence:
MQLSKAAEMCYEITNSYLHIDQKSQIIASTQEAIRLTRKYLLSEIFVRWSPLNGEISFSYNGGKDCQVLLLLYLSCLWEYFFIKAQNSQFDFEFQSFPMQRLPTVFIDQEETFPTLENFVLETSERYCLSLYESQRQSGASVNMADAFRDFIKIYPETEAIVIGIRHTDPFGEALKPIQRTDSNWPDFMRLQPLLHWDLTNIWSFLLYSNEPICGLYGKGFTSIGGINNSLPNPHLRKDSNNPALHFEWEIIHAFGKDAEGERSSAINTSPISVVDKERFSKYHDNYYPGWYLVDDTLERAGRIKN
Protein: BRI3-binding protein (I3-binding protein) (Cervical cancer 1 proto-oncogene-binding protein KG19) (HCCRBP-1) (Q8WY22)
Organism: Homo sapiens (Human)
Function: Involved in tumorigenesis and may function by stabilizing p53/TP53.
Subcellular location: Mitochondrion outer membrane {ECO:0000305|PubMed:17943721}; Multi-pass membrane protein {ECO:0000305|PubMed:17943721}.
Interaction partners:
Sequence:
MGARASGGPLARAGLLLLLLLLLLLGLLAPGAQGARGRGGAEKNSYRRTVNTFSQSVSSLFGEDNVRAAQKFLARLTERFVLGVDMFVETLWKVWTELLDVLGLDVSNLSQYFSPASVSSSPARALLLVGVVLLAYWFLSLTLGFTFSVLHVVFGRFFWIVRVVLFSMSCVYILHKYEGEPENAVLPLCFVVAVYFMTGPMGFYWRSSPSGPSNPSNPSVEEKLEHLEKQVRLLNIRLNRVLESLDRSKDK
Protein: 40S ribosomal protein S7 (Q38FE4)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- 40S ribosomal protein S4
- Ribosomal protein S19, putative
- Small ribosomal subunit protein uS4
- 40S ribosomal protein S14
- 40S ribosomal protein S5, putative
- 40S ribosomal protein S27, putative
- 40S ribosomal protein S15, putative
- 40S ribosomal protein S23, putative
- 40S ribosomal protein S16, putative
- 40S ribosomal protein S8
Sequence:
MSAQPHLRKLRKLKRANPSQEEEGVARVLFELEGSHKTLRAQLPRFHINTVRTSSSPRHKKTAMIILYPLRFIMLVRKIQRTLTAELEKRFPGNIVVLVAQRKITKRPNDVYKLQQVQRSRTSVAVFENILNDLIYPCDVVGRRWRYRTDGSKLMKVFLDARDRKRVESRLPLLAHVYKLLTHRTVTFGFMWNPKLQQVSSR
Protein: Pdia5 protein (Protein disulfide isomerase family A, member 5) (Protein disulfide-isomerase A5 precursor (EC 5.3.4.1)) (A8WG75)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MASWNRHGRRRRLVEMFIFLSLVAVTSALQAVKVSPLIEKVNDHKDFKKLLRTRTNVLVLYTKSASSGDAHLKLLSDVAQAVKGQGTIAWVNCGDSEGRKLCKKVKVDPSSKTKGVELLHYKDGTFHTEYNRPATFKSMVAFLKDPAGAPLWEENPEAKDVVHIESEKDFRKLLKREERPILMMFYAPWCGVCKRMQPIFQQAATETKGKYVLAGMNVHPAEFDGVKQEFSVKGYPTFCYFEKGKFLHHYENYGATSKDITDWLKNPQPPQPKTPEVPWSESGSAVFHLTDDSFDSFLEEHPSALIMFYAPWCGHCKKMKPEYDDAAETLNKDPNSPGVLAAVDTTIHKSTGERFKISGFPTVKYFEKGEEKYTLPHLRSKDKIIEWLKNPQAPPPPEKSWDEMPSSVSHLGAEDFRESLKKKKHALVMFYAPWCPHCKNAVPHFTTAAEMFKEDRKIAYAAVDCTKGQNHELCKQEGVEGYPTFNYYNYGKFSEKYNGERGEAGFTGFMRNLRGRDQEKVGKRKEEL
Protein: Glutamate receptor (Q61984)
Organism: Mus musculus (Mouse)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Postsynaptic cell membrane {ECO:0000256|RuleBase:RU367118}; Multi-pass membrane protein {ECO:0000256|RuleBase:RU367118}.
Interaction partners:
Sequence:
MGGALGPALLLTSLLGAWAGLGAGQGEQAVTVAVVFGSSGPLQAQARTRLTPQNFLDLPLEIQPLTIGVNNTNPSSILTQICGLLGAARVHGIVFEDNVDTEAAAQLLDFVSSQTHVPILSISGGSAVVLTPKEPGSAFLQLGVSLEQQLQVLFKVLEEYDWSAFAVITSLHPGHALFLEGVRAVADASYLSWRLLDVLTLELGPGGPRARTQRLLRQVDAPVLVAYCSREEAEVLFAEAAQAGLVGPGHVWLVPNLALGSTDAPPAAFPVGLISVVTESWRLSLRQKVRDGVAILALGAHSYRRQYGTLPAPAGDCRSHPGPVSPAREAFYRHLLNVTWEGRDFSFSPGGYLVQPTMVVIALNRHRLWEMVGRWDHGVLYMKYPVWPRYSTSLQPVVDSRHLTVATLEERPFVIVESPDPGTGGCVPNTVPCRRQSNHTFSSGDITPYTKLCCKGFCIDILKKLAKVVKFSYDLYLVTNGKHGKRVRGVWNGMIGEVYYKRADMAIGSLTINEERSEIIDFSVPFVETGISVMVARSNGTVSPSAFLEPYSPAVWVMMFVMCLTVVAITVFMFEYFSPVSYNQNLTKGKKSGGPSFTIGKSVWLLWALVFNNSVPIENPRGTTSKIMVLVWAFFAVIFLASYTANLAAFMIQEQYIDTVSGLSDKKFQRPQDQYPPFRFGTVPNGSTERNIRSNYRDMHTHMVKFNQRSVEDALTSLKMGKLDAFIYDAAVLNYMAGKDEGCKLVTIGSGKVFATTGYGIAMQKDSHWKRAIDLALLQFLGDGHLQLLQRGTEPSEPCAAAQPGPYSRLSPGQCAEDAAGGSRHGEHSGRERLFGPRHSYHRELGQQSPRACSHHLRPAVMHPGSSGTTESQRLAASRWGPHPASAPGPAASRSPRDLRRVASARRVPSILQARLGCAVASASRASGIAPLGLRAARAPGALPVARALPLQFLPSSREVRAPISPAIPGAPGARRPAAARAGTAGSAGGSAARGLGQGPAPSARFPAQLRGRSLHSIQPSACQVYRSRLRLPMSPKPAILPARGSNTVVAAAILPGGLCGGRASRGGRHLAAQTACLPAHPYPPAVLLGDCLPSPSTLFQPQSLAHWNLGASITQRQDPGARYRLQGQWGARRGQQGSLWDTRVSKVLHLEADLQPGIRSVRYRQLWFLLDWILWLVLAKFGGQTSFDSSAFFFEILAMRPQ
Protein: Glycine-rich protein (O80985)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MTNGGGGMSSGEGFRRRSSGEGFPAREFRWWVSGDRVFPRGFFGEGVQVGVPTVVSGEGVPAKVPGGDFSGKKVPAVVFRRVSSSDGGGRGSGGGGGGGSGLGW
Protein: Tapetal oleosin GRP-19 (T-oleosin GRP-19) (Glycine-rich protein 19) (AtGRP19) (Oleopollenin GRP-19) (Putative glycine-rich protein 1) (PutG-1) (Q42574)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Lipid-binding oleosin involved in anther tapetum development, especially for the physiology of tapetosomes. Also implicated in the formation of pollen coat.
Subcellular location: Secreted, extracellular space, extracellular matrix, pollen coat {ECO:0000269|PubMed:11431566, ECO:0000269|PubMed:26305561}. Lipid droplet {ECO:0000250|UniProtKB:Q9LY09}. Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}. Note=Surface of oil bodies (By similarity). Oleosins exist at a monolayer lipid/water interface (By similarity). Associated with discrete organelles within the anther tapetum called tapetosomes and with a network of structures previously described as fibrils or 'strings of beads' (PubMed:26305561). {ECO:0000250|UniProtKB:C3S7F0, ECO:0000269|PubMed:26305561}.
Interaction partners:
- Non-specific lipid-transfer protein 12
- Probable peroxygenase 7
- Uncharacterized protein At1g68875
- GDSL esterase/lipase EXL4
- Probable inactive peroxygenase-like protein
- 3-ketoacyl-CoA synthase 7
- GDSL esterase/lipase EXL6
- GDSL esterase/lipase EXL5
- F-box protein At1g19070
- LAZY1
Sequence:
MFEIIQAVFSAGVALALLTFAGITLGGSVVACIISTPLFVIFSPVLVPATIATTLLASGFTASGSFGATAFTILSWLYKKRTGRDLPKIPGLTPPAPASNPAGSGV
Protein: Mitochondrial import inner membrane translocase subunit TIM17-1 (Q9LN27)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Essential component of the TIM17:23 complex, a complex that mediates the translocation of transit peptide-containing proteins across the mitochondrial inner membrane. Links the inner and outer membranes (By similarity).
Subcellular location: Mitochondrion inner membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Mitochondrial import inner membrane translocase subunit TIM23-1
- Mitochondrial import inner membrane translocase subunit TIM23-3
- Mitochondrial import inner membrane translocase subunit TIM23-2
- Mitochondrial import inner membrane translocase subunit TIM50
- Probable mitochondrial import inner membrane translocase subunit TIM21
- Mitochondrial import inner membrane translocase subunit TIM44-2
- Mitochondrial import inner membrane translocase subunit TIM44-1
- GrpE protein homolog 1
- Mitochondrial import inner membrane translocase subunit TIM22-1
- Mitochondrial import inner membrane translocase subunit TIM22-4
Sequence:
MGTPESSREPCPDRILDDVGGAFAMGAVGGSAYHLIRGIYNSPGGARLSGGVQALRMSGPRSGGSFSVWGGLYSTFDCALVYARQKEDPWNSILSGAATGGFLSLRQGLGASARSALVGGVLLAMIEGVGIMLNKVQSTAHNEQFMEDHAATSLPYGMGQISGQSVPVPETSSSSSGSVSWFGSLFKKKKETEDHHSESRTHILESFDAPPVPTYEFK
Protein: Leucine-rich repeat neuronal protein 1 (Neuronal leucine-rich repeat protein 1) (NLRR-1) (Q61809)
Organism: Mus musculus (Mouse)
Subcellular location: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MARLSTGKAACQVVLGLLITSLTESSILTSECPQLCVCEIRPWFTPQSTYREATTVDCNDLRLTRIPGNLSSDTQVLLLQSNNIAKTVDELQQLFNLTELDFSQNNFTNIKEVGLANLTQLTTLHLEENQISEMTDYCLQDLSNLQELYINHNQISTISANAFSGLKNLLRLHLNSNKLKVIDSRWFDSTPNLEILMIGENPVIGILDMNFRPLSNLRSLVLAGMYLTDVPGNALVGLDSLESLSFYDNKLIKVPQLALQKVPNLKFLDLNKNPIHKIQEGDFKNMLRLKELGINNMGELVSVDRYALDNLPELTKLEATNNPKLSYIHRLAFRSVPALESLMLNNNALNAVYQKTVESLPNLREISIHSNPLRCDCVIHWINSNKTNIRFMEPLSMFCAMPPEYRGQQVKEVLIQDSSEQCLPMISHDTFPNHLNMDIGTTLFLDCRAMAEPEPEIYWVTPIGNKITVETLSDKYKLSSEGTLEIANIQIEDSGRYTCVAQNVQGADTRVATIKVNGTLLDGAQVLKIYVKQTESHSILVSWKVNSNVMTSNLKWSSATMKIDNPHITYTARVPVDVHEYNLTHLQPSTDYEVCLTVSNIHQQTQKSCVNVTTKTAAFALDISDHETSTALAAVMGSMFAVISLASIAIYIAKRFKRKNYHHSLKKYMQKTSSIPLNELYPPLINLWEADSDKDKDGSADTKPTQVDTSRSYYMW
Protein: Ankyrin 2 (A0A5F9ZGS7)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}. Membrane {ECO:0000256|ARBA:ARBA00004370}.
Interaction partners:
Sequence:
MTTMLQKSDSNASFLRAARAGNLDKVVEYLKGGIDINTCNQNGLNALHLAAKEGHVGLVQELLGRGSSVDSATKKGNTALHIASLAGQAEVVKVLVKEGANINAQSQNGFTPLYMAAQENHIDVVKYLLENGANQSTATEDGFTPLAVALQQGHNQAVAILLENDTKGKVRLPALHIAARKDDTKSAALLLQNDHNADVQSKMMVNRTTESGFTPLHIAAHYGNVNVATLLLNRGAAVDFTARNGITPLHVASKRGNTNMVKLLLDRGGQIDAKTRDGLTPLHCAARSGHDQVVELLLERGAPLLARTKNGLSPLHMAAQGDHVECVKHLLQHKAPVDDVTLDYLTALHVAAHCGHYRVTKLLLDKRANPNARALNGFTPLHIACKKNRIKVMELLVKYGASIQAITESGLTPIHVAAFMGHLNIVLLLLQNGASPDVTNIRGETALHMAARAGQVEVVRCLLRNGALVDARAREEQTPLHIASRLGKTEIVQLLLQHMAHPDAATTNGYTPLHISAREGQVDVASVLLEAGAAHSLATKKGFTPLHVAAKYGSLDVAKLLLQRRAAADSAGKNGLTPLHVAAHYDNQKVALLLLEKGASPHATAKNGYTPLHIAAKKNQMQIASTLLNYGAETNIVTKQGVTPLHLASQEGHTDMVTLLLDKGANIHMSTKSGLTSLHLAAQEDKVNVADILTKHGADQDAHTKLGYTPLIVACHYGNVKMVNFLLKQGANVNAKTKNGYTPLHQAAQQGHTHIINVLLQHGAKPNATTANGNTALAIAKRLGYISVVDTLKVVTEEVTTTTTTITEKHKLNVPETMTEVLDVSDEEGDDTMTGDGGEYLRPEDLKELGDDSLPSSQFLDGMNYLRYSLEGGRSDSLRSFSSDRSHTLSHASYLRDSAVMDDSVVIPSHQVSTLAKEAERNSYRLSWGTENLDNVALSSSPIHSGFLVSFMVDARGGAMRGCRHNGLRIIIPPRKCTAPTRVTCRLVKRHRLATMPPMVEGEGLASRLIEVGPSGAQFLGKLHLPTAPPPLNEGESLVSRILQLGPPGTKFLGPVIVEIPHFAALRGKERELVVLRSENGDSWKEHFCDYTEDELNEILNGMDEVLDSPEDLEKKRICRIITRDFPQYFAVVSRIKQDSNLIGPEGGVLSSTVVPQVQAVFPEGALTKRIRVGLQAQPMHSELVKKILGNKATFSPIVTLEPRRRKFHKPITMTIPVPKASSDVMLNGFGGDAPTLRLLCSITGGTTPAQWEDITGTTPLTFVNECVSFTTNVSARFWLIDCRQIQESVTFASQVYREIICVPYMAKFVVFAKSHDPIEARLRCFCMTDDKVDKTLEQQENFAEVARSRDVEVLEGKPIYVDCFGNLVPLTKSGQHHIFSFFAFKENRLPLFVKVRDTTQEPCGRLSFMKEPKSTRGLVHQAICNLNITLPIYTKESESDQEQEEEIDMTSEKNPQDEQERIEERLAYIADHLGFSWTELARELDFTEEQIHQIRIENPNSLQDQSHALLKYWLERDGKHATDTNLVECLTKINRMDIVHLMETNTEPLQERISHSYAEIEQTITLDHSEGFSVLQEELCTAQHKQKEEQAVSKESETCDHPPIVSEEDISVGYSTFQDGVPKTEGDSSATALFPQTHKEQVQQDFSGKMQDLPEESSLEYQQEYFVTTPGTETSETQKAMIVPSSPSKTPEEVSTPAEEEKLYLQTPTSSERGGSPIIQEPEEPSEHREESSPRKTSLVIVESADNQPETCERLDEDAAFEKELTEELGELEASSDEEAMVTTRVVRRRVIIQGDDMPEIPPETVTEEEYIDEHGHTVVKKDNNE
Protein: Iron-sulfur cluster assembly 2 homolog, mitochondrial (HESB-like domain-containing protein 1) (Q86U28)
Organism: Homo sapiens (Human)
Function: Involved in the maturation of mitochondrial 4Fe-4S proteins functioning late in the iron-sulfur cluster assembly pathway. May be involved in the binding of an intermediate of Fe/S cluster assembly.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:22323289}.
Interaction partners:
- Iron-sulfur cluster assembly factor IBA57, mitochondrial
- Iron-sulfur cluster assembly 1 homolog, mitochondrial
- Iron-sulfur cluster assembly enzyme ISCU
- Glutaredoxin-related protein 5, mitochondrial
- NFU1 iron-sulfur cluster scaffold homolog, mitochondrial
- Cysteine desulfurase
- Ferredoxin-2, mitochondrial
- Lipoyl synthase, mitochondrial
- BolA-like protein 3
- Frataxin, mitochondrial
Sequence:
MAAAWGSSLTAATQRAVTPWPRGRLLTASLGPQARREASSSSPEAGEGQIRLTDSCVQRLLEITEGSEFLRLQVEGGGCSGFQYKFSLDTVINPDDRVFEQGGARVVVDSDSLAFVKGAQVDFSQELIRSSFQVLNNPQAQQGCSCGSSFSIKL
Protein: Accessory Sec system protein Asp3 (Accessory secretory protein Asp3) (Orf3) (Q9AET7)
Organism: Streptococcus gordonii
Function: Part of the accessory SecA2/SecY2 system specifically required to export GspB, a serine-rich repeat cell wall protein encoded upstream in the same operon.
Interaction partners:
Sequence:
MKIQKHKEIYWGELRGASISKTRKDFTYLYGSTIIFHSPDQVYFENKLIASGQTIHEWSSSWNYQGDRQVPSLPLLKRGRSYSLTRDMTSYPSESVFLKLIFFDRYNREVSNHVERSDKMTFTYPEEAYSYKVQLLSAGVESFEFHCLRIEEILEESNG
Protein: Premelanosome protein a precursor (Silver homolog (Mouse) a) (Q1ECY0)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MWTSLIFLILSLASGALSQSRTRFARYRSWNSQMYPVWRDGDPRYRDCWKGGEVTIEVRSDSPTLTGAKASFNIDVRFPQNQTVLPDGQVVWARNCTVNGTSYTMGQSVYPESSIPQDWSGVFPDRTPFNRTSNKKPRFIYVWKTWGKYWQVADGPSSLLSIDTNSVPLGSYSMEVVIYHCRGKDKFIPLGYVSTQFSITDQIPFAVTLSQVGDINQGDQNFIQNRAVAFSINLHDPSSYLSSSDITFNWDFGDNSGTLISRETTVTHTYLTPGSFRPQVILMAAISTGCPVNPTPAVTVDPPAPVTDEGTALDTIVVAVSPQPVDVIPNAEEGVVANATVVANDLAVAETDPVDPADTVDTTDAVAEADNTAVVEGTVATEAELAAEAENTATDALATPAVIEAEAAAEAENTATDALATPAVIEAEAAAEAENTATDALATPAVIEAEAAAEAENTATDALATPAVIEAEPAAEAENTATDALATPAVIEAEPAAEAENTATDALATPAVTEAEPAVEAPAAEIDLAATVLPEAAAAAVDTTSVQTALEPVAPTGDAVVANVAEDTVIEAAAEADDAANAITGVTSIPEAAVTELEAELVAGTEATQAALIIAKRQAPEMPAEASCMVYRYGSFSTTLTVVQGIESVEIVEVNNVVMLATELEQNAVDLTVTCQGSLPNQVCTVVSDADCISPVQTQCNDVTPTPECQIVLRQFFNNSGTFCINVSLTNDVSLAVTSARLNVAIDTNSSRNTAGATLGVLFFVCALAAIAFTYKRFKEYHPLREESEGSGFASGISAVPSMLWSFLNRRSTAESRPLLLGRVV
Protein: High-affinity fructose transporter ght6 (Hexose transporter 6) (Meiotic expression up-regulated protein 12) (O74849)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: High-affinity fructose transporter.
Subcellular location: Membrane; Multi-pass membrane protein.
Interaction partners:
- SNF1-like protein kinase ssp2
- Uncharacterized transporter C794.04c
- Putative uncharacterized transmembrane protein C1235.18
Sequence:
MAKILTIVMLVFVSMAGWMFGADTGSIGGITNMRDFQSRYADRYDPVTDTYSYSSARQGLLVGMVNTGTTVGCLLSSPLGDRFGKRKCIMGWTLVYITGVIVQLTTIPSWVQMMVAKIWTGLGIGALSVIAPGYQSESSPPHIRGAIVTTYQLFITLGIFIAACINMGTHKYTTHPEAQWRVPIGINLLWGILMFFGMLFLPESPRYLAVKGRNEECMKILTRNAGLPADHPIMQKEYNAIQADVEAELAGGPCSWPQIFSNEIRYRTLLGMGVMAFQQLTGNNYFFYYGTQVFRGTGLNSPFLAALILDAVNFGCTFGAIFVLEYFGRRGPLIVGGVWQSICFFIYASVGDRALTRPNGTSNHRAGAVMIVFSCLFIFSFAQTWAPAAYVIVGESYPIRYRSKCAAVATASNWFWNFMISFFTPFISNSIGFKYGYVFAACNLCAAIIIFLFAKETKGLTLEEINQLYLSNIKPWNTGAYQRDREDIKQSDSEKERGPTSKLHEYVEHAPNSYASTHSTESENYPQQVTNPVGL
Protein: PRAME family member 9 (P0DUQ2)
Organism: Homo sapiens (Human)
Function: Substrate-recognition component of a Cul2-RING (CRL2) E3 ubiquitin-protein ligase complex, which mediates ubiquitination of target proteins, leading to their degradation. The CRL2(PRAMEF9) complex mediates ubiquitination and degradation of truncated MSRB1/SEPX1 selenoproteins produced by failed UGA/Sec decoding.
Interaction partners:
Sequence:
MKMSIRTPPRLLELAGRSLLRDQALAMSTLEELPTELFPPLFMEAFSRRRCEALKLMVQAWPFRRLPLRPLIKMPCLEAFQAVLDGLDALLTQGVRPRRWKLQVLDLQDVCENFWMVWSEAMAHGCFLNAKRNKKPVQDCPRMRGRQPLTVFVELWLKNRTLDEYLTYLLLWVKQRKDLLHLCCKKLKILGMPFRNIRSILKMVNLDCIQEVEVNCKWVLPILTQFTPYLGHMRNLQKLVLSHMDVSRYVSPEQKKEIVTQFTTQFLKLRCLQKLYMNSVSFLEGHLDQLLSCLKTSLKVLTITNCVLLESDLKHLSQCPSISQLKTLDLSGIRLTNYSLVPLQILLEKVAATLEYLDLDDCGIIDSQVNAILPALSRCFELNTFSFCGNPICMATLENLLSHTIILKNLCVELYPAPRESYGADGTLCWSRFAQIRAELMNRVRDLRHPKRILFCTDYCPDCGNRSFYDLEADQYCC
Protein: Ubiquitin-like modifier-activating enzyme ATG7 (ATG12-activating enzyme E1 ATG7) (Autophagy-related protein 7) (APG7-like) (Q641Y5)
Organism: Rattus norvegicus (Rat)
Function: E1-like activating enzyme involved in the 2 ubiquitin-like systems required for cytoplasm to vacuole transport (Cvt) and autophagy. Activates ATG12 for its conjugation with ATG5 as well as the ATG8 family proteins for their conjugation with phosphatidylethanolamine. Both systems are needed for the ATG8 association to Cvt vesicles and autophagosomes membranes. Required for autophagic death induced by caspase-8 inhibition. Facilitates LC3-I lipidation with phosphatidylethanolamine to form LC3-II which is found on autophagosomal membranes (By similarity). Required for mitophagy which contributes to regulate mitochondrial quantity and quality by eliminating the mitochondria to a basal level to fulfill cellular energy requirements and preventing excess ROS production. Modulates p53/TP53 activity to regulate cell cycle and survival during metabolic stress. Also plays a key role in the maintenance of axonal homeostasis, the prevention of axonal degeneration, the maintenance of hematopoietic stem cells, the formation of Paneth cell granules, as well as in adipose differentiation (By similarity). Plays a role in regulating the liver clock and glucose metabolism by mediating the autophagic degradation of CRY1 (clock repressor) in a time-dependent manner (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}. Preautophagosomal structure {ECO:0000250}. Note=Also localizes to discrete punctae along the ciliary axoneme and to the base of the ciliary axoneme. {ECO:0000250}.
Interaction partners:
- Autophagy protein 5
- Ubiquitin-like-conjugating enzyme ATG3
- Ubiquitin-like protein ATG12
- Ubiquitin-like-conjugating enzyme ATG10
- Forkhead box protein O1
- Gamma-aminobutyric acid receptor-associated protein
- Microtubule-associated protein 1 light chain 3 alpha
- Gamma-aminobutyric acid receptor-associated protein-like 1
- Gamma-aminobutyric acid receptor-associated protein-like 2
- NAD-dependent protein deacetylase sirtuin-1
Sequence:
MGDPGLSKLQFAPFNSALDVGFWHELTQKKLNEYRLDEAPKDIKGYYYNGDSAGLPTRLTLEFSAFDMSAPTPARCCPAMGTLHNTNTLEAFKTADKKLLLEQSANEIWEAIKSGAALENPMLLNKFLLLTFADLKKYHFYYWFCCPALCLPESIPLIRGPVGLDQRLSPKQIQALEHAYDDLCRTEGVTALPYFLFKYDDDTVLVSLLKHYSDFFQGQRTKLTVGVYDPCNLTQHPGWPLRNFLVLAAHRWSGSFQSVEVLCFRDRTMQGARDVTHSIIFEVKLPEMAFSPDCPKAVGWEKNQKGGMGPRMVNLSGCMDPKRLAESSVDLNLKLMCWRLVPTLDLDKVVSVKCLLLGAGTLGCNVARTLMGWGVRHVTFVDNAKISYSNPVRQPLYEFEDCLGGGKPKALAAAERLQKIFPGVNASGFNMSIPMPGHPVNFSDVTMEQARRDVEQLEELIDSHDVIFLLMDTRESRWLPTVIAASKRKLVINAALGFDTFVVMRHGLKKPKQQGAGDLCPSHLVAPADLGSSLFANIPGYKLGCYFCNDVVAPGDSTRDRTLDQQCTVSRPGLAVIAGALAVELMVSVLQHPEGGYAIASSSDDRMNEPPTSLGLVPHQIRGFLSRFDNVLPVSLAFDKCTACSSKVLDQYEQEGFTFLAKVFNSSHSFLEDLTGLTLLHQETQAAEIWDMSDEETV