wanglab/gogpt-training-data huggingface dataset:
Protein: Small ribosomal subunit protein uS10 (40S ribosomal protein S20) (Q5A389)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Function: Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel.
Subcellular location: Cytoplasm {ECO:0000305|PubMed:35613268}.
Interaction partners:
- Large ribosomal subunit protein eL33
- Large ribosomal subunit protein uL29
- Large ribosomal subunit protein uL6
- Small ribosomal subunit protein eS24
- Small ribosomal subunit protein uS8A
- Large ribosomal subunit protein eL13
- Large ribosomal subunit protein uL3
- Small ribosomal subunit protein RACK1
- Small ribosomal subunit protein uS13
- Small ribosomal subunit protein eS30
Sequence:
MSAPINKEKVEQEAEQQIHKIRITLTSTKVKQLENVSANIIRNAAQYNIVKKGPVRMPTKVLKITTRKTPNGEGSKTWDAYEMRIHKRVIDLQAPASTVKRITQITIEPGVDVEVTIAA
Protein: Zinc finger protein 24 (Retinoic acid suppression protein A) (RSG-A) (Zinc finger and SCAN domain-containing protein 3) (Zinc finger protein 191) (Zinc finger protein KOX17) (P17028)
Organism: Homo sapiens (Human)
Function: Transcription factor required for myelination of differentiated oligodendrocytes. Required for the conversion of oligodendrocytes from the premyelinating to the myelinating state. In the developing central nervous system (CNS), involved in the maintenance in the progenitor stage by promoting the cell cycle. Specifically binds to the 5'-TCAT-3' DNA sequence (By similarity). Has transcription repressor activity in vitro.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00187, ECO:0000269|PubMed:24224020}.
Interaction partners:
- Zinc finger protein 446
- Zinc finger protein 396
- Zinc finger protein 174
- SCAN domain-containing protein 1
- Zinc finger and SCAN domain-containing protein 32
- PiggyBac transposable element-derived protein 1
- Zinc finger and SCAN domain-containing protein 1
- Zinc finger protein with KRAB and SCAN domains 4
- Zinc finger protein 397
- Zinc finger protein 444
Sequence:
MSAQSVEEDSILIIPTPDEEEKILRVKLEEDPDGEEGSSIPWNHLPDPEIFRQRFRQFGYQDSPGPREAVSQLRELCRLWLRPETHTKEQILELVVLEQFVAILPKELQTWVRDHHPENGEEAVTVLEDLESELDDPGQPVSLRRRKREVLVEDMVSQEEAQGLPSSELDAVENQLKWASWELHSLRHCDDDGRTENGALAPKQELPSALESHEVPGTLNMGVPQIFKYGETCFPKGRFERKRNPSRKKQHICDECGKHFSQGSALILHQRIHSGEKPYGCVECGKAFSRSSILVQHQRVHTGEKPYKCLECGKAFSQNSGLINHQRIHTGEKPYECVQCGKSYSQSSNLFRHQRRHNAEKLLNVVKV
Protein: Palmitoyltransferase ZDHHC6 (EC 2.3.1.225) (Stearoyltransferase ZDHHC6) (EC 2.3.1.-) (Zinc finger DHHC domain-containing protein 6) (DHHC-6) (Q9CPV7)
Organism: Mus musculus (Mouse)
Function: Endoplasmic reticulum palmitoyl acyltransferase that mediates palmitoylation of proteins such as AMFR, CALX, ITPR1 and TFRC. Palmitoylates calnexin (CALX), which is required for its association with the ribosome-translocon complex and efficient folding of glycosylated proteins (By similarity). Mediates palmitoylation of AMFR, promoting AMFR distribution to the peripheral endoplasmic reticulum (By similarity). Together with SELENOK, palmitoylates ITPR1 in immune cells, leading to regulate ITPR1 stability and function. Stearoyltransferase that mediates stearoylation of TFRC to inhibit TFRC-mediated activation of the JNK pathway and mitochondrial fragmentation (By similarity).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9H6R6}; Multi-pass membrane protein {ECO:0000255}. Note=When not palmitoylated, accumulates to dot-like structures in the endoplasmic reticulum. {ECO:0000250|UniProtKB:Q9H6R6}.
Interaction partners:
- Selenoprotein K
- Palmitoyltransferase ZDHHC13
Sequence:
MGIFCSVIKFENLQDLRRLCHWGPIIALGVIAICSTMAMIDSVLWYWPLHTTGGSVNFIMLINWTVMILYNYFNAMFAGPGFVPRGWKPEKSQDSMYLQYCKVCQAYKAPRSHHCRKCNRCVMKMDHHCPWINNCCGHQNHASFTLFLLLAPLGCTHAAFIFVMTMYTQLYNRLSFGWNTVKIDMSAARRDPPPIVPFGLAAFAATLFALGLALGTTIAVGMLFFIQIKIILRNKTSIESWIEEKAKDRIQYYQLDEVFIFPYDMGSKWKNFKQVFTWSGVPEGDGLEWPIREGCDQYSLTIEQLKQKADKRVRSVRYKVIEDYNGACCPLNRGVRTFFTSPCTEEPRIRLQKGEFILATRGLRYWLYGDKILDDSFIEGTSRVRGWFPRNCVEKCPCDGDSDPAPEGEKKNR
Protein: Vitamin K epoxide reductase complex subunit 1 (EC 1.17.4.4) (Vitamin K1 2,3-epoxide reductase subunit 1) (Q6TEK4)
Organism: Rattus norvegicus (Rat)
Function: Involved in vitamin K metabolism. Catalytic subunit of the vitamin K epoxide reductase (VKOR) complex which reduces inactive vitamin K 2,3-epoxide to active vitamin K. Vitamin K is required for the gamma-carboxylation of various proteins, including clotting factors, and is required for normal blood coagulation, but also for normal bone development.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:23772386, ECO:0000269|PubMed:23928358}; Multi-pass membrane protein {ECO:0000269|PubMed:23772386, ECO:0000269|PubMed:23928358}.
Interaction partners:
- Vitamin K-dependent gamma-carboxylase
- NAD
- Vitamin K epoxide reductase complex subunit 1-like protein 1
- Solute carrier family 53 member 1
- Vitamin K-dependent protein S
Sequence:
MGTTWRSPGRLRLALCLAGLALSLYALHVKAARARNEDYRALCDVGTAISCSRVFSSRWGRGFGLVEHVLGADSILNQSNSIFGCMFYTIQLLLGCLRGRWASILLILSSLVSVAGSLYLAWILFFVLYDFCIVCITTYAINAGLMLLSFQKVPEHKVKKP
Protein: Tenascin C (Tenascin isoform 2 precursor) (Tenascin isoform X1) (F1QYE2)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Secreted, extracellular space, extracellular matrix {ECO:0000256|ARBA:ARBA00004498}.
Interaction partners:
- Integrin alpha-9
- Integrin beta
- Syndecan 4.
- Integrin, alpha 8
- Integrin beta
- Integrin, alpha V
- Integrin beta
- Integrin beta
- Integrin beta
- Integrin beta
Sequence:
MGMRGLLLASMAVAVLVHLSSAGLVKRVIRHRRESLSPTTENLTLPSPDQPVVFNHVYNINVPSGSLCSVDMDSPGTTEIKPKSEQSDQHIEHTTDGENQIVFTHRINIPKQACGCDNHMPDMKELLNRLEMLEAEVSSLREQCTSGAGCCSAQVTGEVTTKPYCSGRGNYSTDTCSCVCEPGWKGVNCSEPECPNYCQDQGRCEDGKCVCFEGFGGEDCGIELCPVDCGENGECIDGACICAEGFIGEDCSLSNCPSNCLGRGRCVDDECVCDEPWTGFDCSELICPNDCFDRGRCENGTCYCDEGFTGEDCGELTCPQNCNHHGRCVNGQCICNIGYSGEDCSKLTCLNDCSERGHCFNGKCICDPGFEGEDCSLLSCPDNCNGRGHCVNGECICGPGYEGDDCSELSCLNNCHDRGRCVNGKCICKAGFAGEDCSIKTCPHDCHGRGECVDGKCVCHDGFAGEHCGIKTCPHHCHGHGQCVDGKCICHKGFAGEDCSIKTCPNHCHGQGQCIDGKCICHDGFAGEDCSIKTCPNHCHGRGRCVDGKCICHDGFAGEDCNIKTCPNDCHDHGECVDGKCICHAGFTGHDCSELTCPNDCHNRGRCVNGQCVCNIGFTGEDCGTKTCPNNCLDRGFCEDGKCVCFEGYTGEDCSVLTCPADCNDQGQCLNGMCICDLGFTGDDCSEISPPRDLTVTEVDPETVDVAWVNEMLVTEYLITYVPTAPGGLEMEMRVSGEKKTATIRELEPGIEYLISVFAVLNSKMSVPVSARIATHLPEPEGLKFKSVKETSVEVEWDPLNIPFDGWNLIFRNTKEEDGEILNSLAPPETTFEQSGLGPGQEYEVKLEVVKNNTRGPPASKNVVTMIDAPSQVDVRDVTDTTALVTWLQPVAQVDGISVSYGPNTDSSDRNTIELSSIETQYHLAELSPDTEYEVSLMARRGEMSSFPIYETFTTDLDSPKHLKAIEQTDESITLEWRNSRANVLNYRVKYGPLSGGEHGELVFPSGLQDTTQAKITGLRPGTEYGMGVTSIKEERESLPATTNAVTDLDPPKDLQVSETTETTLALVWRRPVAKIDTYSLVFIPADGDKTELKIPGAANTYILTGLNPGMLHTITLTAERGRKMSAPATLSASTDEEKPQVGNITISDVSWDSFSMSWDLDRGEVEGFLIEVSDPDGLSDGQNHTLSGQEFSLAVTDLSPSTFYRVTLYGLYKGELLDPVFAEAITEAEPEVEHITVSDITPHSFKVTWTAPEAVFDSFALKVLDSSGLGRPHQISVSGDKRTEAVTGLNEDTDYEIELFGIILGRKFQPIFTVARTGLGTPKGIRFSDVTDTSATVHWTMPHTRVDNYRVIYVPIQGGSPLTLRVDGGESQAMLSNLTPGVTYQVTVIAVKGLEESEPGSERVTTALDKPRGLTAVNISDTEALLLWQPSIATVDGYVITYSADSVAPVMERVSGNTVEFEMSSLTPATLYTVKVYAFRDTAKSAATSTDFTTDVDAPQNLAASNIQTETAMLTWKPPRADISGYILSFESADGVVKEVVLSPTATFYSMSQLTASTEYTVKLQAIAGPKRSRVISTVFLTIGVLYKHPKDCSQALLNGDTTSGLYTIYLRGDESQPLQVYCDMTTDGGGWIVFVRRQSGKVEFFRNWKNYTAGFGDLNDEFWLGLSNLHKITSFGQYELRVDLRDKGESAYAQYDKFSISEPRARYKVHVGGYSGTAGDSMTYHHGRPFSTYDNDNDIAVTNCALSYKGAFWYKNCHRVNIMGRYGDNSHSKGVNWFHWKGHEHSVEFAEMKIRPANFRNFEGRKKRS
Protein: Colicin-E9 (EC 3.1.-.-) (P09883)
Organism: Escherichia coli
Function: This plasmid-coded bactericidal protein is an endonuclease active on both single- and double-stranded DNA but with undefined specificity.
Interaction partners:
Sequence:
MSGGDGRGHNTGAHSTSGNINGGPTGIGVSGGASDGSGWSSENNPWGGGSGSGIHWGGGSGRGNGGGNGNSGGGSGTGGNLSAVAAPVAFGFPALSTPGAGGLAVSISASELSAAIAGIIAKLKKVNLKFTPFGVVLSSLIPSEIAKDDPNMMSKIVTSLPADDITESPVSSLPLDKATVNVNVRVVDDVKDERQNISVVSGVPMSVPVVDAKPTERPGVFTASIPGAPVLNISVNDSTPAVQTLSPGVTNNTDKDVRPAGFTQGGNTRDAVIRFPKDSGHNAVYVSVSDVLSPDQVKQRQDEENRRQQEWDATHPVEAAERNYERARAELNQANEDVARNQERQAKAVQVYNSRKSELDAANKTLADAIAEIKQFNRFAHDPMAGGHRMWQMAGLKAQRAQTDVNNKQAAFDAAAKEKSDADAALSAAQERRKQKENKEKDAKDKLDKESKRNKPGKATGKGKPVGDKWLDDAGKDSGAPIPDRIADKLRDKEFKSFDDFRKAVWEEVSKDPELSKNLNPSNKSSVSKGYSPFTPKNQQVGGRKVYELHHDKPISQGGEVYDMDNIRVTTPKRHIDIHRGK
Protein: PhosphatidylinositolN-acetylglucosaminyltransferase subunit c, putative (EC 2.4.1.198) (Q38AZ2)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- phosphatidylinositol N-acetylglucosaminyltransferase
- Dolichol phosphate-mannose biosynthesis regulatory protein
- PIG-P domain-containing protein
- N-acetylglucosaminylphosphatidylinositol deacetylase
- GPI-GlcNAc transferase complex PIG-H component conserved domain-containing protein
- N-acetylglucosaminyltransferase, putative
- CDP-diacylglycerol--inositol 3-phosphatidyltransferase
Sequence:
MRNCQPASLRETSAMGEAAQPRGTIGSVSTETATVRDEGRVWRKVLYTRQPYEDNYVDPQQFLQDLRQNVNVATYEYNKVVLDTFVVIQQFSFVVFYLFVFSMMLSGRVDECALMWVNATLFTLAFVFCIVVQRQQAVDRGEIPTPFTHYLMGLCRQGIPLVGVLILLSPVLQTLTVAYSNDTIVTLSSLSMFVHVLLTDYNYLNCYSERYQQNTAVNAATFGIILIASRIQRVFQSGALIMFGILCFTLSPIPRHNLKHVSLRAHVVLTFTICALAIYFLMEVPVFALLYCVVVVVISVVIPFFFVKLHGSMKDQINGPWDEAKPTNSAAAVEWANAGMLQ
Protein: Iroquois-class homeodomain protein IRX-5 (Homeodomain protein IRX-2A) (Homeodomain protein IRXB2) (Iroquois homeobox protein 5) (P78411)
Organism: Homo sapiens (Human)
Function: Establishes the cardiac repolarization gradient by its repressive actions on the KCND2 potassium-channel gene. Required for retinal cone bipolar cell differentiation. May regulate contrast adaptation in the retina and control specific aspects of visual function in circuits of the mammalian retina (By similarity). Could be involved in the regulation of both the cell cycle and apoptosis in prostate cancer cells. Involved in craniofacial and gonadal development. Modulates the migration of progenitor cell populations in branchial arches and gonads by repressing CXCL12.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Iroquois-class homeodomain protein IRX-3
- A-type voltage-gated potassium channel KCND2
- Histone-lysine N-methyltransferase SMYD1
- Heart- and neural crest derivatives-expressed protein 2
Sequence:
MSYPQGYLYQPSASLALYSCPAYSTSVISGPRTDELGRSSSGSAFSPYAGSTAFTAPSPGYNSHLQYGADPAAAAAAAFSSYVGSPYDHTPGMAGSLGYHPYAAPLGSYPYGDPAYRKNATRDATATLKAWLNEHRKNPYPTKGEKIMLAIITKMTLTQVSTWFANARRRLKKENKMTWTPRNRSEDEEEEENIDLEKNDEDEPQKPEDKGDPEGPEAGGAEQKAASGCERLQGPPTPAGKETEGSLSDSDFKEPPSEGRLDALQGPPRTGGPSPAGPAAARLAEDPAPHYPAGAPAPGPHPAAGEVPPGPGGPSVIHSPPPPPPPAVLAKPKLWSLAEIATSSDKVKDGGGGNEGSPCPPCPGPIAGQALGGSRASPAPAPSRSPSAQCPFPGGTVLSRPLYYTAPFYPGYTNYGSFGHLHGHPGPGPGPTTGPGSHFNGLNQTVLNRADALAKDPKMLRSQSQLDLCKDSPYELKKGMSDI
Protein: Down syndrome cell adhesion molecule 3, isoform E (Q7KSE9)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004370}.
Interaction partners:
Sequence:
MSLLEPPCLVLEKALLLGALLLAVLATPLLATSGLRVPTFLLEPAPRLLFGNDTGAQVTCTAHGSPPPLVTWVLRDGSLATQVPGLRKISGNGTLHFPPFLAQYYRTDVHEATYRCRASNEAGTVLSRNVQVHAVVRRQFHVHVENTEVYLGNSALIKCAIPEYVRPYVRVASWHRGEEILLPDLSDVAGRYVVLAASGDLYVRSVRSEDGLMKFSCLVTNTLNGERQRSDAVMLQVKELSKNLAPRTTQKPVMEIHVERGNDVHLPCNIQGNPFPIFTWYRVSDSAALYPIPSSQRVILSRTLLLIKNADERDAGKWICQASNQFGEQRIEIRLSVNSYVSVHILPQVQIVNSGGTANFNCTTTGSAIDAIDWLHNGKPLQANNALTTGRDNIRFLSKSSLLVQNVGRRDRGVYQCLVENQRASAQAMAELKLGDTVPELIYTFIEQNVRPGPLISLKCSASGSPPPQFAWLLDSQPIMDVSLHHRFAIGQFVDMSGDVISHLNISHVRPDDGGLYKCVASNSMGSVQHSARLNVYGPPYVRAIGPIKAVAGEDIIVHCPFAGYPVEQIRWEKAHQELTTSNHYELASVADGGQLVIKNVEPGRDQGIYTCIVRSRAGEEARRDMQLNVNSPPVIEPFKFPKNLQEGGRAQITCAVSSGDMPIYFSWKKDDSSIPSSLQITEKKEEFYSLLVFKDISARHSGKYTCYASNAAAKVNYTAELQVRVAPRWRYEPMDTAIMLGNTISINCEAEGYPIPTITWFKGQGKGSKDFKPLSMRNHSLLLNLATDNDEGYYMCQATNEIGAGLKKTIRINVNEPARFEQSARNISSRRNDPVTLDCHAKGDEPITIGWTQNNGRIDLNNFRFSIAEMKTEKGVDSQLTIGHSDRHDSGVYRCIAENPYGRAEQIIFLAVQERPDTPSHLEIFEVGSRTVKLSWRRPFDGNSPVLSYLVQYQALKYLQSHGSLAAAGGDWNGHVINVSLPSTSISRSYDSDLRESAIVAGLTPATTFLIRMQAINEIERSAYTEAIVLKTQEEAPTEAPSNVQVQTGGESELIVTWQIPPRESWNGELIGYTVNCSEEKQNINFISVVNSSLKSTIVSGWATTKATLRGLRKYSRYAVTIRAMNSFGSGPWSAAIFGTTAEGVPEAAPQNVNCTALSSQSLKISWLEPPLQFHGGIIQGYKILYRPIVHQIDFPAKLEIKRTSNLETYLHTLHKASNYSIRVLAYTATGDGLASHPLFCQTDDDVPDAPAAIKAAALTADSILISWLTPKNRNGIISHYTVYSREAGRKGQAKTHMVRVDENGYPVTFESRSLAENQMYEFWVSASTSVGEGEPTSVIAQATNTRAPARIASFGQVVRKAVGTGLVLECLAVGNPTPRARWLTRDRPVTFSPFYEVTNEGNLKIHRVEGSLSGNYTCTANNLFGSDEIQYQVIAMKPPSAPQIIVQYASADSIRVSWDAPDDGGAPLQGYTISYHTAGESWSITELLPENNAFTISGLKCGNQYIIKMSAHNMVGSGVASEEINVWTKGKASQAPNANELIATNATCVNLKLSSWQNGGCSIHHFSIEHRPLGDIRWTVVTSDISNAEENRENLIFCDFLPAKWYQLRISATNDAGKTTEHYHFSTTNIDGITIPPPSVFPSENDLMNNLINSTNPTSGDWFATLIVVVIITVSIITIALTIKHRRTLCGPIAEGYESRTLPGDYKEDHENRRNQQVYSASPVKTVDKGNESEMYEISPYATFSVNGGRTGAPAKTPTRAVAAQTPLDYTMQFKTFGHPEGENLNATAYPLLPSSGFGHVKSKSSWHKQRYYNTEDESTLSKSMTIVAGSQAGHSKKSNGGRSAKSSAACSGVVAGSESDTSISPSTEFSNMPTYRVPCKSSRSSDGRAVVDMFRPDSSTESNNDQGSPAPERRHNTPRHVLGMGMAMGLGGGGGGGVGGGNGPAEKRSAGQRSRKHGSAAQQPSNQTLERRKCPGSSNSLDSEVDAETAASLAASIAAMAGSGAGADLSGGFRPPAGFHDGREPGDHSDCEREQRALDLEVQRVMESTGDAQLAKMDREELTSLLARYHEKKEQERLEYTIHV
Protein: Anillin (Q9NQW6)
Organism: Homo sapiens (Human)
Function: Required for cytokinesis. Essential for the structural integrity of the cleavage furrow and for completion of cleavage furrow ingression. Plays a role in bleb assembly during metaphase and anaphase of mitosis. May play a significant role in podocyte cell migration.
Subcellular location: Nucleus. Cytoplasm, cytoskeleton. Cytoplasm, cell cortex {ECO:0000269|PubMed:23870127}. Cell projection, bleb {ECO:0000269|PubMed:23870127}. Note=Mainly found in the nucleus during interphase. Colocalizes with cortical F-actin upon nuclear envelope breakdown in mitosis and subsequently concentrates in the area of the prospective contractile ring in anaphase. This pattern persists until telophase, when the protein becomes concentrated in the midbody.
Interaction partners:
- Transforming protein RhoA
- Rac GTPase-activating protein 1
- Protein ECT2
- Kinesin-like protein KIF23
- Protein diaphanous homolog 3
- Kinesin-like protein KIF20A
- Kinesin-like protein KIF11
- Centrosomal protein of 55 kDa
- Targeting protein for Xklp2
- Mitotic checkpoint serine/threonine-protein kinase BUB1
Sequence:
MDPFTEKLLERTRARRENLQRKMAERPTAAPRSMTHAKRARQPLSEASNQQPLSGGEEKSCTKPSPSKKRCSDNTEVEVSNLENKQPVESTSAKSCSPSPVSPQVQPQAADTISDSVAVPASLLGMRRGLNSRLEATAASSVKTRMQKLAEQRRRWDNDDMTDDIPESSLFSPMPSEEKAASPPRPLLSNASATPVGRRGRLANLAATICSWEDDVNHSFAKQNSVQEQPGTACLSKFSSASGASARINSSSVKQEATFCSQRDGDASLNKALSSSADDASLVNASISSSVKATSPVKSTTSITDAKSCEGQNPELLPKTPISPLKTGVSKPIVKSTLSQTVPSKGELSREICLQSQSKDKSTTPGGTGIKPFLERFGERCQEHSKESPARSTPHRTPIITPNTKAIQERLFKQDTSSSTTHLAQQLKQERQKELACLRGRFDKGNIWSAEKGGNSKSKQLETKQETHCQSTPLKKHQGVSKTQSLPVTEKVTENQIPAKNSSTEPKGFTECEMTKSSPLKITLFLEEDKSLKVTSDPKVEQKIEVIREIEMSVDDDDINSSKVINDLFSDVLEEGELDMEKSQEEMDQALAESSEEQEDALNISSMSLLAPLAQTVGVVSPESLVSTPRLELKDTSRSDESPKPGKFQRTRVPRAESGDSLGSEDRDLLYSIDAYRSQRFKETERPSIKQVIVRKEDVTSKLDEKNNAFPCQVNIKQKMQELNNEINMQQTVIYQASQALNCCVDEEHGKGSLEEAEAERLLLIATGKRTLLIDELNKLKNEGPQRKNKASPQSEFMPSKGSVTLSEIRLPLKADFVCSTVQKPDAANYYYLIILKAGAENMVATPLASTSNSLNGDALTFTTTFTLQDVSNDFEINIEVYSLVQKKDPSGLDKKKKTSKSKAITPKRLLTSITTKSNIHSSVMASPGGLSAVRTSNFALVGSYTLSLSSVGNTKFVLDKVPFLSSLEGHIYLKIKCQVNSSVEERGFLTIFEDVSGFGAWHRRWCVLSGNCISYWTYPDDEKRKNPIGRINLANCTSRQIEPANREFCARRNTFELITVRPQREDDRETLVSQCRDTLCVTKNWLSADTKEERDLWMQKLNQVLVDIRLWQPDACYKPIGKP
Protein: MIP04261p (Mitochondrial morphology and cristae structure 1) (Q9VIB2)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- Coiled-coil-helix-coiled-coil-helix domain containing 2, isoform A
- IP10175p
- Integral membrane protein 2
- Uncharacterized protein
Sequence:
MLLARLNHVLSGRPMRLLGQSGCPRLWSSAHAQMNSNSLRTPSLAQGKSVIPKRNMQELGMRKYSRESRDRDRSQLESRTRGPSLKERMMGPPSENAYSMGKGAAAGAALMGLVGLCYYGLGLANQPSIYDHSMVWPQYVRDRIHATYAYFGASCGVTAASAVAFFQSDAMMALMTRSGWVASLVTLGLVMLSGSIAQGLEYQPGFGAKQLAWLVHCAVLGAVLAPMCLLGGPILTKALLYTSGIVGALSTVAACAPSEKFLHMGGPLAIGLGVVFASSLASMWLPPTTAVGAGLASMSLYGGLILFSGFLLYDTQRIVKSAELYPQYSKFPYDPINHALAIYMDALNIFIRIAIILAGDQKRKN
Protein: AT08349p (Q8T4A1)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MLILEKPREKQESGLFSSLYSFISSEGQREPTYEEQDFIKLGRKCIKECQLDQMLQESKFVQLESLQELLKCVLALLKAPQGHKSIGLPYAEDQTVFWMEFLVKIVVHNRDRMIPLWPAVRDQMYLLLMGSASCGYDYLLNRCIVAVLKLAIYLMRNEELCPIVLQSLKMLLMLKPALLLRISKQISIGIYELLKTSAQNIHSEQDWQIIFNLLECVGAGAVPPNYDDAQLPLPPNGSAKSDGAISGEEDATAVPERGYTSDSEITKASAAPAVSSPSAENWILVNNKDSELTTASRPQSPPSLSAPPVNTLVYNCQLLDHAPFALFKCWDSLAFIVRSVAHITPYNFEACVRCIRIFVEACRDGGIRQRRKLESAAKQKSSKKRSERKPGMASSASSSNLTLLTGDPSDNQINGNAAEQEDLAQRYEQLSIQLLDLMYTLYTRTAQIFRWWAEEGCTVPQSAALWSPGWCPLLQGIARLAMDRRREVRTHAISCLQQRALLVHDLQTLSGTEWCSCFHQVLFPLLNELLPESNAAGQLDAALLEESRIRTATIMSKVFLQHLTTLIELGNAFNELWLDILDYIERFMKVGSDTLSEQMQEILKNMLLVMHSVRVFHNQDGSLQQALWELTWRRIGEFLPNLKEELFHDEADSITPAVSLDYTQIRFAHSTGTTDYSLSLPLYGYSPKISSISASKCDTLPATQRKKPWAKLRSKLKLLKKVGKKN
Protein: Chlorophyll a-b binding protein CP26, chloroplastic (LHCB5) (LHCIIc) (Light-harvesting complex II protein 5) (Q9XF89)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: The light-harvesting complex (LHC) functions as a light receptor, it captures and delivers excitation energy to photosystems with which it is closely associated.
Subcellular location: Plastid, chloroplast thylakoid membrane {ECO:0000269|PubMed:16551629}; Multi-pass membrane protein.
Interaction partners:
- Oxygen-evolving enhancer protein 1-1, chloroplastic
- Photosystem II CP43 reaction center protein
- Photosystem II CP47 reaction center protein
- Photosystem II protein D1
- Expressed protein
- Chlorophyll a-b binding protein CP29.1, chloroplastic
- Photosystem II D2 protein
- Cytochrome b559 subunit alpha
- Photosystem II reaction center protein H
- Photosystem II reaction center protein Z
Sequence:
MASLGVSEMLGTPLNFRAVSRSSAPLASSPSTFKTVALFSKKKPAPAKSKAVSETSDELAKWYGPDRRIFLPDGLLDRSEIPEYLNGEVAGDYGYDPFGLGKKPENFAKYQAFELIHARWAMLGAAGFIIPEALNKYGANCGPEAVWFKTGALLLDGNTLNYFGKNIPINLVLAVVAEVVLLGGAEYYRITNGLDFEDKLHPGGPFDPLGLAKDPEQGALLKVKEIKNGRLAMFAMLGFFIQAYVTGEGPVENLAKHLSDPFGNNLLTVIAGTAERAPTL
Protein: DNA-directed RNA polymerase subunit alpha (PEP) (EC 2.7.7.6) (Plastid-encoded RNA polymerase subunit alpha) (RNA polymerase subunit alpha) (P0C498)
Organism: Oryza sativa (Rice)
Function: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
Subcellular location: Plastid, chloroplast.
Interaction partners:
Sequence:
MVREEVAGSTQTLQWKCVESRVDSKRLYYGRFILSPLRKGQADTVGIALRRALLGETEGTCITHAKFGSVPHEYSTIAGIEESVQEILLNLKEIVLRSNLYGVRTASICVKGPRYITAQDIILPPSVEIVDTAQPIANLTEPTDFRIELRIKRDRGYHTEVRKNTQDGSYPIDAVSMPVRNVNYSIFACGNGNAKYEILFLEIWTNGSLTPKEALYEASRNLIDLFLPFLHTEEEGTRFQENKNRFTSPLLSFQKRLTNLKKNKKRIPLNCIFIDQLELPSRTYNCLKRANIHTLLDLLSKTEEDLMRIDSFRMQDGKQIWDTLEKHLPMDLPKNKF
Protein: Chlorophyll a-b binding protein 6, chloroplastic (LHCI-730) (LHCII type III CAB-6) (Light-harvesting complex protein Lhca1) (Q01667)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: The light-harvesting complex (LHC) functions as a light receptor, it captures and delivers excitation energy to photosystems with which it is closely associated.
Subcellular location: Plastid, chloroplast thylakoid membrane {ECO:0000269|PubMed:10818090}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Photosystem I reaction center subunit psaK, chloroplastic
- Photosystem I P700 chlorophyll a apoprotein A1
- Photosystem I reaction center subunit VI-2, chloroplastic
- Photosystem I chlorophyll a/b-binding protein 3-1, chloroplastic
- Photosystem I reaction center subunit IX
- Photosystem I reaction center subunit III, chloroplastic
- Chlorophyll a-b binding protein 4, chloroplastic
- Photosystem I reaction center subunit V, chloroplastic
- Photosystem I reaction center subunit XI, chloroplastic
- Photosystem I chlorophyll a/b-binding protein 5, chloroplastic
Sequence:
MASNSLMSCGIAAVYPSLLSSSKSKFVSAGVPLPNAGNVGRIRMAAHWMPGEPRPAYLDGSAPGDFGFDPLGLGEVPANLERYKESELIHCRWAMLAVPGILVPEALGYGNWVKAQEWAALPGGQATYLGNPVPWGTLPTILAIEFLAIAFVEHQRSMEKDPEKKKYPGGAFDPLGYSKDPKKLEELKVKEIKNGRLALLAFVGFCVQQSAYPGTGPLENLATHLADPWHNNIGDIVIPFN
Protein: Asc-type amino acid transporter 1 (Asc-1) (D-serine transporter) (Solute carrier family 7 member 10) (P63115)
Organism: Mus musculus (Mouse)
Function: Associates with SLC3A2/4F2hc to form a functional heterodimeric complex that translocates small neutral L- and D-amino acids across the plasma membrane. Preferentially mediates exchange transport, but can also operate via facilitated diffusion (By similarity). Acts as a major transporter for glycine, L- and D-serine in the central nervous system. At the spinal cord and brainstem regulates glycine metabolism and glycinergic inhibitory neurotransmission by providing for glycine de novo synthesis from L-serine and glycine recycling from astrocytes to glycinergic motor neurons. At Schaffer collateral-CA1 synapses mediates D-serine and glycine release that modulates post-synaptic activation of NMDA receptors and excitatory glutamatergic transmission (By similarity). May regulate D-serine release from mesenchymal progenitors located in developing subcutaneous adipose tissue, favoring white adipocyte over thermogenic beige adipocyte lineage commitment.
Subcellular location: Cell membrane {ECO:0000269|PubMed:33707431, ECO:0000269|PubMed:34749773}; Multi-pass membrane protein {ECO:0000255}. Note=Colocalizes with OLIG2 in astrocytic processes (PubMed:34749773). Localizes to the plasma membrane in mature adipocytes and to intracellular structures in preadipocytes (PubMed:33707431). {ECO:0000269|PubMed:33707431, ECO:0000269|PubMed:34749773}.
Interaction partners:
- Amino acid transporter heavy chain SLC3A2
Sequence:
MRRDSDMASHIQQPGGHGNPGPAPSPSPGPGPGPGASERVALKKEIGLVSACTIIIGNIIGSGIFISPKGVLEHSGSVGLALFVWVLGGGVTALGSLCYAELGVAIPKSGGDYAYVTEIFGGLAGFLLLWSAVLIMYPTSLAVISMTFSNYVLQPVFPNCIPPATASRVLSMACLMLLTWVNSSSVRWATRIQVIFTGGKLLALSLIITVGFVQIFQGHFEELRPTNAFAFWMTPSVGHLALAFLQGSFAFSGWNFLNYVTEELVDPRKNLPRAIFISIPLVTFVYTFTNVAYFTAMSPQELLSSNAVAVTFGEKLLGYFSWVMPVSVALSTFGGINGYLFTSSRLCFSGAREGHLPSFLAMIHVRRCTPIPALLVCCGATAVIMLVGDTYTLINYVSFINYLCYGVTILGLLVLRWRRPALHRPIKVNLLVPVVYLVFWAFLLVFSFISEPMVCGVGIIIILTGVPIFFLGVFWRSKPKCVHRFTESMTRWGQELCFVVYPQGSLEEEENGPMGQPSPLPITDKPLKTQ
Protein: Carboxyl-terminal protease (P75023)
Organism: Synechocystis sp. (strain ATCC 27184 / PCC 6803 / Kazusa)
Interaction partners:
- Processing protease
- Processing protease
- Processing protease
- Processing protease
Sequence:
MSPHLLCLRPLVAALVFGLGLGTALRPALSAPNVINPDSPTLATPKDKDSGVSDNVTLLENSPKAVVDEVWQLVNQQFVDKDFNHSNWLSKRQELLGRNYQDNAEAYRQIGRILKDLNDPYTRFLSPEEFAILSSQTSGEASGVGIRVLMDKRSSDLVVVDVMRGTPALKAGIRPGDRIVRINGQPAALMSLEQATEAIQGEIGTELSLQLSRPKSGVFSVTLKRENIEIDSVTYNVKEEGELRVGYIRLDEFSSHSAEQMEKAITELNKSRISGYVLDLRGNPGGLLLSSIDIARLWLNRGEIVSTIDRRGGDRHFSANGRSLTDLPLVVLVNERSASASEILAGALKEQGRATVVGTATYGKGTVQSVNTLSDGSGLAVTIARYYPPSGTDINRKGISPDIHLDISNDTKLQFRNDPELMATEIDPQYQRAISVLRQHRHSLGLPPAKDLGIGLLEPSQL