wanglab/gogpt-training-data huggingface dataset:
Protein: Protein kinase domain-containing protein (A0A384LH69)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MKSMVKKLKQSLRSGSLEKRKEKEKDIQEEKWFLDNGSIFLKELIADCNGKSIPIRNFSSDQILKATSNFGSSCFVTAEGFYVWYKGIIEDRSYMIKRFSEYKVTQYRVAEVYNEIVLSARMSNHNNFLKLIGFCLEFSLPVLVFEYAEHGVLNHRGGVIVNGEEVILPLSLRLKIGKEIANAVTYLHMAFPKILIHRHIKPRNVFLDENWTPKLSDFSISINLPEGKSRIEVECVQGTIGYLDPVYYTTKMVTEYTDVYSFGVFLMVILTGKPALASTSSDGDYKHIASYVKGFHENGQLDGVIDPKVMEDITSAQKVHVEACVVLALRCCELRDENRPKMIQIAKELKQIETLFRRS
Protein: ERCC excision repair 1, endonuclease non-catalytic subunit (K7ER60)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MDPGKDKEGVPQPSGPPARKKFVIPLDEDEVPPGVAKPLFRSTQSLPTVDTSAQAAPQTYAEYAISQPLEGAGATCPTGSEPLAGETPNQALKPGAKSNSIIVSPRQRGNPVLKFVRNVPWEFGDVIPDYVLGQSTCALFLSLRYHNLHPDYIHGRLQSLGKNFALRVLLVQVDVKDPQQALKELAKMCILADCTLILAWRPGGCLMSCTSPS
Protein: Protein GUCD1 (Guanylyl cyclase domain-containing protein 1) (Protein LLN4) (Q96NT3)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MRTEAEAAGPPLEPGDFVQLPVPVIQQLYHWDCGLACSRMVLRYLGQLDDSEFERALQKLQLTRSIWTIDLAYLMHHFGVRHRFCTQTLGVDKGYKNQSFYRKHFDTEETRVNQLFAQAKACKVLVEKCTVSVKDIQAHLAQGHVAIVLVNSGVLHCDLCSSPVKYCCFTPSGHHCFCRTPDYQGHFIVLRGYNRATGCIFYNNPAYADPGMCSTSISNFEEARTSYGTDEDILFVYLDS
Protein: Enhancer of split m5 protein (E(spl)m5) (P13096)
Organism: Drosophila melanogaster (Fruit fly)
Function: Participates in the control of cell fate choice by uncommitted neuroectodermal cells in the embryo. Transcriptional repressor. Binds DNA on N-box motifs: 5'-CACNAG-3'.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Enhancer of split m4 protein
- Bearded
- Sphingosine-1-phosphate lyase
- Enhancer of split m8 protein
- Protein groucho
- Enhancer of split m7 protein
- Enhancer of split mdelta protein
Sequence:
MAPQSNNSTTFVSKTQHYLKVKKPLLERQRRARMNKCLDTLKTLVAEFQGDDAILRMDKAEMLEAALVFMRKQVVKQQAPVSPLPMDSFKNGYMNAVSEISRVMACTPAMSVDVGKTVMTHLGVEFQRMLQADQVQTSVTTSTPRPLSPASSGYHSDNEDSQSAASPKPVEETMWRPW
Protein: DNA 5'-3' helicase (EC 5.6.2.3) (A0A1D8PQH0)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- DNA 3'-5' helicase
- General transcription and DNA repair factor IIH
- RNA polymerase II transcription factor B subunit 2
- General transcription and DNA repair factor IIH subunit TFB4
- RNA polymerase II transcription factor B subunit 3
- TFIIH/NER complex subunit
- Transcription initiation factor IIE subunit beta
- TFIIH complex kinase subunit
- Transcription factor TFIIE subunit
- [RNA-polymerase]-subunit kinase
Sequence:
MKFFIDDLPVLFPYPRIYPEQYSYMCDIKKTLDVGGNCILEMPSGTGKTVSLLSLTVAYQMHYPEHRKIVYCSRTMSEIEKALIELHKLMEFRANELGEVEDFRGLGLTSRKNLCLHPTISKERKGVVVDEKCRRITNGQLKEKIEKGVPTEDSLCSFHEKLYDLEPHNLVPPGVYSFDALIKYCKEEGTCPYFTVRRMIPFCNIIIYSYHYLLDPKIAERVSRELSKDSIVIFDEAHNIDNVCIESLSLDLTDETLKKASRGANKLGEAIEDMKAQDSEKLQNEYEQLVEGLRQAEIARDQELFMANPVLPQDLLDEAIPGNIRKGEHFIAFLKRFIEYLKTRMKVLHVISETPTSFLQHLKELTYIERKPLRFCSERLSLLVRTLEVTEIDDFNALKDIATFATLVSTYDSGFQLILEPYETEGSTVPNPILHFTCLDASIAIKPVFDRFSSVIITSGTISPLDMYPKMLKFETVIQESYAMTLARRSFLPMIVTKGSDQVSISSRFEIRNDPSVVRNYGSLLIEFAKITPDGMVVFFPSYLYMESIISMWQSMGVLDEVWKHKLILVETPDAQETSLALETYRKACSNGRGAVLLSVARGKVSEGIDFDHHYGRTVLMIGIPFQYTESRILKARLEFMRDHFQIKENDFLSFDAMRHAAQCLGRVLRGKDDYGIMVLADRRFARKKNQLPKWIAQALNDSDTNLSTDMALATAKKFLRSLAQPTNPKDSEGVSIWNIEQLQEYQQQFQKDEMDIDEEDLDLL
Protein: Transposon Ty1-OL Gag-Pol polyprotein (Gag-Pol-p199) (TY1A-TY1B) (Transposon Ty1 TYA-TYB polyprotein) (p190) [Cleaved into: Capsid protein (CA) (Gag-p45) (p54); Ty1 protease (PR) (EC 3.4.23.-) (Pol-p20) (p23); Integrase (IN) (Pol-p71) (p84) (p90); Reverse transcriptase/ribonuclease H (RT) (RT-RH) (EC 2.7.7.49) (EC 2.7.7.7) (EC 3.1.26.4) (Pol-p63) (p60)] (Q12273)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Capsid protein (CA) is the structural component of the virus-like particle (VLP), forming the shell that encapsulates the retrotransposons dimeric RNA genome. The particles are assembled from trimer-clustered units and there are holes in the capsid shells that allow for the diffusion of macromolecules. CA has also nucleocapsid-like chaperone activity, promoting primer tRNA(i)-Met annealing to the multipartite primer-binding site (PBS), dimerization of Ty1 RNA and initiation of reverse transcription (By similarity).
Subcellular location: Cytoplasm. Nucleus {ECO:0000250}.
Interaction partners:
Sequence:
MESQQLSNYPQISHGSACASVTSKEVHTNQDPLDVSASKTEECEKASTKANSQQTTTPASSAVPENPHHASPQPASVPPPQNGPYPQQCMMTQNQANPSGWSFYGHPSMIPYTPYQMSPMYFPPGPQSQFPQYPSSVGTPLSTPSPESGNTFTDSSSADSDMTSTKKYVRPPPMLTSPNDFPNWVKTYIKFLQNSNLGGIIPTVNGKPVRQITDDELTFLYNTFQIFAPSQFLPTWVKDILSVDYTDIMKILSKSIEKMQSDTQEANDIVTLANLQYNGSTPADAFETKVTNIINRLNNNGIHINNKVACQLIMRGLSGEYKFLRYTRHRHLNMTVAELFLDIHAIYEEQQGSRNSKPNYRRNLSDEKNDSRSYTNTTKPKVIARNPQKTNNSKSKTARAHNVSTSNNSPSTDNDSISKSTTEPIQLNNKHDLHLGQELTESTVNHTNHSDDELPGHLLLDSGASRTLIRSAHHIHSASSNPDINVVDAQKRNIPINAIGDLQFHFQDNTKTSIKVLHTPNIAYDLLSLNELAAVDITACFTKNVLERSDGTVLAPIVKYGDFYWVSKKYLLPSNISVPTINNVHTSESTRKYPYPFIHRMLAHANAQTIRYSLKNNTITYFNESDVDWSSAIDYQCPDCLIGKSTKHRHIKGSRLKYQNSYEPFQYLHTDIFGPVHNLPKSAPSYFISFTDETTKFRWVYPLHDRREDSILDVFTTILAFIKNQFQASVLVIQMDRGSEYTNRTLHKFLEKNGITPCYTTTADSRAHGVAERLNRTLLDDCRTQLQCSGLPNHLWFSAIEFSTIVRNSLASPKSKKSARQHAGLAGLDISTLLPFGQPVIVNDHNPNSKIHPRGIPGYALHPSRNSYGYIIYLPSLKKTVDTTNYVILQGKESRLDQFNYDALTFDEDLNRLTASYQSFIASNEIQQSDDLNIESDHDFQSDIELHPEQPRNVLSKAVSPTDSTPPSTHTEDSKRVSKTNIRAPREVDPNISESNILPSKKRSSTPQISNIESTGSGGMHKLNVPLLAPMSQSNTHESSHASKSKDFRHSDSYSENETNHTNVPISSTGGTNNKTVPQISDQETEKRIIHRSPSIDASPPENNSSHNIVPIKTPTTVSEQNTEESIIADLPLPDLPPESPTEFPDPFKELPPINSHQTNSSLGGIGDSNAYTTINSKKRSLEDNETEIKVSRDTWNTKNMRSLEPPRSKKRIHLIAAVKAVKSIKPIRTTLRYDEAITYNKDIKEKEKYIEAYHKEVNQLLKMKTWDTDEYYDRKEIDPKRVINSMFIFNKKRDGTHKARFVARGDIQHPDTYDSGMQSNTVHHYALMTSLSLALDNNYYITQLDISSAYLYADIKEELYIRPPPHLGMNDKLIRLKKSLYGLKQSGANWYETIKSYLIKQCGMEEVRGWSCVFKNSQVTICLFVDDMILFSKDLNANKKIITTLKKQYDTKIINLGESDNEIQYDILGLEIKYQRGKYMKLGMENSLTEKIPKLNVPLNPKGRKLSAPGQPGLYIDQDELEIDEDEYKEKVHEMQKLIGLASYVGYKFRFDLLYYINTLAQHILFPSRQVLDMTYELIQFMWDTRDKQLIWHKNKPTEPDNKLVAISDASYGNQPYYKSQIGNIYLLNGKVIGGKSTKASLTCTSTTEAEIHAISESVPLLNNLSYLIQELNKKPIIKGLLTDSRSTISIIKSTNEEKFRNRFFGTKAMRLRDEVSGNNLYVYYIETKKNIADVMTKPLPIKTFKLLTNKWIH
Protein: Collagen type VIII alpha 1 (Collagen, type VIII, alpha 1a precursor) (B7SW26)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Secreted, extracellular space, extracellular matrix {ECO:0000256|ARBA:ARBA00004498}.
Interaction partners:
Sequence:
MAMAAFLVALVQLTFLPLAFGGGYYPHKSHPQQHQPLPQMHMGMGKEMPHMPYPHYRKDLPMHLNKGKDNKGETIPRGEQGVQGQPGAQGPVGPPGPQGPPGPQGNGIQGPPGKPGPPGPPGYPGIGKPGMSGMPGKAGDPGQPGQPGEQGPRGEDGQPGIAGPPGPPGPPGLPGIGKPGGQGLPGQPGNKGEPGHKGFPGLPGLPGPKGDRGIGLPGSQGPKGPVGPPGLRGPAGLPGVGKTGLPGIPGPAGVPGKPGEPGEPGPEGPPGEKGPQGPQGAPGIGSPGEKGLPGQPGTPGHKGLHGPPGLPGKPGLPGFGKPGYPGPKGDRGMGGLPGPQGPKGEKGHMGQPGMMGPPGQTGLPGPSGPIGATGEVGSPGLKGEGGAGGAKGDPGPIGLTGPPGIPGQPGQPGEDGEPGPRGPQGPIGPKGEGGSNGLPGPPGQSGLPGLKGETGPPGPEGPRGPTGIPGLAGPGGLLGPPGPPGPKGEVGPPGQAGQPGEGSPGIQGPVGPPGPPGPNGSPGQPGIQGPPGPPGPPGPAPSPDLMGVLPEMGPALDGVKAGYKKGKYAGEGDMMGANGLEMPAFTAKLTAPFPPVGTPIVLDKLLYNGRQNYNPQTGVFTCDLPGVYYFAYHVHCKGANVWVGLYRNGEPVMYTYDEYKKGFLDQASGSAVIPLQPGDTVYLQLPSDQAAGFYAGQFVHSSFSGFLLYPM
Protein: Ankyrin repeat and SAM domain-containing protein 4B (Harmonin-interacting ankyrin repeat-containing protein) (Harp) (Q8N8V4)
Organism: Homo sapiens (Human)
Function: As part of the intermicrovillar adhesion complex/IMAC plays a role in epithelial brush border differentiation, controlling microvilli organization and length. Plays a role in assembly of the complex. May play a role in cellular response to endoplasmic reticulum stress (By similarity).
Subcellular location: Cell projection, microvillus {ECO:0000269|PubMed:26812018, ECO:0000269|PubMed:32209652}. Note=Localizes at the tip of microvilli (PubMed:26812018, PubMed:32209652). May associate with endoplasmic reticulum membranes (By similarity). {ECO:0000250|UniProtKB:Q8K3X6, ECO:0000269|PubMed:26812018, ECO:0000269|PubMed:32209652}.
Interaction partners:
- Harmonin
- Unconventional myosin-VIIb
- Cadherin-related family member 5
- Cadherin-related family member 2
Sequence:
MSTRYHQAASDSYLELLKEATKRDLNLSDEDGMTPTLLAAYHGNLEALEIICSRGGDPDRCDIWGNTPLHFAASNGHAHCVSFLVNFGANIFALDNDLQTPLDAAASREQNECVALLDKAATAQNIMNPKKVTRLKEQAQKNARRQIKECERLQEKHQNKMAHTYSKEESGTLSSSKGTFSRSSPSNASAPGTFGSLSKGIKDTFKIKFKKNKDTAEQVGKEGRSGQRNVMEVFREEEEDSFSGDFKEKLQLSAEEDGSVHHESILNRPGLGSIVFRRNRISSPEDISDSKREFGFKLPSELLQRQGASEADEGAADEEGEENGLKDDLPWDDDEVEWEEDVVDATPLEVFLLSQHLEEFLPIFKREQIDLEALLLCSDEDLQSIQMQLGPRKKVLNAINRRKQVLQQPGQLVDTSL
Protein: Electroneutral sodium bicarbonate exchanger 1 (Electroneutral Na+-driven Cl-HCO3 exchanger) (Solute carrier family 4 member 8) (k-NBC3) (Q6RVG2)
Organism: Rattus norvegicus (Rat)
Function: Mediates electroneutral sodium- and carbonate-dependent chloride-HCO3(-) exchange with a Na(+):HCO3(-) stoichiometry of 2:1. Plays a major role in pH regulation in neurons. Mediates sodium reabsorption in the renal cortical collecting ducts (By similarity).
Subcellular location: Cell membrane {ECO:0000269|PubMed:18359573, ECO:0000269|PubMed:34584093}; Multi-pass membrane protein {ECO:0000255}. Apical cell membrane {ECO:0000250|UniProtKB:Q2Y0W8}; Multi-pass membrane protein {ECO:0000255}. Basolateral cell membrane {ECO:0000269|PubMed:18359573, ECO:0000269|PubMed:21195699}; Multi-pass membrane protein {ECO:0000255}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000269|PubMed:22102085}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Pendrin
Sequence:
MPAGSNEPDGVLSYQRPDEEAVVDQGGTSTILNIHYEKEELEGHRTLYVGVRMPLGRQSHRHHRTHGQKHRRRGGRGKGASQGEEGLEASAHDTPSQRVQFILGTEEDEEHVPHELFTELDEICMKEGEEAEWKETARWLKFEEDVEDGGERWSKPYVATLSLHSLFELRSCLINGSVLLDMRASSIEEISDLILDQQELLRDLSDSVRVKVREALLKKHHHQNEKKRNNLIPIVRSFAEVGKKQSDPHSMDRDGQTVSPQSAPATNLEVKNGVNCEHSPVDLSKADLHFMKKIPAGAEASNVLVGEVDTLDRPIVAFVRLSPAVLLSGLTEVPIPTRFLFILLGPVGKGQQYHEIGRSMATIMTDEIFHDVAYKAKERDDLLAGIDEFLDQVTVLPPGEWDPSIRIEPPKNVPSQEKRKMPGVPNGNICHVEPEPHGGHSGPELERTGRLFGGLVLDVKRKAPWYWSDYRDALSLQCLASFLFLYCACMSPVITFGGLLGEATEGRISAIESLFGASMTGIAYSLFAGQPLTILGSTGPVLVFEKILFKFCKDYALSYLSLRACIGLWTAFLCIVLVATDASSLVCYITRFTEEAFASLICIIFIYEAIEKLIHLAETYPIHMHSQLDHLSLYYCRCALPENPNNHTLQYWKEHSIPTADVNWANLTVSECQEMHGEFIGSACGHHGPYTPDVLFWSCILFFATFIVSSTLKTFKTSRYFPTRVRSTVSDFAVFLTIFTMVILDFLIGVPSPKLQVPSVFKPTRDDRGWFISPIGPNPWWTVIAAIIPALLCTILIFMDQQITAVIINRKEHKLKKGCGYHLDLLVVAIMLGVCSLMGLPWFVAATVLSITHVNSLKLESECSAPGEQPKFLGIREQRVTGLMIFVLMGCSVFMTAVLKFIPMPVLYGVFLYMGVSSLQGIQFFDRLKLFGMPAKHQPDFIYLRHVPLRKVHLFTLVQLTCLVLLWVIKASPAAIVFPMMVLALVFVRKVMDLCFSKRELSWLDDLMPESKKKKLDDAKKKEEEEEAEKMLDIGGDKFPLESRKLLSSPGKNNSFRCDPSEINISDEMPKTTVWKALSINSGNTKEKSPFN
Protein: Multidrug resistance protein MdtG (P25744)
Organism: Escherichia coli (strain K12)
Function: Confers resistance to fosfomycin and deoxycholate.
Subcellular location: Cell inner membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Multidrug resistance protein MdtL
- Multidrug resistance protein MdtM
- Multidrug resistance protein D
- Multidrug resistance protein MdtH
- Multidrug resistance protein MdtK
- Multidrug resistance outer membrane protein MdtP
- Multidrug resistance protein MdtB
- Multidrug resistance protein MdtA
Sequence:
MSPCENDTPINWKRNLIVAWLGCFLTGAAFSLVMPFLPLYVEQLGVTGHSALNMWSGIVFSITFLFSAIASPFWGGLADRKGRKLMLLRSALGMGIVMVLMGLAQNIWQFLILRALLGLLGGFVPNANALIATQVPRNKSGWALGTLSTGGVSGALLGPMAGGLLADSYGLRPVFFITASVLILCFFVTLFCIREKFQPVSKKEMLHMREVVTSLKNPKLVLSLFVTTLIIQVATGSIAPILTLYVRELAGNVSNVAFISGMIASVPGVAALLSAPRLGKLGDRIGPEKILITALIFSVLLLIPMSYVQTPLQLGILRFLLGAADGALLPAVQTLLVYNSSNQIAGRIFSYNQSFRDIGNVTGPLMGAAISANYGFRAVFLVTAGVVLFNAVYSWNSLRRRRIPQVSN
Protein: GAS2-like protein 2 (D3ZUE1)
Organism: Rattus norvegicus (Rat)
Function: Involved in the cross-linking of microtubules and microfilaments (By similarity). Regulates microtubule dynamics and stability by interacting with microtubule plus-end tracking proteins, such as MAPRE1, to regulate microtubule growth along actin stress fibers (By similarity). Enhances ADORA2-mediated adenylyl cyclase activation by acting as a scaffold to recruit trimeric G-protein complexes to ADORA2A (By similarity).
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:23994616}. Cell membrane {ECO:0000269|PubMed:23994616}. Cytoplasm, cytoskeleton, stress fiber {ECO:0000250|UniProtKB:Q8NHY3}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000250|UniProtKB:Q8NHY3}. Note=Colocalizes with ADORA2A at neuronal processes (PubMed:23994616). Colocalizes with and tracks the tips of microtubule plus ends (By similarity). {ECO:0000250|UniProtKB:Q8NHY3, ECO:0000269|PubMed:23994616}.
Interaction partners:
Sequence:
MSQHVGHGRKPRTPGPPVRSIRPFKSSEQYLEVMKEDLAEWLRDLYGLDIDAANFLRVLETGLVLCRHANTVTEAALAFLAEAPERVQKIPMPQVGVFCNGAAQPGTFQARDNISNFIQWCRKEMGIQEVLMFETEDLVLRKNVKSVVLCLLELGRRAWRFGVAAPSLVYLEEEIEEELRRDLDLPSPDPPPPVPPARRPCHFHNLDQMVQSLVSHCTCPVQFSMVKISDGKYRVGDSNTLIFIRILRSHVMVRVGGGWDTLGHYLDKHDPCRCTSLSHKPGSFLKPPGPPVQHEVKVQDGPSQPQPLMTISRSQSPLPPVDWKTYTSSSRKLRPPTPSSSGPRSEFPARARTPREMAPFLRSQEKPTLSQRMSSPGPQLSSPCRGPDLQSTLSERRVNRSPGELPRGRTPTSWVPKEADSQGAHTKAPIPQRLQIPETTSKKTPARGPSPPPRSSSLASPHTIWLPDQGASPEISEPMSAQSSSPGKGLTKIPIRLSPARPPTPGRGSLGTEGGGSMQRGSLSSRALAGNLDRSTHGHHSVDVSKDHQKVIQISSGTEDPRSLGTQERKERYTSLPLGRTREPALYDNLKEELVANMKLLEVGAACTQGTRSQAIPRSGVYVPSLGGMWPEPRGPYDKVIQELVQGPPRLLKVDLKAWKVGSECLPRPIVNPGSPKEEQVSRERGTRRKARPSAQGTTVKTTSPARGQDCSTLPVSANLKAPTHSCSDPSSDKAKVCLGKGKRTLRKPQKVPSIYKLKLRPRIRPRRDHRPEKRPSRIPKPLVYPFLGPARTAPGSRLLKATLGGTGGDVNGVGKKEEEKKKETSISLESSIQPSESREPMQLDGTPLPPEEESWV
Protein: F-box/LRR-repeat protein 16 (F-box and leucine-rich repeat protein 16) (Spinal cord injury and regeneration-related protein 1) (Q5MJ12)
Organism: Rattus norvegicus (Rat)
Function: Substrate-recognition component of the SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex.
Interaction partners:
- S-phase kinase-associated protein 1
- Cullin-1
Sequence:
MSSPGIDGDPKPSCLPRNGLVKLPGQPNGLGAASITKGTPAAKNRPCQPPPPPTLPPPSLATPLSRVALAGGPCPPASGPASGPVPGPPVERPPLATDEKILNGLFWYFSACEKCILAQVCKAWRRVLYQPKFWAGLTPVLHAKELYNVLPGGEKEFVNLQGFAARGFEGFCLVGVSDLDICEFIDNYSLSKKGVKAMSLKRSTITDAGLEVMLEQMQGVVRLELSGCNDFTEAGLWSSLSARITSLSVSDCINVADDAIAAISQLLPNLAELSLQAYHVTDTALAYFTARQGHSTHTLRLLSCWEITNHGVVNVVHSLPNLTSLSLSGCSKVTDDGVELVAENLRKLRSLDLSWCPRITDMALEYVACDLHRLEELVLDRCVRITDTGLSYLSTMSSLRSLYLRWCCQVQDFGLKHLLAMRSLRLLSLAGCPLLTTTGLSGLVQLQELEELELTNCPGATPELFKYFSQHLPRCLVIE
Protein: Carbohydrate sulfotransferase 3 (EC 2.8.2.17) (EC 2.8.2.21) (Chondroitin 6-O-sulfotransferase 1) (C6ST-1) (Chondroitin 6-sulfotransferase) (C6ST) (Galactose/N-acetylglucosamine/N-acetylglucosamine 6-O-sulfotransferase 0) (GST-0) (Q7LGC8)
Organism: Homo sapiens (Human)
Function: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the transfer of sulfate to position 6 of the N-acetylgalactosamine (GalNAc) residue of chondroitin. Chondroitin sulfate constitutes the predominant proteoglycan present in cartilage and is distributed on the surfaces of many cells and extracellular matrices. Catalyzes with a lower efficiency the sulfation of Gal residues of keratan sulfate, another glycosaminoglycan. Can also catalyze the sulfation of the Gal residues in sialyl N-acetyllactosamine (sialyl LacNAc) oligosaccharides (By similarity). May play a role in the maintenance of naive T-lymphocytes in the spleen (By similarity).
Subcellular location: Golgi apparatus membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}.
Interaction partners:
- Carbohydrate sulfotransferase 7
- Sulfotransferase 1C4
- Lumican
- Sulfotransferase 1C3
- Sulfotransferase 1B1
- Carbohydrate sulfotransferase 12
- Carbohydrate sulfotransferase 11
- Carbohydrate sulfotransferase 13
- Carbohydrate sulfotransferase 15
Sequence:
MEKGLTLPQDCRDFVHSLKMRSKYALFLVFVVIVFVFIEKENKIISRVSDKLKQIPQALADANSTDPALILAENASLLSLSELDSAFSQLQSRLRNLSLQLGVEPAMEAAGEEEEEQRKEEEPPRPAVAGPRRHVLLMATTRTGSSFVGEFFNQQGNIFYLFEPLWHIERTVSFEPGGANAAGSALVYRDVLKQLFLCDLYVLEHFITPLPEDHLTQFMFRRGSSRSLCEDPVCTPFVKKVFEKYHCKNRRCGPLNVTLAAEACRRKEHMALKAVRIRQLEFLQPLAEDPRLDLRVIQLVRDPRAVLASRMVAFAGKYKTWKKWLDDEGQDGLREEEVQRLRGNCESIRLSAELGLRQPAWLRGRYMLVRYEDVARGPLQKAREMYRFAGIPLTPQVEDWIQKNTQAAHDGSGIYSTQKNSSEQFEKWRFSMPFKLAQVVQAACGPAMRLFGYKLARDAAALTNRSVSLLEERGTFWVT
Protein: Uncharacterized protein Rv3778c (P9WQ67)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Is essential for optimal growth.
Interaction partners:
- Possible nitrogen fixation related protein
- Probable conserved ATP-binding protein ABC transporter
- Iron-sulfur cluster assembly SufBD family protein Rv1462
- Iron-sulfur cluster assembly SufBD family protein Rv1461
- Sphingomyelinase
- PPE family protein PPE43
- Uncharacterized SufE-like protein Rv3284
- Probable O-antigen/lipopolysaccharide transport integral membrane protein ABC transporter RfbD
Sequence:
MAYDVARVRGLHPSLGDGWVHFDAPAGMLIPDSVATTVSTAFRRSGASTVGAHPSARRSAAVLDAAREAVADLVNADPGGVVLGADRAVLLSLLAEASSSRAGLGYEVIVSRLDDEANIAPWLRAAHRYGAKVKWAEVDIETGELPTWQWESLISKSTRLVAVNSASGTLGGVTDLRAMTKLVHDVGALVVVDHSAAAPYRLLDIRETDADVVTVNAHAWGGPPIGAMVFRDPSVMNSFGSVSTNPYATGPARLEIGVHQFGLLAGVVASIEYLAALDESARGSRRERLAVSMQSADAYLNRVFDYLMVSLRSLPLVMLIGRPEAQIPVVSFAVHKVPADRVVQRLADNGILAIANTGSRVLDVLGVNDVGGAVTVGLAHYSTMAEVDQLVRALASLG
Protein: E3 ubiquitin-protein ligase ubr11 (EC 2.3.2.27) (N-end-recognizing protein 11) (N-recognin-11) (RING-type E3 ubiquitin transferase ubr11) (O13731)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: E3 ubiquitin-protein ligase which is a component of the N-end rule pathway (By similarity). Recognizes and binds to proteins bearing specific N-terminal residues that are destabilizing according to the N-end rule, leading to their ubiquitination and subsequent degradation (By similarity). Targets sde2 for degradation (Probable).
Interaction partners:
- Ubiquitin-conjugating enzyme E2 2
- BAG family molecular chaperone regulator 1B
- Sexual differentiation process protein isp4
- E3 ubiquitin-protein ligase ptr1
- Uncharacterized oligopeptide transporter C1840.12
- Glutathione transporter 1
- LON peptidase N-terminal domain and RING finger protein C14F5.10c
- Probable peptide transporter ptr2
Sequence:
MQLHDPPAPLSQPSASRLQKYLLESAEKHAYDSNEESKTHLLQEVFLSLLNYNEDNWKYFLKEKPGAITSDFRLSRLQHSEPECAQELQDKRSGSKVCGHVFRAGEVIYRCKNCGLDNTCVLCAPCFHATNHEGHETHVSISTSYSGICDCGDPEAWNVDLNCKIHNVPDDEEQKKPEEVIPLELQHSIRTTIHILLDFILDVFSCSPVNLKAQSTVGSILADEEASRLSSAKYGVADRPCNVFRVMLWNDEVHTFDAVVGSVLEALDSSNTAFGLEVAQRVDSIGRFAVATSASVHEAIRIANAISKENLAVNVRTARDFFREDICGILLEWFDDLLESHVCYFADYLQIIVCDEILKNWSPGLEKPAKPEVNFNNLPLEIVNDDDSEDDIYAAEELLDVIANLQDETGVTRIANLGGDEDFEADMTDPTIAGFDHPLDDDNDVNDLLDFETEREDIDDLTDEVMETEENEAAEADYPGVNRNTRQDDVQDISMETESQNETDESQNTENVDYNPQTHTPVPIPTTATQDVVTIRPEFNSQLLNNLRQIINARRRPRPAAVCQVSLREDYWKSPHPIPPSSYSFVESPSSILRLDYFLLFDLKFWKRLRGLLSKLYVVPFNRNLLFKRLMGIRFVIHYRSLATAFLFADREPDHSVMFLSVQFFTTPSLAEAVVKDYDFLTNLNATTLSLLTQSNRPSTLFSSDIEYTPTIQLNRQVLKTRRTYNLFSDLGYLLQHPQVKKLVVDDTRYVHQYIDLLRVFQGVIPQQRAILSHVQWDFPHGKNILFVMQRVAMLSNTVSSCFTQAPYERLFYAIKCIITSITHPKLDIAESLEPLSCIPSSSLTNFTQPLVPFSVSRDPISFYHPLHWMLSNLFSYCRVDASSHWDKDTLLALLDHPLRVCVLLAQIDCNLWIRNGRSILLTDAFYRQLNNIEVSYDKDILAIQTILMFVDPNLVLNAVVQRFEFTDWLYNLTYNEHPNYDTERIPAMLCKMLELLIALITEREQILHVDIQDIIRTRLAQQLCFGPLAYSALLSTISSNLVESLSFDKIREEVTSYKAPDGLHDFGVYSLKDEYYDLVDPYYFHYNKNEREESDTILKKRLAKKNNVSAESIIIEPKIRFLEKDGHDIFFAAVNASTFSLIIFRAIEYALVQAESFGSSDIGNTILGDALQLCLISMKIHEFSKSNDFCSRSCAERYPTDSSIMREFGGSAYCLAELCFAILKSPKYKDVHVKVNAVLAGLQKNDPSAYSNMLEATHFELSTTSSTSDSNEIEKTQEKKRLALEKQKKIMQQFRDQQASFLAQNTDFDIGEDQTEDEVTTEEPEEEVKYHEHIRGNCLLCQEECNDQAPYGVIGIIQGSSLLRKTDVHSEIILDEIYSVPPNLDRESHSRPFGKKYDTVVFNRSKDRLLSAYPPGNNIRGVFVSGCGHLMHLGCFKNYYVARSMYRNDVTAGLSEYYYKYSTAKFFMCPLCRSLSNVLLPMPQIPKMCLNIDTLNFPRSMNGWLEEIGTMSSSSFEYQLVRSSLSDTKDTFRSCFLRPWINSKIISAMLARLKIADGALIDQSNNRDVSDLYDRYCETTKLAMKLVKGSTFTNVSPHDLLNSLAYTVSSLEVSQRCSPKQSGATRSVWFNELGPLTLSFLPTLSDTVLKCVCDQIIKSDQQALLLMESQKLLVCKIFYRHSQLKSMLRNGRMSDHDQIQPFLLSNTFDDFVKISSLMLIFGKQDNILYYVKLFYLSEICKTIISMIKVVADSSVVPDLTINYSQQSKSQFYILCKNVLLWCGSSNNIEILDDESNLLRLMSLVEKYSLPFLRRVALVLYCMFDISLEFNEFSNNEDDSELERLSKLIKVPPLQELYSQMSSDENNQILELIAGWCEHLAQNTWGDSTISLEYPGIYELVKLPHRLENLIDSMQESVCCMCHKTPILPAICMLCGSVICFNARQNTVSSRRLTGECNKHAATCTGSVGIFFITKACGILLLDSISNTGTIMPTPYLDIHGETDLQLRRGCPQFLNQKRYDFVVREQWLRQTVLQKMARHMDMTEMQNWRMA
Protein: Lon protease homolog, mitochondrial (EC 3.4.21.53) (P36775)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: ATP-dependent serine protease that mediates the selective degradation of misfolded, unassembled or oxidatively damaged polypeptides as well as certain short-lived regulatory proteins in the mitochondrial matrix. May also have a chaperone function in the assembly of inner membrane protein complexes. Participates in the regulation of mitochondrial gene expression and in the maintenance of the integrity of the mitochondrial genome. Binds to mitochondrial DNA in a site-specific manner. Endogenous substrates include ABF2, ACO2, ILV1, ILV2, LSC1, LYS4, MGM101 and several oxidized proteins. The 2 nucleic acid-binding proteins ABF2 and MGM101 are protected from degradation by PIM1 when they are bound to DNA.
Subcellular location: Mitochondrion matrix {ECO:0000255|HAMAP-Rule:MF_03120, ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:9405361}.
Interaction partners:
- GrpE protein homolog
- Mitochondrial inner membrane m-AAA protease component YTA10
- Mitochondrial inner membrane i-AAA protease supercomplex subunit YME1
- ATP-dependent clpX-like chaperone, mitochondrial
- Heat shock protein 78
- Mitochondrial inner membrane m-AAA protease component YTA12
- Heat shock protein 104
- ATP-dependent molecular chaperone HSC82
- ATP-dependent molecular chaperone HSP82
- Import motor subunit, mitochondrial
Sequence:
MLRTRTTKTLSTVARTTRAIQYYRSIAKTAAVSQRRFASTLTVRDVENIKPSHIIKSPTWQEFQHQLKDPRYMEHFAQLDAQFARHFMATNSGKSILAKDDSTSQKKDEDVKIVPDEKDTDNDVEPTRDDEIVNKDQEGEASKNSRSSASGGGQSSSSRSDSGDGSSKQKPPKDVPEVYPQMLALPIARRPLFPGFYKAVVISDERVMKAIKEMLDRQQPYIGAFMLKNSEEDTDVITDKNDVYDVGVLAQITSAFPSKDEKTGTETMTALLYPHRRIKIDELFPPNEEKEKSKEQAKDTDTETTVVEDANNPEDQESTSPATPKLEDIVVERIPDSELQHHKRVEATEEESEELDDIQEGEDINPTEFLKNYNVSLVNVLNLEDEPFDRKSPVINALTSEILKVFKEISQLNTMFREQIATFSASIQSATTNIFEEPARLADFAAAVSAGEEDELQDILSSLNIEHRLEKSLLVLKKELMNAELQNKISKDVETKIQKRQREYYLMEQLKGIKRELGIDDGRDKLIDTYKERIKSLKLPDSVQKIFDDEITKLSTLETSMSEFGVIRNYLDWLTSIPWGKHSKEQYSIPRAKKILDEDHYGMVDVKDRILEFIAVGKLLGKVDGKIICFVGPPGVGKTSIGKSIARALNRKFFRFSVGGMTDVAEIKGHRRTYIGALPGRVVQALKKCQTQNPLILIDEIDKIGHGGIHGDPSAALLEVLDPEQNNSFLDNYLDIPIDLSKVLFVCTANSLETIPRPLLDRMEVIELTGYVAEDKVKIAEQYLVPSAKKSAGLENSHVDMTEDAITALMKYYCRESGVRNLKKHIEKIYRKAALQVVKKLSIEDSPTSSADSKPKESVSSEEKAENNAKSSSEKTKDNNSEKTSDDIEALKTSEKINVSISQKNLKDYVGPPVYTTDRLYETTPPGVVMGLAWTNMGGCSLYVESVLEQPLHNCKHPTFERTGQLGDVMKESSRLAYSFAKMYLAQKFPENRFFEKASIHLHCPEGATPKDGPSAGVTMATSFLSLALNKSIDPTVAMTGELTLTGKVLRIGGLREKAVAAKRSGAKTIIFPKDNLNDWEELPDNVKEGLEPLAADWYNDIFQKLFKDVNTKEGNSVWKAEFEILDAKKEKD
Protein: DUF3402 domain-containing protein (Q19300)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MGIRPNFAEDVYGDKERRSADDEHVEYSESSLAARRSANVLKLKQLKEAQPMITPAYGGFIHHESSDNVAAIDKDLDFEYGDGDAGIREMAELYSYSEIEEFGINISNWKEYIEESYDGKHEQFPSTFEEFSAVQKNYVIQDLCSRMESADLEVRLKSARIILFLLQGSATDFGCLENEEIEYQYDQKLLMNVPIRKTKEMDPEGPSMVYHRAIENSFICYKNGVYQALCTLLMTEIKEPFESPPNDGRISKASSRSSRNASLADLSDSEKWRTRQLPTMVDNEMLRVILAGLYHMIVQILDERSGREDETDSDLETRKAFREEVQEPIENGNEPLLIVLFDMLHPFYIGTAPHFPIKKIVLLIWKILLLTLGGWEELTVRKREKRMTAGLDIMEDTITVAASQAAFIAKDQEHVRNMAHRAGSFARGGMMARQMAYNDDSKDEDAYSEASSEDSTIASKKEDSPGASSSTPPSIPDTASNFRQGSGEQTPRVGSPVFPVIQKKTLPWRSKTNAQDIEDFIQKGRFKYFNYDFDPGDDTTLFGLPPSFCGAVKILRNNMYTSLTELQVKKDEELNRYLFSMKEDIPETKTETLYRKILPNLSQYICALVKVMVSSVPSTKARHEGLNVLIDCLTPEMEASDILSNSISLDNSTSSPLEEGFRLAIDINRHKEIIVKSLSAILLLLVKHFKLNHIYQFEYICQQIVYVNGIPLILKFLDQNTNKLIQSRHEIYAYNYPQCLYHYVRNNEEWPILTQDNIEEPRPPGAGPYFMWRNVFFAINLIRLLNKLVKAKNDRVKMLMVFKSAPVLKRLFKVRVSVLQLYVLKAIKMQSRYLGRQWRKSNMDIISAIYSRVRHRMTDDWAFASDIKRKCDYQKEDSLIKASIERFHSRRYSALYPQFAIEVNDAPMPGDDYLNRVDMRDFEPVDTCAHSVLGANLKLGRHFKKDYEKWLEQEVFNASIDWDKLLIETRGVEDLM