wanglab/gogpt-training-data huggingface dataset:
Protein: Diacylglycerol O-acyltransferase 1 (AtDGAT1) (EC 2.3.1.20) (Protein TRIACYLGLYCEROL 1) (Q9SLD2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Major contributor to triacylglycerol (TAG) synthesis and oil accumulation in seeds. Catalyzes the acylation of the sn-3 hydroxy group of sn-1,2-diacylglycerol using acyl-CoA. Can use palmitoyl-CoA and oleoyl-CoA as substrates. Can use oleoyl-CoA and linoleoyl-CoA as substrates. Has substrate preference for oleoyl-CoA compared to linoleoyl-CoA. Has complementary functions with PDAT1 that are essential for triacylglycerol synthesis and normal development of both seeds and pollen.
Subcellular location: Plastid, chloroplast membrane {ECO:0000269|PubMed:12177474}; Multi-pass membrane protein {ECO:0000269|PubMed:12177474}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:12177474}; Multi-pass membrane protein {ECO:0000269|PubMed:12177474}.
Interaction partners:
- Diacylglycerol O-acyltransferase 2
- Diacylglycerol O-acyltransferase 3
- Phospholipid:diacylglycerol acyltransferase 1
- Putative phospholipid:diacylglycerol acyltransferase 2
- Phosphatidate phosphatase PAH1
- Phosphatidate phosphatase PAH2
- Triacylglycerol lipase SDP1
- Lipid phosphate phosphatase 2
- Putative lipid phosphate phosphatase 3, chloroplastic
- Lipid phosphate phosphatase 1
Sequence:
MAILDSAGVTTVTENGGGEFVDLDRLRRRKSRSDSSNGLLLSGSDNNSPSDDVGAPADVRDRIDSVVNDDAQGTANLAGDNNGGGDNNGGGRGGGEGRGNADATFTYRPSVPAHRRARESPLSSDAIFKQSHAGLFNLCVVVLIAVNSRLIIENLMKYGWLIRTDFWFSSRSLRDWPLFMCCISLSIFPLAAFTVEKLVLQKYISEPVVIFLHIIITMTEVLYPVYVTLRCDSAFLSGVTLMLLTCIVWLKLVSYAHTSYDIRSLANAADKANPEVSYYVSLKSLAYFMVAPTLCYQPSYPRSACIRKGWVARQFAKLVIFTGFMGFIIEQYINPIVRNSKHPLKGDLLYAIERVLKLSVPNLYVWLCMFYCFFHLWLNILAELLCFGDREFYKDWWNAKSVGDYWRMWNMPVHKWMVRHIYFPCLRSKIPKTLAIIIAFLVSAVFHELCIAVPCRLFKLWAFLGIMFQVPLVFITNYLQERFGSTVGNMIFWFIFCIFGQPMCVLLYYHDLMNRKGSMS
Protein: Choline-phosphate cytidylyltransferase B (EC 2.7.7.15) (CCT-beta) (CTP:phosphocholine cytidylyltransferase B) (CCT B) (CT B) (Phosphorylcholine transferase B) (Q9Y5K3)
Organism: Homo sapiens (Human)
Function: Catalyzes the key rate-limiting step in the CDP-choline pathway for phosphatidylcholine biosynthesis.
Subcellular location: [Isoform 1]: Cytoplasm {ECO:0000269|PubMed:9593753}. Endoplasmic reticulum {ECO:0000269|PubMed:10480912}.; SUBCELLULAR LOCATION: [Isoform 2]: Endoplasmic reticulum {ECO:0000269|PubMed:10480912}.
Interaction partners:
- Choline kinase alpha
- Cholinephosphotransferase 1
- Choline/ethanolaminephosphotransferase 1
- Choline/ethanolamine kinase
- Choline-phosphate cytidylyltransferase A
- Phosphoethanolamine/phosphocholine phosphatase
- Mitogen-activated protein kinase 9
- Mitogen-activated protein kinase 8
- Mitogen-activated protein kinase 3
- Mitogen-activated protein kinase 1
Sequence:
MPVVTTDAESETGIPKSLSNEPPSETMEEIEHTCPQPRLTLTAPAPFADETNCQCQAPHEKLTIAQARLGTPADRPVRVYADGIFDLFHSGHARALMQAKTLFPNSYLLVGVCSDDLTHKFKGFTVMNEAERYEALRHCRYVDEVIRDAPWTLTPEFLEKHKIDFVAHDDIPYSSAGSDDVYKHIKEAGMFVPTQRTEGISTSDIITRIVRDYDVYARRNLQRGYTAKELNVSFINEKRYRFQNQVDKMKEKVKNVEERSKEFVNRVEEKSHDLIQKWEEKSREFIGNFLELFGPDGAWKQMFQERSSRMLQALSPKQSPVSSPTRSRSPSRSPSPTFSWLPLKTSPPSSPKAASASISSMSEGDEDEK
Protein: Receptor expression-enhancing protein 1 (Spastic paraplegia 31 protein) (Q9H902)
Organism: Homo sapiens (Human)
Function: Required for endoplasmic reticulum (ER) network formation, shaping and remodeling; it links ER tubules to the cytoskeleton. May also enhance the cell surface expression of odorant receptors. May play a role in long-term axonal maintenance.
Subcellular location: Membrane {ECO:0000255}. Mitochondrion membrane {ECO:0000269|PubMed:16826527}; Multi-pass membrane protein {ECO:0000255}. Endoplasmic reticulum {ECO:0000269|PubMed:20200447}. Note=Localizes to endoplasmic reticulum tubular network. {ECO:0000269|PubMed:20200447}.
Interaction partners:
- Receptor-transporting protein 2
- Atlastin-1
- Spastin
- Receptor-transporting protein 1
- Atlastin-3
- Atlastin-2
- Protrudin
- WASH complex subunit 5
- Magnesium transporter NIPA1
- Kinesin heavy chain isoform 5A
Sequence:
MVSWIISRLVVLIFGTLYPAYYSYKAVKSKDIKEYVKWMMYWIIFALFTTAETFTDIFLCWFPFYYELKIAFVAWLLSPYTKGSSLLYRKFVHPTLSSKEKEIDDCLVQAKDRSYDALVHFGKRGLNVAATAAVMAASKGQGALSERLRSFSMQDLTTIRGDGAPAPSGPPPPGSGRASGKHGQPKMSRSASESASSSGTA
Protein: AcrIIA6 (A0A2U7VKE8)
Organism: Streptococcus phage D1811
Interaction partners:
Sequence:
MKINDDIKELILEYMSRYFKFENDFYKLPGIKFTDANWQKFKNGGTDIEKMGAARVNAMLDCLFDDFELAMIGKAQTNYYNDNSLKMNMPFYTYYDMFKKQQLLKWLKNNRDDVIGGTGRMYTASGNYIANAYLEVALESSSLGSGSYMLQMRFKDYSKGQEPIPSGRQNRLEWIENNLENIR
Protein: Probable D-alanyl-D-alanine carboxypeptidase (Q9HZG1)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Interaction partners:
- serine-type D-Ala-D-Ala carboxypeptidase
- Ribosomal protein S3AE
Sequence:
MFKSLRTLAFATLLPFALPTLAQVNATLPANVQKALQTNKLTGNDLSLVLIPLDGPGNPTYYNADVSVNPASTMKLFTTYAALEMLGPTYQWKTEFYTDGQLKNGVLNGNLYLKGGGDPKLNMEKLWLLMRDLRANGVTKVTGDLVLDRSYFNIPQLPVFNDDGGDDTKPFLVGPDSLLVNLKSVRMVVRTDGNKVNVQMDPPLANVRIDNQVKMTAPATCPAWPKLRFSPVTQFDGTTLLATGQIPQGCSAQTYMSLLDHPGYTAGAVRGIWQELGGSILGKDRQGSVPRNATLIAKAFSPDLVEIIRDINKYSNNTMARQLFLSIGAQFRNSADGDDAQAAQRVVRQWLARKGITAPRLVMENGSGLSRQERVSAREMAAMLQAAWHSPYAAEYISSLPLAGLDGTMRKRLRRTALVGEAHVKTGTLNTVRALAGFSRDASGHNWVVVAILNSPRPWGASAILDQVLLSLHARK
Protein: Polynucleotide 5'-triphosphatase CTL1 (EC 3.6.1.74) (Capping enzyme RNA triphosphatase-like protein 1) (mRNA 5'-triphosphatase CTL1) (TPase CTL1) (Q03220)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Probably involved in an RNA processing event other than mRNA capping. Releases gamma-phosphate from the 5'-end of RNA to produce a diphosphate terminus.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:10219091}. Nucleus {ECO:0000269|PubMed:10219091}.
Interaction partners:
- mRNA-capping enzyme subunit alpha
Sequence:
MSDQPETPSNSRNSHENVGAKKADANVASKFRSLHISETTKPLTSTRALYKTTRNNSRGATEFHKHVCKLAWKYLACIDKSSISHIEIEMKFGVITDKRTHRRMTPHNKPFIVQNRNGRLVSNVPEQMFSSFQELLRSKSENPSKCAPRVVKQVQKYTKDSIYNCNNASKVGKLTSWRCSEDLRNKELKLTYIKKVRVKDFLIRYPQSSLDAKISISLEVPEYETSAAFRNGFILQRTKSRSTYTFNDKMPLHLDLTKVTTTRRNSHQYTSHEVEVEMDPIFKETISANDREKFNEYMCSFLNASDLIRKAAERDNMLTT
Protein: Mothers against decapentaplegic homolog (MAD homolog) (Mothers against DPP homolog) (SMAD family member) (Q8AY15)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cytoplasm {ECO:0000256|RuleBase:RU361195}. Nucleus {ECO:0000256|RuleBase:RU361195}.
Interaction partners:
- Mothers against decapentaplegic homolog.
- Mothers against decapentaplegic homolog 2
- Receptor protein serine/threonine kinase
- Receptor protein serine/threonine kinase
- TGF-beta receptor type-2
- receptor protein serine/threonine kinase
- Mitogen-activated protein kinase
- Serine/threonine-protein kinase receptor
- Mothers against decapentaplegic homolog
- SMAD family member 4.
Sequence:
MSILPFTPPIVKRLLGWKKGEQNGQEEKWCEKAVKSLVKKLKKTGQLDELEKAITTQDVNTKCITIPRSLDGRLQVSHRKGLPHVIYCRLWRWPDLQSHHELRAIELCEFAFHMKKDEVCVNPYHYQRVETPVLPPVLVPRHTEIPSEFPPLDDYSHSIPENTIFPAGIEPQSNYIPETPPPGYISEDGETSDHQMNRSMDTGSPNLSPNPVSPAHNNLDLQPVTYCEPAFWCSISYYELNQRVGETFHASQPSLTVDGFTDPSNSERFCLGLLSNVNRNAAVELTRRHIGRGVRLYYIGGEVFAECLSDSAIFVQSPNCNQRYGWHPATVCKIPPGCNLKIFNNQEFAALLAQSVNQGFEAVYQLTRMCTIRMSFVKGWGAEYRRQTVTSTPCWIELHLNGPLQWLDKVLTQMGSPSIRCSSVS
Protein: NTF2-related export protein 1 (p15) (P0CAN8)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Stimulator of protein export for NES-containing proteins (By similarity). Also plays a role in mRNA nuclear export.
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- mRNA export factor mex67
- Nuclear transport factor 2
- Poly
- ATP-dependent RNA helicase uap56
- Nucleoporin nup146
- Transcriptional protein swt1
- Nucleoporin nup189
Sequence:
MESSVKYAQEFVQRYYSSLDTNRNGIAEFYRENSLILWNGKPMQVTEFTSMIVNLPYSKTKVEDFDSQQVMGNDMNIIIVVSGTIRFDGKKPHVFSYVSFYCIYLLVLRSSTNFL
Protein: Collagen type VI alpha 1 chain (D3ZUL3)
Organism: Rattus norvegicus (Rat)
Interaction partners:
- Collagen alpha-2
- Collagen alpha-1
- CD44 antigen
- Glycoprotein VI
- Integrin subunit alpha 5
- Collagen alpha-1
- Integrin alpha-8
- Integrin alpha-1
- Integrin alpha-11
- Collagen alpha-1
Sequence:
MVTRRPAGNMRLAHTLLPLLLQACWVAAQDIQGSRAIAFQDCPVDLFFVLDTSESVALRLKPYGALVDKVKSFTKRFIDNLRDRYYRCDRNLVWNAGALHYSDEVEIIRGLMRMPSGRDELKASIDAVKYFGKGTYTDCAIKKGLEELLIGGSHLKENKYLIVVTDGHPLEGYKEPCGGLEDAVNEAKHLGIKVFSVAITPDHLEPRLSIIATDHTYRRNFTAADWGHSRDAEETISQTIDTIVDMIKNNVEQVCCTFECQAARGPPGPRGDPGYEGERGKPGLPGEKGEAGDPGRPGDLGPVGYQGMKGEKGSRGEKGSRGPKGYKGEKGKRGIDGVDGMKGETGYPGLPGCKGSPGFDGIQGPPGPKGDAGAFGLKGEKGEAGAEGEAGRPGNSGPPGDEGEPGEPGPPGEKGEAGDEGNAGPDGAPGERGGPGERGPRGTPGVRGPRGDPGEAGPQGDQGREGPVGIPGDPGESGPIGPKGYRGDEGPPGPEGLRGAPGPVGPPGDPGLMGERGEDGPPGNGTEGFPGFPGYPGNRGPPGINGTKGYPGLKGDEGEAGDPGEDNNDVSPRGVKGAKGYRGPEGPQGPPGHVGPPGPDECEILDIIMKMCSCCECTCGPIDILFVLDSSESIGLQNFEIAKDFIIKVIDRLSKDELVKFEPGQSHAGVVQYSHNQMQEHVDMRSPNVRNAQDFKEAVKKLQWMAGGTFTGEALQYTRDRLLPPTQNNRIALVITDGRSDTQRDTTPLSVLCGSDIQVVSVGIKDVFGFVAGSDQLNVISCQGLSQSRPGISLVKENYAELLDDGFLKNITAQICIDKKCPDYTCPITFSSPTDITILLDSSASVGSHNFETTKVFAKRLAERFLSAGREDPTQVVRVAVVQYSGQGQQQPGRASLQFQQNYTVLASSVDSMDFINDATDVNDALSYVTRFYRENSSGATKKRVLLFSDGNSQGATAEAIEKAVQEAQRGGIEIFVMVVGPQVNEPHIRVLVTGKTAEYDVAFGERHLFRVPNYQALLRGVLYQTVSRKVALG
Protein: General transcription factor IIH subunit 3 (General transcription factor IIH polypeptide 3) (H0YFF7)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|RuleBase:RU368090}.
Interaction partners:
Sequence:
KDGKYELLTSANEVIVEEIKDLMTKSDIKGQHTETLLAGSLAKALCYIHRMNKEVKDNQEMKSRILVIKAAEDSALQYMNFMNVIFAAQKQACDITGGLYLKVPQMPSLLQYLLWVFLPDQDQRSQLILPPPVHVDYRAACFCHRNLIEIGYVCSVCLSIFCNFSPICTTCETAFKISLPPVLKAKKKKLKVSA
Protein: Kinesin-like protein KIF3C (O14782)
Organism: Homo sapiens (Human)
Function: Microtubule-based anterograde translocator for membranous organelles.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000305}.
Interaction partners:
- Kinesin-associated protein 3
- Kinesin-like protein KIF3A
- Kinesin light chain 1
- Putative Polycomb group protein ASXL2
- Fragile X messenger ribonucleoprotein 1
- Kinesin light chain 2
- Pleckstrin homology domain-containing family A member 7
Sequence:
MASKTKASEALKVVARCRPLSRKEEAAGHEQILTMDVKLGQVTLRNPRAAPGELPKTFTFDAVYDASSKQADLYDETVRPLIDSVLQGFNGTVFAYGQTGTGKTYTMQGTWVEPELRGVIPNAFEHIFTHISRSQNQQYLVRASYLEIYQEEIRDLLSKEPGKRLELKENPETGVYIKDLSSFVTKNVKEIEHVMNLGNQTRAVGSTHMNEVSSRSHAIFIITVECSERGSDGQDHIRVGKLNLVDLAGSERQNKAGPNTAGGAATPSSGGGGGGGGSGGGAGGERPKEASKINLSLSALGNVIAALAGNRSTHIPYRDSKLTRLLQDSLGGNAKTIMVATLGPASHSYDESLSTLRFANRAKNIKNKPRVNEDPKDTLLREFQEEIARLKAQLEKRGMLGKRPRRKSSRRKKAVSAPPGYPEGPVIEAWVAEEEDDNNNNHRPPQPILESALEKNMENYLQEQKERLEEEKAAIQDDRSLVSEEKQKLLEEKEKMLEDLRREQQATELLAAKYKAMESKLLIGGRNIMDHTNEQQKMLELKRQEIAEQKRREREMQQEMMLRDEETMELRGTYTSLQQEVEVKTKKLKKLYAKLQAVKAEIQDQHDEYIRVRQDLEEAQNEQTRELKLKYLIIENFIPPEEKNKIMNRLFLDCEEEQWKFQPLVPAGVSSSQMKKRPTSAVGYKRPISQYARVAMAMGSHPRYRAENIMFLELDVSPPAVFEMEFSHDQEQDPRALHMERLMRLDSFLERPSTSKVRKSRSWCQSPQRPPPSTTHASLASASLRPATVADHE
Protein: Ribulose bisphosphate carboxylase large chain, catalytic domain-containing protein (F4INE2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Methylcrotonoyl-CoA carboxylase subunit alpha, mitochondrial
- Biotin carboxylase, chloroplastic
- Ribulose bisphosphate carboxylase small subunit 1A, chloroplastic
- Ribulose bisphosphate carboxylase small subunit 2B, chloroplastic
- Ribulose bisphosphate carboxylase small subunit 3B, chloroplastic
- Ribulose bisphosphate carboxylase small subunit 1B, chloroplastic
- 4-hydroxyphenylpyruvate dioxygenase
- EMBRYO DEFECTIVE 3147
- Putative 2-dehydropantoate 2-reductase
- AT4g33140/F4I10_70 superfamily protein)
Sequence:
MNNAAKRADCWFGAKNYGRAVYECLRGGLYFTKDDENVNSQPFMRWRDRFLFCAEAVYKAQAETGGIKGHYLNATPGTCEEMIKRAVFARELGVPIVMHDYLTGGFTANTSLAHSR
Protein: Low-density lipoprotein receptor class A domain-containing protein 1 (Q5T700)
Organism: Homo sapiens (Human)
Subcellular location: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
- Sentan
Sequence:
MNKVFPQGENGYTAAESKAHPGGEAGGGHLCCSRRGACLSASLLLLLATVAALIALVTILGLPSCTPGAQACITLTNRTGFLCHDQRSCIPASGVCDGVRTCTHGEDEDESLCRDVPQSLPHFLVAHCGDPASWIYSDQKCDGTNNCGDCSDELSPVTVCPPCGPGWWRCPSTFFKYCDCIPRHLCRDHVQHCSDWSDEYACPGP
Protein: Zona pellucida sperm-binding protein 1 (Zona pellucida glycoprotein 1) (Zp-1) [Cleaved into: Processed zona pellucida sperm-binding protein 1] (Q62005)
Organism: Mus musculus (Mouse)
Function: Component of the zona pellucida, an extracellular matrix surrounding oocytes which mediates sperm binding, induction of the acrosome reaction and prevents post-fertilization polyspermy. The zona pellucida is composed of 3 to 4 glycoproteins, ZP1, ZP2, ZP3, and ZP4. ZP1 ensures the structural integrity of the zona pellucida.
Subcellular location: [Processed zona pellucida sperm-binding protein 1]: Zona pellucida {ECO:0000250|UniProtKB:P60852}.; SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P48829}; Single-pass type I membrane protein {ECO:0000255}.
Interaction partners:
- Zona pellucida sperm-binding protein 3
- Zona pellucida sperm-binding protein 2
- Growth/differentiation factor 9
- Oviduct-specific glycoprotein
- Factor in the germline alpha
- Homeobox protein NOBOX
- Zona pellucida sperm-binding protein 3 receptor
- Izumo sperm-egg fusion protein 1
- NACHT, LRR and PYD domains-containing protein 5
- Astacin-like metalloendopeptidase
Sequence:
MAWGCFVVLLLLAAAPLRLGQRLHLEPGFEYSYDCGVRGMQLLVFPRPNQTVQFKVLDEFGNRFEVNNCSICYHWVTSEAQEHTVFSADYKGCHVLEKDGRFHLRVFIQAVLPNGRVDIAQDVTLICPKPDHTVTPDPYLAPPTTPEPFTPHAFALHPIPDHTLAGSGHTGLTTLYPEQSFIHPTPAPPSLGPGPAGSTVPHSQWGTLEPWELTELDSVGTHLPQERCQVASGHIPCMVNGSSKETCQQAGCCYDSTKEEPCYYGNTVTLQCFKSGYFTLVMSQETALTHGVLLDNVHLAYAPNGCPPTQKTSAFVVFHVPLTLCGTAIQVVGEQLIYENQLVSDIDVQKGPQGSITRDSAFRLHVRCIFNASDFLPIQASIFSPQPPAPVTQSGPLRLELRIATDKTFSSYYQGSDYPLVRLLREPVYVEVRLLQRTDPSLVLVLHQCWATPTTSPFEQPQWPILSDGCPFKGDNYRTQVVAADREALPFWSHYQRFTITTFMLLDSSSQNALRGQVYFFCSASACHPLGSDTCSTTCDSGIARRRRSSGHHNITLRALDIVSSPGAVGFEDAAKLEPSGSSRNSSSRMLLLLLAITLALAAGIFVGLIWAWAQKLWEGIRY
Protein: Protein FAM151A (Q8WW52)
Organism: Homo sapiens (Human)
Subcellular location: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MVCREQLSKNQVKWVFAGITCVSVVVIAAIVLAITLRRPGCELEACSPDADMLDYLLSLGQISRRDALEVTWYHAANSKKAMTAALNSNITVLEADVNVEGLGTANETGVPIMAHPPTIYSDNTLEQWLDAVLGSSQKGIKLDFKNIKAVGPSLDLLRQLTEEGKVRRPIWINADILKGPNMLISTEVNATQFLALVQEKYPKATLSPGWTTFYMSTSPNRTYTQAMVEKMHELVGGVPQRVTFPVRSSMVRAAWPHFSWLLSQSERYSLTLWQAASDPMSVEDLLYVRDNTAVHQVYYDIFEPLLSQFKQLALNATRKPMYYTGGSLIPLLQLPGDDGLNVEWLVPDVQGSGKTATMTLPDTEGMILLNTGLEGTVAENPVPIVHTPSGNILTLESCLQQLATHPGHWGIHLQIAEPAALRPSLALLARLSSLGLLHWPVWVGAKISHGSFSVPGHVAGRELLTAVAEVFPHVTVAPGWPEEVLGSGYREQLLTDMLELCQGLWQPVSFQMQAMLLGHSTAGAIGRLLASSPRATVTVEHNPAGGDYASVRTALLAARAVDRTRVYYRLPQGYHKDLLAHVGRN
Protein: Putative ERAD-associated E3 ubiquitin-protein ligase component (Q9USV0)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Component of the endoplasmic reticulum quality control (ERQC) system involved in ubiquitin-dependent degradation of missfolded endoplasmic reticulum proteins.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}.
Interaction partners:
- ERAD-associated E3 ubiquitin-protein ligase hrd1
- Uncharacterized derlin-like protein C365.08c
- Cell division cycle protein 48
- Protein OS-9 homolog
- Uncharacterized derlin-like protein C1687.17c
- Uncharacterized Sel1-like repeat-containing protein C1B3.10c
- Nuclear protein localization protein 4
- Ubiquitin fusion degradation protein 1
- Ubiquitin-conjugating enzyme E2-18 kDa
- ER-derived vesicles protein 41
Sequence:
MQLLNFLICLFFIFKRCVFTVIGGEFSYDNIDKKPILVASYPEGSRFNVSASIKTLPDLVTLTFPKLVKDPGYVYEEAEKGDPESQFLIAMLYAMGPDERLGLSFPRNEPLSRIFLELSATQNYTYALLALAYKHLNGLSTPMSVDKGVELYKQVAHQISCLVQPLSHFAPDIAAEYPVDLYDLSRTSSYSVQKKDDIVEYLKDYALRGNNISAHISLATIYQYGTPGKLKDIKLAVKHYLAAIRLVNSGIPDSPSEAIKSIHNNPRHAPTTKETANSLSIAAFRLGCMALHGELGKPDPSLAYAWFEYGVSLNHSSSKAAIAYMYFMGYPVAENTESITKLLENALASNDPLAFAVAGKVSLANGQIDEATVHLIRAVSNGHLESVLHIADIYYGSNNQLSIAYYENFISRVLELFDVKTISFDPLTRHFAHRLSAELGNLMSQILAAKDRDPSTSYLKTVIFPTNEQTHRNARIAMNYYSRAAARNHIHSLIKIGDFYRMGLGTSAKPELAFSYYSQAAAIHPSALAYWRLGWMHEYGVGVPVDFEMAKKNYDNALMHDTRAFLAVTLARLRMRLSSPDSWFSNIYRILGKVTYKFLKLVQYFIINIFDILSPAGPDSQLPPEPPTLQVDRTPQQPDPQETSESLPSPNTEEMGESYNDIRFTYDYIDGRFLETACVTLIVVVVGLVLMRRHQQHRLQERRERIIRRQNRA
Protein: Succinate dehydrogenase [ubiquinone] iron-sulfur subunit, mitochondrial (EC 1.3.5.1) (Q59QN7)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Subcellular location: Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00004443, ECO:0000256|RuleBase:RU361237}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004443, ECO:0000256|RuleBase:RU361237}; Matrix side {ECO:0000256|ARBA:ARBA00004443, ECO:0000256|RuleBase:RU361237}.
Interaction partners:
- Succinate dehydrogenase flavoprotein subunit, mitochondrial
- Succinate dehydrogenase cytochrome b small subunit
- Uncharacterized protein
- Succinate dehydrogenase cytochrome b small subunit
- Succinate dehydrogenase flavoprotein subunit, mitochondrial
- Succinate--CoA ligase subunit alpha, mitochondrial
- Succinate--CoA ligase subunit beta, mitochondrial
- Nuc2p
- Uncharacterized protein
- 4Fe-4S ferredoxin-type domain-containing protein
Sequence:
MFRSILHQQKAVQFSVRSLATAAAEKAPRLKKFQIYRWNPDTPEVQPKMQTYEVDLNKCGPMVLDALLKIKNEQDATLTLRRSCREGICGSCAMNIGGRNTLACLCRIDQDESKDLKVYPLPHMFVVRDLVPDLTHFYKQYKSIEPYLQRESNPADGRENLQSIEDRAKLDGLYECILCACCSTSCPSYWWNQQQYLGPAVLMQAYRWLIDSRDQATANRKAMLQNSMSLYRCHTIMNCARTCPKGLNPGKAIAEIKKQLAFD
Protein: CCNG2 protein (Q8N5D4)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MKDLGAEHLAGHEGVQLLGLLNVYLEQEERFQPREKGLSLIEATPENDNTLCPGLRNAKVEDLRSLANFFGSCTETFVLAVNILDRFLALMKVKPKHLSCIGVCSFLLAARIVEEDCNIPSTHDVIRISQCKCTASDIKRMEKIISEKLHYELEATTALNFLHLYHTIILCHTSERKEILSLDKLEAQLKACNCRLIFSKAKPSVLALCLLNLEVETLKSVELLEILLLVKKHSKINDTEFFYWRELVSKCLAEYSSPECCKPDLKKLVWIVSRRTAQNLHNSYYSVPELPTIPEGGCFDESESSVAQAGVQWPDLSSFQPPPTRFKRFSCLSLRSSWDYSSWT
Protein: Tight junction protein 2 (Tight junction protein ZO-2) (Zona occludens protein 2) (Zonula occludens protein 2) (Q9Z0U1)
Organism: Mus musculus (Mouse)
Function: Plays a role in tight junctions and adherens junctions. Acts as a positive regulator of RANKL-induced osteoclast differentiation, potentially via mediating downstream transcriptional activity.
Subcellular location: Cell junction, adherens junction {ECO:0000269|PubMed:10026224}. Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Nucleus {ECO:0000269|PubMed:22437732}. Cell junction, tight junction {ECO:0000269|PubMed:10026224, ECO:0000269|PubMed:26609154}. Note=Also nuclear under environmental stress conditions and in migratory endothelial cells and subconfluent epithelial cell cultures. Localizes to tight junctions during initial stages of their formation (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:Q95168}.
Interaction partners:
- Tight junction protein 1
- Afadin
- Occludin
- Junctional adhesion molecule A
- MARVEL domain-containing protein 2
- Claudin-1
- Claudin-5
- Tight junction protein ZO-3
- Cingulin
- Transcriptional coactivator YAP1
Sequence:
MEEVIWEQYTVTLQKDSKRGFGIAVSGGRDNPHFENGETSIVISDVLPGGPADGLLQENDRVVMVNGTPMEDVLHSFAVQQLRKSGKIAAIVVKRPRKVQVAPLQGSPPLSHDDRGFEVIEEFDGRSFRSGYSERSRHSSHDMLSHSWEGNRERGRPHQRTQSRERERSRGRSLERGLDQEDYGRSRERSRGRSLERGLDRDFVSRDHSRGRSIDRDYDRDYERSYHEAYEPDYGGGYSPSYDRRAHPETRYERSRSREHLRSRSPSPESRSRHEHKGQHDPDRPIGVLLTKSKANEEYGLRLGSQIFIKEMTRTGLATKDGNLHEGDIILKINGTVTENMSLTDARKLIEKSRGKLQLVVLRDSKQTLINIPALNDSDSEVEDISEIESNRSFSPEERRQQYSDQDYHSSTEKLKERPSSREETSGRLSRMGATPTPFKSTGDITAAGVTEASREPRYQEEGPVPQPRTAPRVFLRPSPEDEAIYGPNTKMVRFKKGDSVGLRLAGGNDVGIFVAGIQEGTSAEQEGLQEGDQILKVNTQDFRGLVREDAVLYLLEIPKGETVTILAQSRADVYRDILACGRGDSFFIRSHFECEKETPQSLAFTRGEVFRVVDTLYDGKLGHWLAVRIGNELEKGLIPNKSRAEQMASVQNAQRENAGDRADFWRMRGQRSSGGVKKNLRKSREDLAAAVSVSTKFPAYEKVLLREAGFKRPVVLFGPIADIAMERLATELPDLFQTAKTEPKDAGSEKSSGVVRLNTVRQIIEQDKHALLDVTPKAVDLLNYTQWFPIVIFFNPDSRQGVKTIRQRLSPTSNKSSRKLFDQANKLKKTCSHLFTATINVNSANDGWFGSLKDSIQQQQNEAVWVSEGKMEGMDDDAEDRMSYLTAMGADYLSCDSRLISDFEDTDGEGGAYTDNELEEPAEEPLVSSITRSSEPVQHEENIRKSSPEPRAQMRRAASRDQLRDASPPPAFKPEPPKARSQNREDSFDYSKSNLPATAGSEIPGGSTKGYPPPIAAKPAFGRPILKPSTPVPMPESEEVGESTEEQEDAPRSVLGRVKIFEKMDHKAKLQRMQELQEAQNARIEIAQKHPDIYAVPIKAPKPDAGLPPHMSSRPPEPQKAPSRLYQDTRGSYGSDPEEEEYRQQLAAHSKRGYYSQPSRYRDTEL
Protein: SHC SH2 domain-binding protein 1 (Q8NEM2)
Organism: Homo sapiens (Human)
Function: May play a role in signaling pathways governing cellular proliferation, cell growth and differentiation. May be a component of a novel signaling pathway downstream of Shc. Acts as a positive regulator of FGF signaling in neural progenitor cells.
Subcellular location: Midbody {ECO:0000269|PubMed:21187330}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:21187330}. Note=Displays weak localization to the spindle midzone in some early telophase cells and is concentrated at the midbody in late cytokinesis. {ECO:0000269|PubMed:21187330}.
Interaction partners:
- Rac GTPase-activating protein 1
- Kinesin-like protein KIF23
- SHC-transforming protein 1
- Kinesin-like protein KIF11
- Condensin-2 complex subunit G2
- Baculoviral IAP repeat-containing protein 5
- Ribonucleoside-diphosphate reductase subunit M2
- Lymphokine-activated killer T-cell-originated protein kinase
- Condensin complex subunit 3
- Polymerase delta-interacting protein 3
Sequence:
MADGSLTGGGLEAAAMAPERMGWAVEQELASLEKGLFQDEDSCSDCSYRDKPGSSLQSFMPEGKTFFPEIFQTNQLLFYERFRAYQDYILADCKASEVQEFTAEFLEKVLEPSGWRAVWHTNVFKVLVEITDVDFAALKAVVRLAEPYLCDSQVSTFTMECMKELLDLKEHRLPLQELWVVFDDSGVFDQTALAIEHVRFFYQNIWRSWDEEEEDEYDYFVRCVEPRLRLHYDILEDRVPSGLIVDYHNLLSQCEESYRKFLNLRSSLSNCNSDSEQENISMVEGLKLYSEMEQLKQKLKLIENPLLRYVFGYQKNSNIQAKGVRSSGQKITHVVSSTMMAGLLRSLLTDRLCQEPGEEEREIQFHSDPLSAINACFEGDTVIVCPGHYVVHGTFSIADSIELEGYGLPDDIVIEKRGKGDTFVDCTGADIKISGIKFVQHDAVEGILIVHRGKTTLENCVLQCETTGVTVRTSAEFLMKNSDLYGAKGAGIEIYPGSQCTLSDNGIHHCKEGILIKDFLDEHYDIPKISMVNNIIHNNEGYGVVLVKPTIFSDLQENAEDGTEENKALKIQTSGEPDVAERVDLEELIECATGKMELCARTDPSEQVEGNCEIVNELIAASTQKGQIKKKRLSELGITQADDNLMSQEMFVGIVGNQFKWNGKGSFGTFLF
Protein: Mitochondrial-processing peptidase subunit beta (EC 3.4.24.64) (Beta-MPP) (Q23295)
Organism: Caenorhabditis elegans
Function: Catalytic subunit of the essential mitochondrial processing protease (MPP), which cleaves the mitochondrial sequence off newly imported precursors proteins (Probable). Preferentially, cleaves after an arginine at position P2 (Probable).
Subcellular location: Mitochondrion matrix {ECO:0000250|UniProtKB:O75439}.
Interaction partners:
- Cytochrome c domain-containing protein
- Mitochondrial-processing peptidase subunit alpha
- Cytochrome b-c1 complex subunit 7
- Cytochrome b-c1 complex subunit Rieske, mitochondrial
- NADH dehydrogenase 1 alpha subcomplex subunit 9, mitochondrial
- Cytochrome c oxidase subunit 5A, mitochondrial
- COX5B-domain-containing protein
- NADH dehydrogenase flavoprotein 1, mitochondrial
- Cytochrome c oxidase subunit 4
- Cytochrome b-c1 complex subunit 8
Sequence:
MYRRLASGLYQTSQRRIAQVQPKSVFVPETIVTTLPNGFRVATENTGGSTATIGVFIDAGSRYENEKNNGTAHFLEHMAFKGTPRRTRMGLELEVENIGAHLNAYTSRESTTYYAKCFTEKLDQSVDILSDILLNSSLATKDIEAERGVIIREMEEVAQNFQEVVFDILHADVFKGNPLSYTILGPIELIQTINKNDLQGYINTHYRSGRMVLAAAGGVNHDAIVKMAEKYFGELKHGDSSTEFVPATYSPCEVRGDIPDLPMLYGAMVVEGVSWTHEDNLALMVANTLMGEYDRMRGFGVNAPTRLAEKLSQDAGIEVFQSFNTCYKETGLVGTYFVAAPESIDNLIDSVLQQWVWLANNIDEAAVDRAKRSLHTNLLLMLDGSTPVCEDIGRQLLCYGRRIPTPELHARIESITVQQLRDVCRRVFLEGQVSAAVVGKTQYWPVNEEIHGRLIRMQ