wanglab/gogpt-training-data huggingface dataset:
Protein: Cytochrome c oxidase 19-1 (F4IEX1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Cytochrome c oxidase assembly protein COX11
- Cytochrome c oxidase copper chaperone 1
- Cytochrome c oxidase copper chaperone 2
- Cytochrome c oxidase subunit 6b-3
- Mitochondrial intermembrane space import and assembly protein 40 homolog
- RING-H2 finger protein ATL48
- Cytochrome c oxidase subunit 6b-2
- Large ribosomal subunit protein uL11m
- Surfeit locus protein 1
Sequence:
MMITIKFDLNRYSCSWGAGGAFGGNRGLRPIPPEKGIFPLDHLHECDAEKKEYLGCLKSSAHKSEQCRHLSKKYLQCRMAKNLMAKQDMAELGFSGVKELDSTEDKNTESIEH
Protein: Tyrosine-protein phosphatase CDC14 homolog (EC 3.1.3.48) (CDC fourteen-like phosphatase 1) (Q9P7H1)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Protein phosphatase which antagonizes mitotic cyclin-dependent kinase cdc2, the inactivation of which is essential for exit from mitosis. To access its substrates, is released from nucleolar sequestration during mitosis. Plays an essential in coordinating the nuclear division cycle with cytokinesis through the cytokinesis checkpoint. Involved in chromosome segregation, where it is required for meiosis I spindle dissambly as well as for establishing two consecutive chromosome segregation phases. Allows damaged actomyosin rings to be maintained to facilitate completion of cell division in response to minor perturbation of the cell division machinery. Dephosphorylates the mitotic inducer cdc25 for its rapid degradation. Down-regulation of cdc25 activity ensures a prompt inactivation of mitotic cdc2 complexes to trigger cell division. Dephosphorylates also cdc2-phosphorylated nsk1, allowing nsk1-binding to kinetochores and spindle. Dephosphorylates ase1, which is essential for spindle midzone assembly and for continuous extension of the anaphase spindle. Tethered to the contractile ring by mid1, where it dephosphorylates cdc15.
Subcellular location: Nucleus, nucleolus. Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body. Note=Localizes to kinetochores in prometaphase. Cytoplasmic retention is mediated through the binding of rad24. Tethered to the contractile ring by mid1.
Interaction partners:
- Serine/threonine-protein kinase plo1
- Septum-promoting GTP-binding protein 1
- Cell division control protein 16
- Cell division control protein 7
- Cyclin-dependent kinase 1
- Separin
- Maintenance of ploidy protein mob1
- WD repeat-containing protein srw1
- Mitogen-activated protein kinase spm1
- Serine/threonine-protein kinase ppk35
Sequence:
MDYQDDGLGEMIEFLEDKLYYTSLSQPPKAELYPHMHFFTIDDELIYNPFYHDFGPLNVSHLIRFAVIVHGIMGKHRQAKKSKAIVLYSSTDTRLRANAACLLACYMVLVQNWPPHLALAPLAQAEPPFLGFRDAGYAVSDYYITIQDCVYGLWRARESSILNIRNIDVHDYETYERVENGDFNWISPKFIAFASPIQAGWNHASTRPKKLPQPFAIVLDYFVANKVKLIVRLNGPLYDKKTFENVGIRHKEMYFEDGTVPELSLVKEFIDLTEEVEEDGVIAVHCKAGLGRTGCLIGAYLIYKHCFTANEVIAYMRIMRPGMVVGPQQHWLHINQVHFRAYFYEKAMGRAIQQATAAEPLATPPRHPLNATNGTSQSNISTPLPEPTPGQPRKVSGHNPPSARRLPSASSVKFNEKLKNASKQSIQNENKASYSSYEDSEIQNDDETRTVGTPTETISVVRLRRSSSQSNIEPNGVRSPTSSPTGSPIRRTSGNRWSSGSSHSKKSAQRSVSMSSLNNTSNGRVAKPKPSKSRLIS
Protein: Copper transport protein CTR1 (Q59NP1)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Function: Required for high affinity copper (probably reduced Cu I) transport into the cell.
Subcellular location: Cell membrane {ECO:0000269|PubMed:19824013}; Multi-pass membrane protein {ECO:0000269|PubMed:19824013}.
Interaction partners:
Sequence:
MEFLKRHEGHMHMSDSATSMVTSATSAVMDMASATMSMTMSSSTSSSSGMAMEGMDHGSSHMAMNMWLTASFKDYPVVFKDLRASTKAQAFGIFVLLFFVAFLARMLEFVRNYLEEIVWKNNNYAEVEQGISQHSANLQSPPVKSCCDDNAKEVVSDESIDKQNSPQHEETTKARGTGKSLSLASTISRDIIRLALCIIPDLFAYSLMLAAMTYTLTYFFAVVIGSGVGRFVAERLMEHYRIKRGPPRNCC
Protein: Transcription factor Sp7 (Transcription factor osterix) (Q6U1J4)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MAASILEEETRYGSSPLAMLTATCNKFGSTSPVRDSATPGKPGSTIPIKKAYSMTSELQSAKNGRNESVADSYTGSFSSSGGLLTPTGSPPPAPTGAYGSEYNPFSTFQTSSVSQDPSLLGSKATADCLTSVNTYLDMTHPYGSWYKGIHPGITASPANATSSWWDVHTNANWLSPGQAQPDSLQAPLQPVAPQASLNPQMPSYTPDFTPLNPAPYPSVGLSSSSHLLQSSQHMLPQDMYKPKPVPTSGILDNSMGLKSARGSGYAAGSTTGRSSCDCPNCQELERLGASAASLRKKPVHSCHIPGCGKVYGKASHLKAHLRWHTGERPFVCNWLFCGKRFTRSDELERHVRTHTREKKFTCLLCNKRFTRSDHLSKHQKTHSEASLQGKEEPETRAEESSADKVAPAGSEIGIQEPAVGGEEKSSTGNGVDSGSGLLEI
Protein: Glutaredoxin-related protein 5, mitochondrial (Monothiol glutaredoxin-5) (Q86SX6)
Organism: Homo sapiens (Human)
Function: Monothiol glutaredoxin involved in mitochondrial iron-sulfur (Fe/S) cluster transfer. Receives 2Fe/2S clusters from scaffold protein ISCU and mediates their transfer to apoproteins, to the 4Fe/FS cluster biosynthesis machinery, or export from mitochondrion. Required for normal regulation of hemoglobin synthesis by the iron-sulfur protein ACO1.
Subcellular location: Mitochondrion matrix {ECO:0000269|PubMed:20364084}.
Interaction partners:
- BolA-like protein 3
- BolA-like protein 1
- Iron-sulfur cluster assembly 2 homolog, mitochondrial
- Iron-sulfur cluster assembly 1 homolog, mitochondrial
- Iron-sulfur cluster co-chaperone protein HscB
- Mitochondrial glycine transporter
- Glutaredoxin-1
- Iron-sulfur cluster assembly enzyme ISCU
- Cysteine desulfurase
- 5-aminolevulinate synthase, erythroid-specific, mitochondrial
Sequence:
MSGSLGRAAAALLRWGRGAGGGGLWGPGVRAAGSGAGGGGSAEQLDALVKKDKVVVFLKGTPEQPQCGFSNAVVQILRLHGVRDYAAYNVLDDPELRQGIKDYSNWPTIPQVYLNGEFVGGCDILLQMHQNGDLVEELKKLGIHSALLDEKKDQDSK
Protein: Superoxide dismutase [Mn], mitochondrial (EC 1.15.1.1) (P09671)
Organism: Mus musculus (Mouse)
Function: Destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems.
Subcellular location: Mitochondrion matrix.
Interaction partners:
- Superoxide dismutase
- Small ribosomal subunit protein mS29
- Large ribosomal subunit protein uL29m
- Large ribosomal subunit protein mL46
- Large ribosomal subunit protein uL3m
- Large ribosomal subunit protein uL13m
- Large ribosomal subunit protein bL17m
- Peroxisome proliferator-activated receptor gamma coactivator 1-alpha
- Small ribosomal subunit protein uS17
- Large ribosomal subunit protein mL43
Sequence:
MLCRAACSTGRRLGPVAGAAGSRHKHSLPDLPYDYGALEPHINAQIMQLHHSKHHAAYVNNLNATEEKYHEALAKGDVTTQVALQPALKFNGGGHINHTIFWTNLSPKGGGEPKGELLEAIKRDFGSFEKFKEKLTAVSVGVQGSGWGWLGFNKEQGRLQIAACSNQDPLQGTTGLIPLLGIDVWEHAYYLQYKNVRPDYLKAIWNVINWENVTERYTACKK
Protein: Structural maintenance of chromosomes flexible hinge domain-containing protein GMI1 (SMC hinge domain-containing protein GMI1) (Protein GAMMA-IRRADIATION AND MITOMYCIN C INDUCED 1) (F4KFS5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Contributes to DNA double-strand break (DSB) repair via somatic homologous recombination. Functions downstream of ATM.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- MATH domain and coiled-coil domain-containing protein At3g58270
- Replication protein A 70 kDa DNA-binding subunit E
- At1g09815
- ATP-dependent DNA helicase Q-like 3
- DNA repair protein RAD51 homolog 1
- Protein XRI1
- BRCT domain-containing protein At4g02110
- Protein MICRORCHIDIA 5
- Structural maintenance of chromosomes protein 4
- CBL-interacting serine/threonine-protein kinase 11
Sequence:
MSSRRSVKRSLVLDDDDDEDIFYNFKVLLPNGTSVKLTLKNPEPEISMQSFVNLVKKEYDNARKDCLLMSKRMKVDWNSGGKFHLESNGGKMKGIVRFAAFKPDLCHIIRLDDGSGIASTMYENLWDLTPDTDLLKELPENYSFETALADLIDNSLQAVWPYREGARKLISVDISGDHITVFDTGRGMDSSEGNSIDKWGKIGASLHRSQKTGAIGGNPPYLKPYFGMFGYGGPYASMFLGRCDFSFCLPILICIVLLRLTLFSVRRTLVSSKTKESKKVFTLQFKKEALIDNRSIVGKNWKTDGGMRDPSEEEMKLSPHGSFTKVEIFESEFDISKIYQLQCRLKDIYFPYIQFCLATIFLCDELSKTGRTERPVAFQVNGEDLAEIAGGEVAITNLHSKGQFFSFQIRFTLFGGKRKGTAQEANARLKFVYFPIVQGKESIEKILQSLEEEGCKVSESFQTFGRVSLRRLGRLLPEVRWDSIPFMQRGNRASTLQKSCRRVKCFVDLDAGFSPTPSKTDLASQNPFSVALRNFGSKSTEKEKDDDVNIVIHREGKSVSYAHLEEKYQEWVLEMHNTHDEEAASGLDEAVLIVGSLDKKALGILRDAVRVHKEVRRKEKTWKRGQNIKILRGAYAGIHNNNVYATIDYFLIEGFEDEAGGDTRILCRPIDRPENEGCKLSIIDGISKLEVQSSLSLPITIIDSGKCLPVDANEWNRKLDKQQEKAPSKIDLLDERDCRELKIDGELPIGNSVRAGKAPPKQIVAVVRPACFTSLTPSKKLDQKNIVKMDGEEMVMVVKLKSSDKNISSQRLFPTSRKGISGLYIFSLGSKFPNLFKKAGTYNFSFSIGNSIKCNKTVVVRPSSKAARWELDDNLESLPCNVRVGSSLPPFRIACFDKYKNKIPFTSVPSLEVELEASPGFLIKIDKLETNLINDGLILKIENMLVETDELDQIRPNYEATLEIRAMDNPFSVSVPCKVNPGPLKRVAVNNPKALENLLPDSTVEDFILELFDGYNNHVAEGTDVLIHIDGYRIEDWMGINRKVDSRGCINLSGILKVTEGYGKSVSLSVMSGNEVIFCKESQIDERQLRLVTELPDCCTAGTNLMNLIFQVTELDGSLDTSIHHDEKSGCFHTMSIESDSSSVESAIRYAFVHGSCKVSSLSLPENEGVFSCRVFHSRYPELQMSIKIQVTSAPTSEREESGYSTPHSKTTPPPESGIPSITNPWPTPCSQFGVLAIRSSSLALSSETSLMDMAQYTEDLKEKINIDEERRVELEERLKCLQAQREHAEQECSRLQASLEPLGAPFPECLSTKESMMKQIEEKHHDTAASVFCCLYRKAPPPRSLFLSQKGMFGVVALLGSVASTSLSRVLSEYLGKDTMLSLVCKSSQFGPKSDEYRKFQSEAASLGRSITNRFLVICLDATRPWRNGLVRNDPQKRLAMDNPYLPNGDPIPGFKGYAVNMIDLASEELDIQSSSGYGLRETLFYGVFRELQVYETAEHLEAALPHINGGDAVSLDGVIARENGFIYSGCCTPEVHFPITVTERQEKALVQLEITRDKKRKTEEMMTEENRSLRRLVKKLKKANEKYQNFTAMADS
Protein: Transcription factor MTB2 (Basic helix-loop-helix protein 133) (Protein MYC2-TARGETED BHLH 2) (Transcription factor bHLH133) (bHLH transcription factor bHLH133) (A0A3Q7HES4)
Organism: Solanum lycopersicum (Tomato) (Lycopersicon esculentum)
Function: Transcription factor that negatively regulates jasmonate (JA) signaling. Negatively regulates JA-dependent response to wounding, JA-induced expression of defense genes, JA-dependent responses against herbivorous insects, and JA-dependent resistance against Botrytis cinerea infection. Plays a positive role in resistance against the bacterial pathogen Pseudomonas syringae pv tomato DC3000.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981}.
Interaction partners:
Sequence:
MTMLWSDEDKTMVAAVLGTKAFDYLMSSLVSAECSLMAMGSDENLQNMLSDLVERPNASNFSWNYAIFWQISRSKLGELVLGWGDGCCREAREGEESELTRILNIRLADEAQQRMRKRVLQKLHMFFGGTDEDNYVSGLDKVTDTEMFFLASMYFSFPRGQGGPGKCFTAGKHVWLSDVMRSSVDYCSRSFLMKSAGMQTVVLIPTDIGVMELGSVRTIPESLELVHSIKSCFSSFLAQVRAKQAAPLAAVVAEKKNGNNSVFPSSFPFDQSKENPKIFGQNLESGSTEFREKLALRKPVDGPLEMYRNGNRAPIINTQNGVRPVSWASFGNVKPGNSVDLYSPQAPPNNLREFVNGGREELRLNSLQHQKPGGMQIDFTNSRPVVSPVPTVESEHSDVEVSCKEKHAGPADERRPRKRGRKPANGREEPLNHVEAERQRREKLNQRFYALRAVVPNISKMDKASLLGDAIAHITDMQKRIRDAEYKLEKRGSTSVDAADINIEAASDEVIVRARCPLGTHPVAKVVEAFKETQVSVVESKLAVGNDTVYHTFVVKSSGPEQLTKEKLMAAFAGESNSL
Protein: Ubiquitin-fold modifier-conjugating enzyme 1 (Ufm1-conjugating enzyme 1) (Q9Y3C8)
Organism: Homo sapiens (Human)
Function: E1-like enzyme which specifically catalyzes the second step in ufmylation. Accepts the ubiquitin-like modifier UFM1 from the E1 enzyme UBA5 and forms an intermediate with UFM1 via a thioester linkage. Ufmylation is involved in reticulophagy (also called ER-phagy) induced in response to endoplasmic reticulum stress.
Interaction partners:
- Ubiquitin-like modifier-activating enzyme 5
- Ubiquitin-fold modifier 1
- ELAV-like protein 1
- E3 UFM1-protein ligase 1
- DDRGK domain-containing protein 1
- NEDD8-conjugating enzyme Ubc12
- Ufm1-specific protease 2
- Ufm1-specific protease 1
- CDK5 regulatory subunit-associated protein 3
Sequence:
MADEATRRVVSEIPVLKTNAGPRDRELWVQRLKEEYQSLIRYVENNKNADNDWFRLESNKEGTRWFGKCWYIHDLLKYEFDIEFDIPITYPTTAPEIAVPELDGKTAKMYRGGKICLTDHFKPLWARNVPKFGLAHLMALGLGPWLAVEIPDLIQKGVIQHKEKCNQ
Protein: NEB protein (Q6P516)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
ATTVTPEIERVKRNQENFSSVLYKENLGKGIPTPITPEMERVKRNQENFSSVLYKENLGTGIPIPITPEMQRVKHNQENLSSVLYKENMGKGTPLPVTPEMERVKHNQENISSVLYKENMGKGTPLPVTPEMERVKHNQENISSVLYKENMGKGTPLPVTPEMERVKHNQENISSVLYKENVGKATATPVTPEMQRVKRNQENISSVLYKENLGKATPTPFTPEMERVKRNQENFSSVLYKENMRKATPTPVTPEMERAKRNQENISSVLYSDSFRKQIQGKAAYVLDTPEMRRVRETQRHISTVKYHEDFEKHKGCFTPVVTDPITERVKKNMQDFSDINYRGIQRKVVEMEQKRNDQDQETITGLRVWRTNPGSVFDYDPAEDNIQSRSLHMINVQAQRRSREQSRSASALSISGGEEKSEHSEAPDHHLSTYSDGGVFAVSTAYKHAKTTELPQQRSSSVATQQTTVSSIPSHPSTAGKIFRAMYDYMAADADEVSFKDGDAIINVQAIDEGWMYGTVQRTGRTGMLPANYVEAI
Protein: Olfactory receptor 14J1 (Hs6M1-28) (Olfactory receptor 5U1) (Olfactory receptor OR6-25) (Q9UGF5)
Organism: Homo sapiens (Human)
Function: Odorant receptor.
Subcellular location: Cell membrane; Multi-pass membrane protein.
Interaction partners:
Sequence:
MVNLTSMSGFLLMGFSDERKLQILHALVFLVTYLLALTGNLLIITIITVDRRLHSPMYYFLKHLSLLDLCFISVTVPQSIANSLMGNGYISLVQCILQVFFFIALASSEVAILTVMSYDRYAAICQPLHYETIMDPRACRHAVIAVWIAGGLSGLMHAAINFSIPLCGKRVIHQFFCDVPQMLKLACSYEFINEIALAAFTTSAAFICLISIVLSYIRIFSTVLRIPSAEGRTKVFSTCLPHLFVATFFLSAAGFEFLRLPSDSSSTVDLVFSVFYTVIPPTLNPVIYSLRNDSMKAALRKMLSKEELPQRKMCLKAMFKL
Protein: Potassium/sodium hyperpolarization-activated cyclic nucleotide-gated channel 3 (Q9JKA8)
Organism: Rattus norvegicus (Rat)
Function: Hyperpolarization-activated potassium channel. May also facilitate the permeation of sodium ions (By similarity).
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:O88705}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Potassium/sodium hyperpolarization-activated cyclic nucleotide-gated channel 2
- Potassium/sodium hyperpolarization-activated cyclic nucleotide-gated channel 1
- PEX5-related protein
- BTB/POZ domain-containing protein KCTD3
Sequence:
MEEEARPAVGDGEAATPARETPPAAPAQARAASGGVPESAPEPKRRQLGTLLQPTVNKFSLRVFGSHKAVEIEQERVKSAGAWIIHPYSDFRFYWDLIMLLLMVGNLIVLPVGITFFKEENSPPWIVFNVLSDTFFLLDLVLNFRTGIVVEEGAEILLAPRAIRTRYLRTWFLVDLISSIPVDYIFLVVELEPRLDAEVYKTARALRIVRFTKILSLLRLLRLSRLIRYMHQWEEIFHMTYDLASAVVRIFNLIGMMLLLCHWDGCLQFLVPMLQDFPSDCWVSMNRMVNHSWGRQYSHALFKAMSHMLCIGYGQQAPVGMPDVWLTMLSMIVGATCYAMFIGHATALIQSLDSSRRQYQEKYKQVEQYMSFHKLPADTRQRIHEYYEHRYQGKMFDEESILGELSEPLREEIINFTCRGLVAHMPLFAHADPSFVTAVLTKLRFEVFQPGDLVVREGSVGRKMYFIQHGLLSVLARGARDTRLTDGSYFGEICLLTRGRRTASVRADTYCRLYSLSVDHFNAVLEEFPMMRRAFETVAMDRLRRIGKKNSILQRKRSEPSPGSSSGGVMEQHLVQHDRDMARGIRGLAPGTGARLSGKPVLWEPLVHAPLQAAAVTSNVAIALTHQRGPLPLSPDSPATLLARSARRSAGSPASPLVPVRAGPLLARGPWASTSRLPAPPARTLHASLSRTGRSQVSLLGPPPGGGGRRLGPRGRPLSASQPSLPQRATGDGSPRRKGSGSERLPPSGLLAKPPGTVQPSRSSVPEPVTPRGPQISANM
Protein: YEATS domain containing 4 (A0A8I6GLW6)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|PROSITE-ProRule:PRU00376}.
Interaction partners:
Sequence:
MFKRMAEFGPDSGGRVKGVTIVKPIVYGNVARYFGKKREEDGHTHQWTVYVKPYRNEVTLYHLLKLFQSDTNAMLGKKTVVSEFYDEMIFQDPTAMMQQLLTTSRQLTLGAYKHETEFAELEVKTREKLEAAKNKTSLEIAELKERLKASRETINCLKNEIRKLEEDDQTKDI
Protein: ATP-dependent RNA helicase SUV3 homolog, mitochondrial (EC 3.6.4.13) (Q9VN03)
Organism: Drosophila melanogaster (Fruit fly)
Function: Major helicase player in mitochondrial RNA metabolism and maintenance. Likely component of the mitochondrial degradosome (mtEXO) complex, that degrades 3' overhang double-stranded RNA with a 3'-to-5' directionality in an ATP-dependent manner (By similarity). ATPase and ATP-dependent multisubstrate helicase, able to unwind double-stranded (ds) DNA and RNA, and RNA/DNA heteroduplexes in the 5'-to-3' direction (By similarity). Regulates mRNA stability and is required for the correct processing and maturation of mitochondrial transcripts.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:26152302}. Note=Unlike in mammals, does not localize to the nucleus. {ECO:0000269|PubMed:26152302}.
Interaction partners:
- polyribonucleotide nucleotidyltransferase
- Exosome complex exonuclease RRP44
- Dis3 like 3'-5' exoribonuclease 2, isoform C
- Ribonuclease Z, mitochondrial
- Eukaryotic initiation factor 4A-III
- Poly
- DNA-directed RNA polymerase
- ATP synthase subunit a
- LD23303p
- ATP-dependent RNA helicase DDX54
Sequence:
MQNCRRCISLTGLLRMTLYLRPSFSIDLSLRRLHRAAFLFSRKKPETNLSTLFKPVQVHAYVDSEDVGSELSGKLEKAELLKILNKFTQRREIKSLCNENGLDDYLQQQAFGSFRRFCIEAENLPVDLHITFSDITQGAGHIDDIFPYFLRHAKTVFPHLDCMDDLKKISDLRQPANWYSNARAITRKIVFHAGPTNSGKTYHAMERYLSAKTGVYCGPLKLLATEVYNKANERGTPCDLVTGEERKFGISESLPANHVACTVEMTSVNTPYEVAVIDEIQQIRDPQRGWAWTRAFLGLIADEVHVCGEPGALDLLQKICETTGETVEVRLYDRLTELTVENTALGSLDNIVPGDCIVCFSKHDIYTVSREIEARGKEVAVIYGGLPPGTKLAQAAKFNDPANSCKVMVATDAIGMGLNLSIRRIIFYSLIKPSMNERGEREIDTISVSSALQIAGRAGRFRTQWEHGYVTAFKSEDLQTLQRILARTPEPIKQAGLHPTADQIELYAYHLPSSSLSNLMDIFVNLCTVDDSLYFMCNIEDFKFLAEMIQHVALPLRARYVFCCAPINRKMPFVCSMFLKVARQYSRNEPITFDFIKKNCGWPFKLPKTILDLVHLEAVFDVMDLYLWLSYRFMDLFPEAAYVRDAQKELDEIIQQGVFQITRLLKNTEASQDGETSNYAIRRITHVKEPRLPSLSRGRLTERLLAQGLLTPGMLSELRKEWDAQQLGKSNSQSNENSEPVVNSDDEDNYSGIGRKTRKKRRK
Protein: Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit TUSC3 (Oligosaccharyl transferase subunit TUSC3) (Magnesium uptake/transporter TUSC3) (Protein N33) (Tumor suppressor candidate 3) (Q13454)
Organism: Homo sapiens (Human)
Function: Acts as accessory component of the N-oligosaccharyl transferase (OST) complex which catalyzes the transfer of a high mannose oligosaccharide from a lipid-linked oligosaccharide donor to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains. Involved in N-glycosylation of STT3B-dependent substrates. Specifically required for the glycosylation of a subset of acceptor sites that are near cysteine residues; in this function seems to act redundantly with MAGT1. In its oxidized form proposed to form transient mixed disulfides with a glycoprotein substrate to facilitate access of STT3B to the unmodified acceptor site. Has also oxidoreductase-independent functions in the STT3B-containing OST complex possibly involving substrate recognition.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase 48 kDa subunit
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit DAD1
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 2
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit STT3B
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 1
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit STT3A
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 4
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit TMEM258
- Mannosyl-oligosaccharide glucosidase
- Platelet-derived growth factor receptor-like protein
Sequence:
MGARGAPSRRRQAGRRLRYLPTGSFPFLLLLLLLCIQLGGGQKKKENLLAEKVEQLMEWSSRRSIFRMNGDKFRKFIKAPPRNYSMIVMFTALQPQRQCSVCRQANEEYQILANSWRYSSAFCNKLFFSMVDYDEGTDVFQQLNMNSAPTFMHFPPKGRPKRADTFDLQRIGFAAEQLAKWIADRTDVHIRVFRPPNYSGTIALALLVSLVGGLLYLRRNNLEFIYNKTGWAMVSLCIVFAMTSGQMWNHIRGPPYAHKNPHNGQVSYIHGSSQAQFVAESHIILVLNAAITMGMVLLNEAATSKGDVGKRRIICLVGLGLVVFFFSFLLSIFRSKYHGYPYSDLDFE
Protein: Glutathione S-transferase (EC 2.5.1.18) (C0HLL7)
Organism: Lactiplantibacillus plantarum (Lactobacillus plantarum)
Function: Glutathione S-transferase, which conjugates reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles.
Interaction partners:
Sequence:
YLFVMTNRMKLLNYSFEGLPNLKKLDEIMRQHPAVKRVLEQEGAPHTLTD
Protein: Lipase 5 (EC 3.1.1.3) (Q9P8W0)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Subcellular location: Secreted {ECO:0000269|PubMed:11131027}.
Interaction partners:
Sequence:
MLYLILFLIAPIYAGLIFPTKPSSDPFYNPPKGFENAAVGDILQSRATPKSITGGFTPLKIQNSWQLLVRSEDSFGNPNVIVTTVIEPVNADPSKIASYQVFEDAAKADCAPSYALQFGSDLTTFVTQAEMYLMAPLLDQGYYVVSPDYEGPKSTFTIGKQSGQAVLNSIRAALKSGKITNIKDDAKVVMWGYSGGSLASGWAAALQPSYAPELGGNLLGAALGGFVTNITATAQATDGTVFAGIVANALGGVANEYPEFKSILQSDTDKKSVFDEFDGHCLIDGVLNYIGTSFLTGDHKIFKTGWDILKNPKIGKVVEDNGLVYQKQLVPKIPVFIYHGSIDQIVPIVDTKKTYQNWCDAGISSLEFAEDASNGHLTEAIMGAPAALTWIIDRFDGKQTVSGCQHIQRFSNLEYPNIPSSIANYFKAAMDVVLHLGLGPDVQKDQVSPEGIKKLGSIEMRWL
Protein: Ras-related protein Rab-4A (EC 3.6.5.2) (Q6PHI9)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Small GTPase which cycles between an active GTP-bound and an inactive GDP-bound state (By similarity). Involved in protein transport. Plays a role in vesicular traffic. Mediates VEGFR2 endosomal trafficking to enhance VEGFR2 signaling (By similarity).
Subcellular location: Membrane {ECO:0000250|UniProtKB:P20338}; Peripheral membrane protein {ECO:0000250|UniProtKB:P20338}. Cytoplasm {ECO:0000250|UniProtKB:P20338}. Early endosome membrane {ECO:0000250|UniProtKB:P05714}; Peripheral membrane protein {ECO:0000250|UniProtKB:P05714}. Recycling endosome membrane {ECO:0000250|UniProtKB:P05714}; Peripheral membrane protein {ECO:0000250|UniProtKB:P05714}. Note=Generally associated with membranes. Cytoplasmic when phosphorylated by CDK1. {ECO:0000250|UniProtKB:P20338}.
Interaction partners:
- RUN and FYVE domain-containing 1
- Rabenosyn, RAB effector.
- TBC1 domain family member 16
Sequence:
MSETYDFLFKFLVIGNAGTGKSCLLHQFIEKRFKDDSNHTIGVEFGSKIISVVNKFVKLQIWDTAGQERFRSVTRSYYRGAAGALLVYDITSRETYNALTNWLTDARMLASQNIVIILCGNKKDLDADREVTFLEASRFAQENELMFLETSALTGENVEEAFVQCARKILNKIESGELDPERMGSGIQYGDAALRQLRSPRRAQAESIQECGC
Protein: Disintegrin and metalloproteinase domain-containing protein 19 (ADAM 19) (EC 3.4.24.-) (Meltrin-beta) (Metalloprotease and disintegrin dendritic antigen marker) (MADDAM) (Q9H013)
Organism: Homo sapiens (Human)
Function: Participates in the proteolytic processing of beta-type neuregulin isoforms which are involved in neurogenesis and synaptogenesis, suggesting a regulatory role in glial cell. Also cleaves alpha-2 macroglobulin. May be involved in osteoblast differentiation and/or osteoblast activity in bone (By similarity).
Subcellular location: Membrane; Single-pass type I membrane protein.
Interaction partners:
- SH3 and PX domain-containing protein 2A
- Mitotic spindle assembly checkpoint protein MAD2B
Sequence:
MPGGAGAARLCLLAFALQPLRPRAAREPGWTRGSEEGSPKLQHELIIPQWKTSESPVREKHPLKAELRVMAEGRELILDLEKNEQLFAPSYTETHYTSSGNPQTTTRKLEDHCFYHGTVRETELSSVTLSTCRGIRGLITVSSNLSYVIEPLPDSKGQHLIYRSEHLKPPPGNCGFEHSKPTTRDWALQFTQQTKKRPRRMKREDLNSMKYVELYLVADYLEFQKNRRDQDATKHKLIEIANYVDKFYRSLNIRIALVGLEVWTHGNMCEVSENPYSTLWSFLSWRRKLLAQKYHDNAQLITGMSFHGTTIGLAPLMAMCSVYQSGGVNMDHSENAIGVAATMAHEMGHNFGMTHDSADCCSASAADGGCIMAAATGHPFPKVFNGCNRRELDRYLQSGGGMCLSNMPDTRMLYGGRRCGNGYLEDGEECDCGEEEECNNPCCNASNCTLRPGAECAHGSCCHQCKLLAPGTLCREQARQCDLPEFCTGKSPHCPTNFYQMDGTPCEGGQAYCYNGMCLTYQEQCQQLWGPGARPAPDLCFEKVNVAGDTFGNCGKDMNGEHRKCNMRDAKCGKIQCQSSEARPLESNAVPIDTTIIMNGRQIQCRGTHVYRGPEEEGDMLDPGLVMTGTKCGYNHICFEGQCRNTSFFETEGCGKKCNGHGVCNNNQNCHCLPGWAPPFCNTPGHGGSIDSGPMPPESVGPVVAGVLVAILVLAVLMLMYYCCRQNNKLGQLKPSALPSKLRQQFSCPFRVSQNSGTGHANPTFKLQTPQGKRKVINTPEILRKPSQPPPRPPPDYLRGGSPPAPLPAHLSRAARNSPGPGSQIERTESSRRPPPSRPIPPAPNCIVSQDFSRPRPPQKALPANPVPGRRSLPRPGGASPLRPPGAGPQQSRPLAALAPKVSPREALKVKAGTRGLQGGRCRVEKTKQFMLLVVWTELPEQKPRAKHSCFLVPA