wanglab/gogpt-training-data huggingface dataset:
Protein: L-serine dehydratase TdcG (SDH) (EC 4.3.1.17) (L-serine deaminase) (P42630)
Organism: Escherichia coli (strain K12)
Interaction partners:
- L-threonine dehydratase catabolic TdcB
- Serine hydroxymethyltransferase
- D-serine dehydratase
- Phosphoserine phosphatase
- L-threonine dehydratase biosynthetic IlvA
- CDP-diacylglycerol--serine O-phosphatidyltransferase PssA
- Serine acetyltransferase
- Tryptophan synthase beta chain
- L-serine dehydratase 1
- L-serine dehydratase 2
Sequence:
MISAFDIFKIGIGPSSSHTVGPMNAGKSFIDRLESSGLLTATSHIVVDLYGSLSLTGKGHATDVAIIMGLAGNSPQDVVIDEIPAFIELVTRSGRLPVASGAHIVDFPVAKNIIFHPEMLPRHENGMRITAWKGQEELLSKTYYSVGGGFIVEEEHFGLSHDVETSVPYDFHSAGELLKMCDYNGLSISGLMMHNELALRSKAEIDAGFARIWQVMHDGIERGMNTEGVLPGPLNVPRRAVALRRQLVSSDNISNDPMNVIDWINMYALAVSEENAAGGRVVTAPTNGACGIIPAVLAYYDKFRRPVNERSIARYFLAAGAIGALYKMNASISGAEVGCQGEIGVACSMAAAGLTELLGGSPAQVCNAAEIAMEHNLGLTCDPVAGQVQIPCIERNAINAVKAVNAARMAMRRTSAPRVSLDKVIETMYETGKDMNDKYRETSRGGLAIKVVCG
Protein: Lectin-related NK cell receptor LY49T (Q9JHV2)
Organism: Mus musculus (Mouse)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004606}; Single-pass type II membrane protein {ECO:0000256|ARBA:ARBA00004606}.
Interaction partners:
Sequence:
MSEQEVTYSTMRFHKSSRLQKLVRTEEPQMPREACYRKYSVPWKLIVIACGILCFLLLVTVVLLAIKINKKHELQETLNCNDNCSTTQSDINLMDELLRNKSIECRPGNDLLESLNKEQSRWYSETKTLLDSSQHTGRGFEIYWFCYGIKCYYLIMDRKPWNGCKQSCQNSGLSLLKIDDEDELKFLQLVVPSDSCWIGLSYDNKKKDWAWIDNGPSKLALNTTKYNIRDGGCMLLSKTRLDNDNCDKSFFCICGKRLDKFPH
Protein: Ras-related protein Ral-B (EC 3.6.5.2) (P11234)
Organism: Homo sapiens (Human)
Function: Multifunctional GTPase involved in a variety of cellular processes including gene expression, cell migration, cell proliferation, oncogenic transformation and membrane trafficking. Accomplishes its multiple functions by interacting with distinct downstream effectors. Acts as a GTP sensor for GTP-dependent exocytosis of dense core vesicles (By similarity). Required both to stabilize the assembly of the exocyst complex and to localize functional exocyst complexes to the leading edge of migrating cells (By similarity). Required for suppression of apoptosis. In late stages of cytokinesis, upon completion of the bridge formation between dividing cells, mediates exocyst recruitment to the midbody to drive abscission. Involved in ligand-dependent receptor mediated endocytosis of the EGF and insulin receptors.
Subcellular location: Cell membrane {ECO:0000269|PubMed:17875936}; Lipid-anchor {ECO:0000269|PubMed:17875936}; Cytoplasmic side {ECO:0000269|PubMed:17875936}. Midbody {ECO:0000269|PubMed:18756269}. Note=During late cytokinesis, enriched at the midbody. {ECO:0000269|PubMed:18756269}.
Interaction partners:
- Exocyst complex component 8
- RalA-binding protein 1
- Exocyst complex component 2
- Ral guanine nucleotide dissociation stimulator
- Ral guanine nucleotide dissociation stimulator-like 2
- Phospholipase D1
- Ral guanine nucleotide dissociation stimulator-like 1
- Ras-related protein Ral-A
- Phospholipase D2
- Ras-related C3 botulinum toxin substrate 2
Sequence:
MAANKSKGQSSLALHKVIMVGSGGVGKSALTLQFMYDEFVEDYEPTKADSYRKKVVLDGEEVQIDILDTAGQEDYAAIRDNYFRSGEGFLLVFSITEHESFTATAEFREQILRVKAEEDKIPLLVVGNKSDLEERRQVPVEEARSKAEEWGVQYVETSAKTRANVDKVFFDLMREIRTKKMSENKDKNGKKSSKNKKSFKERCCLL
Protein: Autonomous cohesin (W5IDC3)
Organism: Ruminococcus flavefaciens
Interaction partners:
Sequence:
MGSSSVTADLNNAVINVDEMNEAFKDVPDLEGEGAHITLSNTTAKPGEMAEVTMSVSNADMQWNMCGIHIIYPDILKPEMKDPEERTVAFQKGDALEAATGIVCMEWQEGLPPVLTENKKGCLFLTAMFSGNQGGEGDMATFRFKVPDNAEPGAVYNLGYYYMNTDLFINEQNIPTYQKYAFTHMEGGTITVELEHHHHHH
Protein: SEC14 and spectrin domain containing 1 (C9J4X8)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MEASVILPILKKKLAFLSGGKDRRSGLILTIPLCLEQTNMDELSVTLDYLLSIPSEKCKARGFTVIVDGRKSQWNVVKTVVVMLQNVVPAEVSLVCVVKPDEFWDKKVTHFCFWKEKDRLGFEVILVSANKLTRYIEPCQLTE
Protein: Pyruvate dehydrogenase E1 component subunit beta, mitochondrial (PDHE1-B) (EC 1.2.4.1) (Q9D051)
Organism: Mus musculus (Mouse)
Function: The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2), and thereby links the glycolytic pathway to the tricarboxylic cycle.
Subcellular location: Mitochondrion matrix {ECO:0000250}.
Interaction partners:
- Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial
- 2-oxoisovalerate dehydrogenase subunit alpha, mitochondrial
- Pyruvate dehydrogenase E1 component subunit alpha, testis-specific form, mitochondrial
- Pyruvate dehydrogenase E1 component subunit alpha, somatic form, mitochondrial
- Dihydrolipoyl dehydrogenase, mitochondrial
- Pyruvate dehydrogenase protein X component, mitochondrial
- Pyruvate kinase PKM
- Pyruvate carboxylase, mitochondrial
- Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex, mitochondrial
- [Pyruvate dehydrogenase
Sequence:
MAVVAGLVRGPLRQASGLLKRRFHRSAPAAVQLTVREAINQGMDEELERDEKVFLLGEEVAQYDGAYKVSRGLWKKYGDKRIIDTPISEMGFAGIAVGAAMAGLRPICEFMTFNFSMQAIDQVINSAAKTYYMSAGLQPVPIVFRGPNGASAGVAAQHSQCFAAWYGHCPGLKVVSPWNSEDAKGLIKSAIRDNNPVVMLENELMYGVAFELPAEAQSKDFLIPIGKAKIERQGTHITVVAHSRPVGHCLEAAAVLSKEGIECEVINLRTIRPMDIEAIEASVMKTNHLVTVEGGWPQFGVGAEICARIMEGPAFNFLDAPAVRVTGADVPMPYAKVLEDNSVPQVKDIIFAVKKTLNI
Protein: Uncharacterized amino-acid permease C359.01 (Q9P5N4)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Ribose-phosphate pyrophosphokinase 1
Sequence:
MSHSDYNFDIEQNAFEKEAPKVSIERKGDVVEEEVIATGEVENYAEPKSRNFLQRFFDDFKPALTTRGDGVALKRKLTSRHMQMISVGGAIGSGLYVGSGSAFADGGPASVIINYILIGIMMIFVIYALGELAIAYPVAGSFNTYATRFIDPAWGFAVSWNYFLNYFVTCPLELTTCAITFKFWTEINSAAWISIFLAVVIVINLFGVRAYGEVEFILSTIKVIATVGFIILAIIINCGGVPTDHRGYIGGSIIKQKPFRHGFKGFCSVFTTAAFSFSGTEIIGLAAAEVGNPRKSVPSAVKQVFWRIAIFYVVSLILIGLLVSPDDPRLMGNGDVSVSPFVLAIQEANIKGLPSVFNAVIIISVVSVTNSTTYTAARTLQGMATLKQAPKFFSYTDRVGRPLIAMVVVLLFGFFAYINEADKNGSDISDTVFDWLLAISGLSSFFTWGSICLSHIMFRLAFKKQGHSLKELGFVSPMGIWGSVIGLGFNILCLMAEFYVSLFLIGGSPNANDFFQGYLAACIALAFFIGYKIYDRSHIPSLDKLDIDTGLKTYDNQDEEKEEYSSKGPLNILKKAWNAVC
Protein: Nudix hydrolase 11 (AtNUDT11) (EC 3.6.1.-) (Coenzyme A diphosphatase NUDT11) (Q8LET2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Coenzyme A diphosphatase which mediates the cleavage of CoA into 3',5'-ADP from CoA and 4'-phosphopantetheine. Can use malonyl-CoA, hexanoyl-CoA, lauroyl-CoA, myristoyl-CoA and palmitoyl-CoA as substrates, but not isobutyryl-CoA or propionyl-CoA.
Subcellular location: Peroxisome membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
- Nudix hydrolase 1
- Nudix hydrolase 10
- Nudix hydrolase 4
- Nudix hydrolase 12, mitochondrial
- Nudix hydrolase 25
- Nudix hydrolase 14, chloroplastic
- Nudix hydrolase 13, mitochondrial
- Pyridoxine/pyridoxamine 5'-phosphate oxidase 1, chloroplastic
- mRNA-decapping enzyme-like protein
- Nudix hydrolase 5
Sequence:
MSSTTTDSTELQNLIKLFQNCQTHPRQHFPAKSSAVLVCLYQEQREDKNELRVILTKRSTTLSSHPGEVALPGGKRDQEDKDDIATALREAREEIGLDPSLVTIISVLEPFVNKKGMSVAPVIGFLHDKKAFKQLPNPAEVEEIFDVPLEMFLKDRNRRAEEREHEGERYLLQYFDYYSEDKERSFIIWALTAGILIRVASIVYQRLPEFQERKPSFWNQPN
Protein: Fatty acyl-CoA reductase 3 (EC 1.2.1.84) (Protein ECERIFERUM 4) (Q93ZB9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes the reduction of fatty acyl-CoA to fatty alcohols. The preferred substrates are C24:0 and C26:0. May be unable to use saturated and monounsaturated C16 and C18 acyl-CoA as substrates. Involved in cuticular wax formation.
Subcellular location: Endoplasmic reticulum {ECO:0000305|PubMed:16980563}.
Interaction partners:
- Wax ester synthase/diacylglycerol acyltransferase 1
- Very-long-chain 3-oxoacyl-CoA reductase 1
- Very-long-chain aldehyde decarbonylase CER1
- Alkane hydroxylase MAH1
- Very-long-chain enoyl-CoA reductase
- Protein ECERIFERUM 2
- 3-ketoacyl-CoA synthase 6
- Fatty acyl-CoA reductase
- Very-long-chain aldehyde decarbonylase CER3
- Ethylene-responsive transcription factor WIN1
Sequence:
MSTEMEVVSVLKYLDNKSILVVGAAGFLANIFVEKILRVAPNVKKLYLLLRASKGKSATQRFNDEILKKDLFKVLKEKYGPNLNQLTSEKITIVDGDICLEDLGLQDFDLAHEMIHQVDAIVNLAATTKFDERYDVALGINTLGALNVLNFAKRCAKVKILVHVSTAYVCGEKSGLIMETPYRMGETLNGTTGLDINYEKKLVQEKLDQLRVIGAAPETITETMKDLGLRRAKMYGWPNTYVFTKAMGEMMVGTKRENLSLVLLRPSIITSTFKEPFPGWTEGIRTIDSLAVGYGKGKLTCFLCDLDAVSDVMPADMVVNSILVSMAAQAGKQEEIIYHVGSSLRNPMKNSKFPELAYRYFSIKPWTNKEGKVVKVGAIEILSSMRSFHRYMTIRYLIALKGLELVNIILCKLFEKEFQYFNKKINFIFRLVDLYQPYLFFYGIFDDSNTEKLRKMVSKTGVENEMFYFDPKVLDWDDYFLNTHVIGLLKYVF
Protein: Proteasome subunit alpha type (Q5AEB8)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Subcellular location: Cytoplasm {ECO:0000256|RuleBase:RU000551}. Nucleus {ECO:0000256|RuleBase:RU000551}.
Interaction partners:
- Proteasome regulatory particle base subunit
- Proteasome subunit beta
- Proteasome subunit alpha type
- 26S proteasome regulatory subunit 8 homolog
- 26S proteasome regulatory subunit RPN8
- Proteasome regulatory particle base subunit
- proteasome endopeptidase complex
- Proteasome regulatory particle lid subunit
- Proteasome subunit beta
- Proteasome subunit alpha type
Sequence:
MSRRYDSRTTIFSPEGRLYQVEYAQEAISNAGTAIGILSPEGVVLACEKKVTSKLLDDDGSAEKLYIINDQMICAVAGMTADASILVNNARIQAQQYLKLYDEEIPCEMLINRVCDVKQGYTQHGGLRPFGVSFLYAGYDDRYQFQLFTSNPSGNYSGWKATSIGANNSAAQTLLKKDYKDDLTLKDACELAIKVLSKTMDASNINSEKLEFATLSLGKDNKVLHKIWNDKDIDILIKASGVLNEKNSDDE
Protein: Peroxiredoxin-2B (EC 1.11.1.25) (Glutaredoxin-dependent peroxiredoxin) (Peroxiredoxin IIB) (Peroxiredoxin TPx1) (Thioredoxin peroxidase 2B) (Thioredoxin-dependent peroxidase 1) (Q9XEX2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Reduces hydrogen peroxide and alkyl hydroperoxides with reducing equivalents provided through the thioredoxin or glutaredoxin system. May be involved in intracellular redox signaling.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:12913160}.
Interaction partners:
- 2-Cys peroxiredoxin BAS1-like, chloroplastic
- Peroxiredoxin Q, chloroplastic
- Thioredoxin H2
- 1-Cys peroxiredoxin PER1
- 2-Cys peroxiredoxin BAS1, chloroplastic
- Glutaredoxin-C4
- CAP superfamily protein
Sequence:
MAPIAVGDVVPDGTISFFDENDQLQTASVHSLAAGKKVILFGVPGAFTPTCSMKHVPGFIEKAEELKSKGVDEIICFSVNDPFVMKAWGKTYPENKHVKFVADGSGEYTHLLGLELDLKDKGLGVRSRRFALLLDDLKVTVANVESGGEFTVSSADDILKAL
Protein: Transposase InsH for insertion sequence element IS5Y (P76071)
Organism: Escherichia coli (strain K12)
Function: Involved in the transposition of the insertion sequence IS5.
Interaction partners:
- Transposase InsH for insertion sequence element IS5R
- Transposase InsH for insertion sequence element IS5H
Sequence:
MSHQLTFADSEFSTKRRQTRKEIFLSRMEQILPWQNMTAVIEPFYPKAGNGRRPYPLETMLRIHCMQHWYNLSDGAMEDALYEIASMRLFARLSLDSALPDRTTIMNFRHLLEQHQLARQLFKTINRWLAEAGVMMTQGTLVDATIIEAPSSTKNKEQQRDPEMHQTKKGNQWHFGMKAHIGVDAKSGLTHSLVTTAANEHDLNQLGNLLHGEEQFVSADAGYQGAPQREELAEVDVDWLIAERPGKVKTLKQNPRKNKTAINIEYMKASIRARVEHPFRIIKRQFGFVKARYKGLLKNDNQLAMLFTLANLFRVDQMIRQWERSQ
Protein: Transducin/WD40 repeat-like superfamily protein (F4J6P6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- DNA damage-binding protein 1a
- YCF49-like protein
- DNA damage-binding protein 1b
- Protein ALTERED SEED GERMINATION 2
- Transducin/WD40 repeat-like superfamily protein
- Cullin-4
- WD repeat-containing protein 76
- Protein DAMAGED DNA-BINDING 2
- Uncharacterized mitochondrial protein AtMg00810
- Transducin/WD40 repeat-like superfamily protein
Sequence:
MARPRRRNTEIGDGFTEIFNREIGFSHPITISRRISASEFRIMDLSVPKTKCYGLSVFCRMLRKSEPIQRLISGRVKKLDLYGKLNGHEGCVNAVEFNSTGDVLVSGSDDRQIMLWNWLSGSRKLSYPSGHCENVFQTKFIPFTDDRTIITSGADGQVRLGQILENGKVETKRLGRHHGRVYKLAVLPGDPNVFYSCGEDGFVQHFDIRSNSATMVLYSSPFTQGCRRHHSSSRIRLNSIAIDPRNSYYLAVGGSDEYARVYDTRRVQLAPVCRHVLPDAPVNTFCPRHLRETNSVHITGLAYSKAGELLVSYNDELIYLFEKNMGYGSSPVSVSPEKLQEMEEPQVYIGHRNAQTVKGVNFFGPNDEYVTSGSDCGHIFIWKKKGGKLVRAMVGDRRVVNQLESHPHIPLLASCGIEKSVKLWTPMSNDVLSLPEKIDKVMELNRVGREDQSRVTLTPDVIMHVLRLQRRQTSAFTERRYVSTDIGSDEGNDARFIASLVANDDESSDRECTVS
Protein: Mannosyl-oligosaccharide glucosidase (EC 3.2.1.106) (Processing A-glucosidase I) (Q13724)
Organism: Homo sapiens (Human)
Function: Cleaves the distal alpha 1,2-linked glucose residue from the Glc(3)Man(9)GlcNAc(2) oligosaccharide precursor in a highly specific manner.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:7635146}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:O88941}.
Interaction partners:
- Neutral alpha-glucosidase AB
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase 48 kDa subunit
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit TUSC3
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 1
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit STT3A
- ADP-ribosylation factor GTPase-activating protein 1
- Calnexin
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit STT3B
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 2
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit DAD1
Sequence:
MARGERRRRAVPAEGVRTAERAARGGPGRRDGRGGGPRSTAGGVALAVVVLSLALGMSGRWVLAWYRARRAVTLHSAPPVLPADSSSPAVAPDLFWGTYRPHVYFGMKTRSPKPLLTGLMWAQQGTTPGTPKLRHTCEQGDGVGPYGWEFHDGLSFGRQHIQDGALRLTTEFVKRPGGQHGGDWSWRVTVEPQDSGTSALPLVSLFFYVVTDGKEVLLPEVGAKGQLKFISGHTSELGDFRFTLLPPTSPGDTAPKYGSYNVFWTSNPGLPLLTEMVKSRLNSWFQHRPPGAPPERYLGLPGSLKWEDRGPSGQGQGQFLIQQVTLKIPISIEFVFESGSAQAGGNQALPRLAGSLLTQALESHAEGFRERFEKTFQLKEKGLSSGEQVLGQAALSGLLGGIGYFYGQGLVLPDIGVEGSEQKVDPALFPPVPLFTAVPSRSFFPRGFLWDEGFHQLVVQRWDPSLTREALGHWLGLLNADGWIGREQILGDEARARVPPEFLVQRAVHANPPTLLLPVAHMLEVGDPDDLAFLRKALPRLHAWFSWLHQSQAGPLPLSYRWRGRDPALPTLLNPKTLPSGLDDYPRASHPSVTERHLDLRCWVALGARVLTRLAEHLGEAEVAAELGPLAASLEAAESLDELHWAPELGVFADFGNHTKAVQLKPRPPQGLVRVVGRPQPQLQYVDALGYVSLFPLLLRLLDPTSSRLGPLLDILADSRHLWSPFGLRSLAASSSFYGQRNSEHDPPYWRGAVWLNVNYLALGALHHYGHLEGPHQARAAKLHGELRANVVGNVWRQYQATGFLWEQYSDRDGRGMGCRPFHGWTSLVLLAMAEDY
Protein: Homocysteine-induced endoplasmic reticulum protein, isoform A (Homocysteine-induced endoplasmic reticulum protein, isoform C) (RE13884p) (Q9VLW9)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004370}.
Interaction partners:
- alpha-1,2-Mannosidase
- Protein TRC8 homolog
Sequence:
MEENAAPPAAATAAGCDAATRQKNPETSVRLLIKSSNQQYEDLNVDSDLCWTVQRLKKHLSLIYPGKPLIQDQKLIYSGKLLDDSQKISEVIRSYKDVYQQHHIFHLVCASKQVIRPAAKAPTVPQKDAVPAGPEVTGNANELRQRHAPHQQQAQQGNAGPHVTGDIGLANPWTHFWQQSQGAAPAANASASPHALFQQQALIYNAWMQQAYAQYMQQLTLRSTLPGSNQSGLPPPTQPLLPSVPLIAGRNFGEVQQVAGAAAAPAAQVPADPQINGAPQNRNFPNIQEEPEMHDWLDSFFSFTRLAIFVTVLYFNSSALRCLLVVLIAGAIYLYHIGVLRRRRERNNNNINRNNNAGDAAAFAAVQQIQRMMDAAVQRENNDPQAANEPGAVPAAGPAAAGEQDAIDAPPAGAPVAPASAANPEPTDVSAEAVEPPNANNSVISVVRTFVITFFTSLLPEAPAL
Protein: Serum amyloid A like 1 (E9PRZ1)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MDRNPSPPPPGRDKEEEEEVAGGDCIGSTVYSKHWLFGVLSGLIQIVSPENTKSSSDDEEQLTELDEEMENEICRVWDMSMDEDVALFLQEFNAPDIFMGVLAKSKCPRLREICVGILGNMACFQEICVSISSDKNLGQVLLHCLYDSDPPTLLETSRLLLTCLSQAEVASVWVERIQEHPAIYDSICFIMSSSTNVDLLVKVGEVVDKLFDLDEKLMLEWVRNGAAQPLDQPQEESEEQPVFRLVPCILEAAKQVRSENPEWLDVYMHILQLLTTVDDGIQAIVHCPDTGKDIWNLLFDLVCHEFCQSDDPPIILQEQKTVLASVFSVLSAIYASQTEQEYLKIEKGKYNLPLIDSLIRVLQNMEQCQKKPENSAESNTEETKRTDLTQDDFHLKILKDILCEFLSNIFQALTKETVAQGVKEGQLSKQKCSSAFQNLLPFYSPVVEDFIKILREVDKALADDLEKNFPSLKVQT
Protein: Cyclin-dependent kinases regulatory subunit 1 (CKS-1) (P61024)
Organism: Homo sapiens (Human)
Function: Binds to the catalytic subunit of the cyclin dependent kinases and is essential for their biological function.
Interaction partners:
- Cyclin-dependent kinase 2
- Cyclin-dependent kinase 1
- S-phase kinase-associated protein 1
- S-phase kinase-associated protein 2
- Cyclin-A2
- G2/mitotic-specific cyclin-B1
- Cullin-1
- Cyclin-dependent kinase inhibitor 1B
- Cyclin-dependent kinases regulatory subunit 2
- E3 ubiquitin-protein ligase RBX1
Sequence:
MSHKQIYYSDKYDDEEFEYRHVMLPKDIAKLVPKTHLMSESEWRNLGVQQSQGWVHYMIHEPEPHILLFRRPLPKKPKK
Protein: Eukaryotic translation initiation factor 3 subunit E (AtEIF3E-1) (eIF3e) (p48) (Eukaryotic translation initiation factor 3 subunit 6) (AtINT6) (INT-6) (Q9C5Z3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is involved in protein synthesis of a specialized repertoire of mRNAs and, together with other initiation factors, stimulates binding of mRNA and methionyl-tRNAi to the 40S ribosome. The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation (Potential). Regulates negatively translation during flower development.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03004, ECO:0000269|PubMed:11029466}. Nucleus {ECO:0000269|PubMed:11029466}.
Interaction partners:
- Eukaryotic translation initiation factor 3 subunit B
- Eukaryotic translation initiation factor 3 subunit H
- Eukaryotic translation initiation factor 3 subunit I
- Eukaryotic translation initiation factor 3 subunit J
- Eukaryotic translation initiation factor 3 subunit D
- Eukaryotic translation initiation factor 3 subunit J
- Eukaryotic translation initiation factor 3 subunit L
- Eukaryotic translation initiation factor 3 subunit F
- Eukaryotic translation initiation factor 3 subunit A
- Eukaryotic translation initiation factor 3 subunit C
Sequence:
MEESKQNYDLTPLIAPNLDRHLVFPIFEFLQERQLYPDEQILKSKIQLLNQTNMVDYAMDIHKSLYHTEDAPQEMVERRTEVVARLKSLEEAAAPLVSFLLNPNAVQELRADKQYNLQMLKERYQIGPDQIEALYQYAKFQFECGNYSGAADYLYQYRTLCSNLERSLSALWGKLASEILMQNWDIALEELNRLKEIIDSKSFSSPLNQVQNRIWLMHWGLYIFFNHDNGRTQIIDLFNQDKYLNAIQTSAPHLLRYLATAFIVNKRRRPQLKEFIKVIQQEHYSYKDPIIEFLACVFVNYDFDGAQKKMKECEEVIVNDPFLGKRVEDGNFSTVPLRDEFLENARLFVFETYCKIHQRIDMGVLAEKLNLNYEEAERWIVNLIRTSKLDAKIDSESGTVIMEPTQPNVHEQLINHTKGLSGRTYKLVNQLLEHTQAQATR
Protein: KRAB zinc finger protein (Zinc finger protein 119) (Q9JIC0)
Organism: Mus musculus (Mouse)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MDAVTYEDVHVNFSREEWVLLDPSQKSLYKDVMLETYWNLTCIGYKWKDHDNEEYCQNSGRHGRCINCPSAYGKKQCTNLFPRTIRRRYVVTPFVRRGGECDTSLQVLGFPASVGIHQNTDLGEKPSADKESGKPLVCPGSLCTCSVTHTIGECCECNQCGKALSSSCSLQRRDQTHMGKGSDKCEPSSKSLTHPRYLQIQKTAYNEEDLYVWNQCGKSSLQLHRRTHLEMKYSECNQGDKSFAFYNHHQVGRSNTTEKNYEYNQWGKAFSYPSYLQVHETIHTGKSPYECNQCGKTFAYKSHFHKHERIHTGEKPYECNRCGKAFSSNSNLQRHERIHTGEKPYECSQCGKAFAYRNSLHIHERNHTGEKPYKCYQCGKDFASNSNLQIHRRVHSGEKPYKCFECGKHFSCNSHLQMHERIHTGEKPYKCNQCGKTFAYSSSFHMHERTHTGEKPYECNQCGKAFAYCCHLQRHERCHTGEKPYECNQCGKAFAYLSSLHKHERNHTGEKLFECNQCGKVFACLSTLQEHKRIHTDKIPKETNK
Protein: Solute carrier family 16 member 7 (F8VS95)
Organism: Homo sapiens (Human)
Subcellular location: Basolateral cell membrane {ECO:0000256|ARBA:ARBA00004554}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004554}.
Interaction partners:
Sequence:
MGFITGLGLAFNLQPALTIIGKYFYRKRPMANGLAMAGSPVFLSSLAPFNQYLFNTFGWKGSFLILGSLLLNACVAGSLMRPLGPNQTTSKSKNKTGKTEDDSSPKKIKTKKSTWEKVNKYLDFSLFKHRG
Protein: Expressed protein (Transmembrane protein (DUF788)) (O82222)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004477}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004477}.
Interaction partners:
- Autophagy-related protein 9
Sequence:
MANQGAKKRKEENAKHMAKLRRIIIASNAVYFVVRMLIFYSSFTWKHWIGLVITSLAYAFPYKQLDQMAKPSVTDDGELIDGGFDMTTGGICGYLHDVIYITCFVQLASIITGKFWYTYLVIPAFGVYKASGLIRGFMSQGSEGGVEDEKSRKKREKMERKASRGQVVKTRTR
Protein: T. brucei spp.-specific protein (Q382Q8)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MSCLHGGGTPLRVAFPSPCMAEFDRIRTSMERVENLLNESMTLLCGYRSVRLAWGETNSVSGFNGGNSPSPTGTTSLKGFSATSGKSSRHRSTSSAVSGPKPKAGRPSNAAFDIVDDRMDISLTALRNRIRAELNDYCRFGLAACCHKPG
Protein: Laminin subunit beta 1 (A0A8I6A3T2)
Organism: Rattus norvegicus (Rat)
Subcellular location: Secreted, extracellular space, extracellular matrix, basement membrane {ECO:0000256|ARBA:ARBA00004302}.
Interaction partners:
Sequence:
SGALHIYQLNAVSPPWKASLWGTRVCAQEPEFSYGCAEGSCYPATGDLLIGRAQKLSVTSTCGLHKPEPYCIVSHLQEDKKCFICDSRDPYHETLNPDSHLIENVVTTFAPNRLKIWWQSENGVENVTVQLDLEAEFHFTHLIMTFKTFRPAAMLIERSSDFGKTWGVYRYFAYDCESSFPGISTGPMKKVDDIICDSRYSDIEPSTEGEVIFRALDPAFKIEDPYSPRIQNLLKITNLRIKFVKLHTLGDNLLDSRMEIREKYYYAVYDMVVRGNCFCYGHASECAPVDGFNEEVEGMVHGHCMCRHNTKGLNCELCMDFYHDLPWRPAEGRNSNACKKCNCNEHSSSCHFDMAVFLATGNVSGGVCDNCQHNTMGRNCEQCKPFYFQHPERDIRDPNLCEPCTCDPAGSENGGICDGYTDFSVGLIAGQCRCKLHVEGERCDVCKEGFYDLSAEDPFGCKSCACNPLGTIPGGNPCDSETGYCYCKRLVTGQRCDQCLPQHWGLSNDLDGCRPCDCDLGGALNNSCSEDSGQCSCLPHMIGRQCNEVESGYYFTTLDHYIYEAEEANLGPGVVVVERRYIQDRIPSWTGPGFVRVPEGAYLEFFIDNIPHSMEYEILIRYEPQLPDHWEKAVITVQRPGRIPTSSRCGNTVPDDDNQVVSLSPGSRYVVLPRPVCFEKGMNYTVRLELPQYTASGSDVESPYTLIDSLVLMPYCKSLDIFTVGGSGDGEVTNSAWETFQRYRCLENSRSVVKTPMTDVCRNIIFSISALIHQAGLACECDPQGSLSSVCDPNGGQCQCRPNVVGRTCNRCAPGTFGFGPNGCKPCDCHLQGSVSAFCDAVTGQCHCFQGIYARQCDRCLPGFWGFPSCQPCQCNGHAEDCDTVTGECLSCQDYTTGHNCERCLAGYYGDPIIGSGDHCRPCPCPDGPDSGRQFARSCYQDPVTLQLACVCDPGYIGSRCDGCASGYFGNPSDFGGSCQPCQCHHNIDTTDPEACDKETGRCLKCLYHTEGDHCQFCQHGYYGDALRQDCRKCVCNYLGTVREHCNGSDCHCDKTTGQCSCLPNVIGQNCDRCAPHTWQLASGTGCEPCNCNAVHSFGPSCNEFTGQCQCMPGFGGRTCSECQELFWGDPDVECRACDCDPRGIETPQCDQSTGQCVCVEGVEGPRCDKCTRGYSGVFPDCTPCHQCFALWDVIIGELTNRTHKFLEKAKALKISGVIGPYRETVDSVEKKVNEIRDILAQSPAAEPLKNIGILFEEAEKLTKDVTEKMAQVEVKLSDTASRSNSTAGELDALQAEAGSLDKTVNELAEQLEFIKNSDIQGALDSITKYFQISLEAEKRVNASTTDPNSTVEQSALTRDRVEDLMLERESQFKEKQEEQARLLDELAGKLQSLDLSAAAEMTCGTHPGADCSESECGGPNCRTDEGEKKCGGPGCGGLVTVAHSAWQKAMDFDRDVLNALAEVEQLSKMVSEAKVRADEAKQNAQDVLLKTNATREKVDRSNEDLRNLIKQIRDFLTEDSADLDSIEAVANEVLKMEMPSTPQQLQNLTEDIRERVETLSQVEVILQQSAADIARAELLLEEAKRASKSATDVKVTADMVKEALEEAEKAQVAAEKAIKQADEDIQGTQNLLTSIESETAASEETLTNASQRISKLERNVEELKRKAAQNSGEADYIEKVVYSVKQSADEVKKTLDGELDEKYKKVESLIAQKTEESADARRKAELLQNEAKTLLAQANSKLQLLEDLERKYEDNQKYLEDKAQELVRLEGEVRSLLKDISEKVAVYSTCL
Protein: Terminal uridylyltransferase 3 (TUTase 3) (EC 2.7.7.52) (3' terminal uridylyl transferase) (RNA editing 3' terminal uridylyltransferase 3) (Q6B9Y8)
Organism: Trypanosoma brucei brucei
Function: Terminal uridylyltransferase which catalyzes the addition of Us to the 3'-hydroxyl group of single-stranded RNAs. Does not mediate RNA-independent UTP polymerization.
Subcellular location: Cytoplasm {ECO:0000305|PubMed:15304317}.
Interaction partners:
Sequence:
MIFFFKKRYHVFLKAPSIRLMPCSFFFFRSFIKVIFIIRCIFFSSLSGDSCPTQRSRSTLACMFTSVPVAPTVVPGVVYSSGVHEEWKEAEQKLLDGCLIHSEGDGATKQIKEKLTSRNSQSVRCDLCAKMIESRDEEQIQEHFQVHHAALSLWCREILASKDNLLHYGCIPSGHIVSCGNFVLESAATLDMGRKTFDVIERAFSQMSQVISCFVRNLVLFPFGSCVSCGCWDGVSDADFTAIGLQDMKKGKWPPEDEKKVILRLTAALRKAGFFFGELEPLVRTRVPVVRRVQKVRVPLRSHGEHDTYSVVWSNSKEFSSPPRMLVEAAISSTVERKDSDTVTFHFKDSLKAVKFFCNSAMCGPRDMEVSWKTGSQLPEMFSLDFDLSCRAQGVRNSLFLRKYFQQDPFVRTGYLFLKKWSKLYGINNAKNGYLTSYAMSILWVHFLLENGLVKFVRPADVEPIPDLSQQKMSYLPLLRDDGDGGERPSDVLKSPELTMLRGALGGLIPLFFLYYTRIRWDKVVVTLRVPGGGPPVTPDSLGWVEANEVKCGPLRDRVWYRLCIDDPYEDNFNLGRHLSPDKASFVKVQFMRALASIVAGRPQQLLVDEQKFAEETMPAYVTRLSVQGELRNLRPVTVSALRQLLIDSAGADCVAIYEASHNWETLLDMASTLNNKSKEGDDDAEGVTNNQEGEPPDHVESCEAPRRHLLCSKMHSIDDALLVAGPLGVSDANIPAGLLGVYFLARGRAFRTAEDRDNFLMHAEAVSAARARGCTTREEILERVADAIPSIVRNGTLLDDLLVSGSEENITVQSPVVVETRCAETVQRKKSKGSKKRKNAVRRGNHAGQGTCSECGASGTDLWEASDKSADDGLYCGACWKAYNCQKN
Protein: Uncharacterized protein (Q583D3)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MSTRCAQQRDGMSLRCRSGRRGFHILDGPDTCRRSGVGTRGSRTPDTKSSPISARRAFSCVGIRTRSPNSCMGTRRRLTRDVMPRSCRTPSPRARSQRQQACRGQNHWTPERNSTCGNVKDDNAGNNNSDNSIVSASTADIANDPKGEPGVAVKKREENLTLKDVEELRRRREQLRYGVDTSLSRITELQLLTQSFRSGQRNTTGEGSNSLSATAVSAAAVGDGATGSVDNDEMTARPTFAEDYDTTSGKEEALLFLHAAEEEYIEFRLQLTLANAALSAVPQSLWADIRRFRQPPPAVAAVMDAMLILLGFPRIRRMRLSFGSGGWPSLPQQLIRCEPLTAYLNIAELTGRDSQINGCSPLEELEQFLRQWTHLRVSRVHPTLGPLHQWVKAMLDASRAAGRLKTLRDASRAADITPVTDRVALLRELEENEEYVQLAQEEIRAIDALVADVAAAGAKGHYRTSLNPGSLYSPRGSVAGGIRETGELAEKVGGAAAGRFGAARTSGKEVSRNRRLQNSCPTAPRFGAKAALAAGGLGSLKADPARPTLSFKACMSSFNQVEQGPRSLRERFERLKTSSLCHSPRVGPGSHLEGSTARDGLGCSTEVVNSIGGVSLLGTTRVFRDREKLLLRVHQLEEQLSDICSNQPGEVELVLMRDELAATQDEVNKLRKERDELQQRLKRYEAYDGPPSPRRSIARRLNHNIANTDEDASTAIASGEIMTIMALEQQLRAAHTRIQHLESVMMGATSDDGTRCTSASGSGNESPETPYDSTVRPCNLAASNLGHNASSLGEMVFLQRRLDDMQQSLEVQQCAVSEAEERLNNEMHAKNEAQQLVRQLQAELRSVWQKLEITEYQLKLALEGSHCHRSCMDGNNLGTEFIRDLQRQRQREAICEGEIERLRMQLREQKERSAEGRRRRLEIRRVRTALLLKLENALSEALRQHEG