wanglab/gogpt-training-data huggingface dataset:
Protein: Ammonium-dependent carbamoyl phosphate synthetase (EC 6.3.4.16) (EC 6.3.5.5) (Arginine-specific carbamoyl phosphate synthetase, ammonia chain) (Glutamine-dependent carbamoyl phosphate synthetase) (Q5B0D1)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Interaction partners:
- Argininosuccinate synthase
- Amidophosphoribosyltransferase
- Carbamoyl phosphate synthase arginine-specific small chain
- Ornithine carbamoyltransferase, mitochondrial
- Acetylglutamate kinase
- Glutamate synthase
- glutamine--fructose-6-phosphate transaminase
- Glutamine synthetase
- Glutamine synthetase
- Dihydroorotate dehydrogenase
Sequence:
MVLAARCGQATSSLLRQRCLAETRRSALALRSFTSPSTTRSTASALRLQQKTPSPWRSQQLRNFSSALCRLAAESSSVGDSLFSSGIVNPGANLVDVKKVLVIGSGGLSIGQAGEFDYSGSQALKALKEAGVQSVLINPNIATIQTDHKLADEVYYLPVTPEYVTYVIERERPDGIFLSFGGQTALNLGVQMNRMGTFERYGVRVLGTSIKTLETSEDRDLFAKALNEINIPIAESIAVGTVDEALKAADEVGYPIIVRSAYALGGLGSGFANNPEELKNLASRSLTLSPQILVEKSLRGWKEVEYEVVRDASNNCITVCNMENFDPLGIHTGDSIVVAPSQTLSDEEYHMLRTAAIKIVRHLGVVGECNVQYALQPDGLDYRVIEVNARLSRSSALASKATGYPLAYTAAKIGLGHTLPELPNAVTKTTTANFEPSLDYIVTKIPRWDLSKFQHVNRDIGSAMKSVGEVMAIGRTFEESFQKAIRQVDPRFVGFQGDKFENLDEVLKNPTDRRWLAVGQAMLHENYSVDKVHELTKIDKWFLYKLQNIVDNHNELKEIGSLFGVNKELMLKSKKLGFSDKQIAQLVGASEDDVRARRKGFGIRPWVKKIDTLAAEFPADTNYLYTTYNATSHDVTFDDHGTIILGSGVYRIGSSVEFDWCAVNATLSLRNMGKKTVMINYNPETYSTDFDTADKLYFEELSYERVMDIYELESASGVVVSVGGQLPQNIALRLQETGGANVLGTNPKDIDNAEDRHKFSQILDSIGVDQPAWKELTSVAEAERFAEAVGYPVLVRPSYVLSGAAMSVIHSQDELKEKLLNASAVSPDHPVVITKFIEGAQEIDVDAVASNGKLLLHAISEHVEPAGVHSGDATLVLPPASLEKPVMSRVKEIAEKVAKAWNITGPFNMQIIKADQEGAEPQLKVIECNLRASRSFPFVSKVLGTNFIDVATKALVGRDVPEPVDLMEVKRDYLATKVPQFSWTRLAGADPFLGVEMASTGEIACFGKDVVEAYWASLQSTMNFRVPEPGEGILLGGDITNPALAQIVDLLHPLGFKFFAASPEVKAHIESATKEHTPVQVIEFPKKDKRALREVFQKYDIRGCFNLAKTRGKTLLDEDYVMRRNAVDFGVPLFMETKTAQLFAQAMNQKLPRPEGIPSEVRTWSNFVGGKLL
Protein: Histone-lysine N-methyltransferase EZH2 (EC 2.1.1.356) (A0A8I6GAA5)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MGQTGKKSEKGPVCWRKRVKSEYMRLRQLKRFRRADEVKTMFSSNRQKILERTETLNQEWKQRRIQPVHIMTSVSSLRGTREVEDETVLHNIPYMGDEVLDQDGTFIEELIKNYDGKVHGDRECGFINDEIFVELVNALGQYNDDDDDDDGDDPDEREEKQKDLDDSRDDKETCPPRKFPADKIFEAISSMFPDKGTAEELKEKYKELTEQQLPGALPPECTPNIDGPNAKSVQREQSLHSFHTLFCRRCFKYDCFLHPFHATPNTYKRKNTETALDNKPCGPQCYQHLEGAKEFAAALTAERIKTPPKRPGGRRRGRLPNNSSRPSTPTISVLESKDTDSDREAGTETGGENNDKEEEEKKDETSSSSEANSRCQTPIKMKPNIEPPENVEWSGAEASMFRVLIGTYYDNFCAIARLIGTKTCRQVYEFRVKESSIIAPVPTEDVDTPPRKKKRKHRLWAAHCRKIQLKKDGSSNHVYNYQPCDHPRQPCDSSCPCVIAQNFCEKFCQCSSECQNRFPGCRCKAQCNTKQCPCYLAVRECDPDLCLTCGAADHWDSKNVSCKNCSIQRGSKKHLLLAPSDVAGWGIFIKDPVQKNEFISEYCGEIISQDEADRRGKVYDKYMCSFLFNLNNDFVVDATRKGNKIRFANHSVNPNCYAKVMMVNGDHRIGIFAKRAIQTGEELFFDYRYSQADALKYVGIEREMEIP
Protein: WD repeat domain-containing protein 83 (Mitogen-activated protein kinase organizer 1) (Q9VJL9)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
- Splicing factor 3B subunit 4
- Pre-mRNA-processing-splicing factor 8
- G patch domain-containing protein 1 homolog
- Ragulator complex protein LAMTOR3 homolog
- Ragulator complex protein LAMTOR2 homolog
Sequence:
MPEFENFNVKTTIDCKQGAVRAVRYNVDGTYCLSCGSDKKIKLWNPASGLLLKTYGGHADEVTDAAGSCDSSYIVSASLDKSIIYWDVSTGAPVRRLRSHAGGVRCVCFNEDSSIAISGGRDNAVMCWDIRTRRLDPVQVMKEARDCITTVATNENRIYAASLDGCVRTYDIRVGELTCDKIGEPITYLAQTRDEQCLVAGCQDSVVRLLDCETGGLLSEYRGHRGDDYHIECGILSNDAQIVTGSSDGDAFVYDLLDGKVLQRIRISDNGGVVHSLATHPKRQEMLFARRRDMYVFSTDLQIEEEQL
Protein: X-linked retinitis pigmentosa GTPase regulator-interacting protein 1 (RPGR-interacting protein 1) (Q96KN7)
Organism: Homo sapiens (Human)
Function: May function as scaffolding protein. Required for normal location of RPGR at the connecting cilium of photoreceptor cells. Required for normal disk morphogenesis and disk organization in the outer segment of photoreceptor cells and for survival of photoreceptor cells.
Subcellular location: Cell projection, cilium {ECO:0000269|PubMed:21685204}. Note=Situated between the axonemal microtubules and the plasma membrane (By similarity). In the retinal photoreceptor cell layer, localizes at the connecting cilium, a thin bridge linking the cell body and the light-sensing outer segment (By similarity). Colocalizes with RGPR in the photoreceptor connecting cilium (By similarity). {ECO:0000250|UniProtKB:Q9EPQ2}.
Interaction partners:
- X-linked retinitis pigmentosa GTPase regulator
- Nephrocystin-4
- Spermatogenesis-associated protein 7
- Centrosomal protein of 290 kDa
- Retinal guanylyl cyclase 1
- Aryl-hydrocarbon-interacting protein-like 1
- Nephrocystin-1
- Lebercilin
- Tubby-related protein 1
- Retinol dehydrogenase 12
Sequence:
MSHLVDPTSGDLPVRDIDAIPLVLPASKGKNMKTQPPLSRMNREELEDSFFRLREDHMLVKELSWKQQDEIKRLRTTLLRLTAAGRDLRVAEEAAPLSETARRGQKAGWRQRLSMHQRPQMHRLQGHFHCVGPASPRRAQPRVQVGHRQLHTAGAPVPEKPKRGPRDRLSYTAPPSFKEHATNENRGEVASKPSELVSGSNSIISFSSVISMAKPIGLCMPNSAHIMASNTMQVEEPPKSPEKMWPKDENFEQRSSLECAQKAAELRASIKEKVELIRLKKLLHERNASLVMTKAQLTEVQEAYETLLQKNQGILSAAHEALLKQVNELRAELKEESKKAVSLKSQLEDVSILQMTLKEFQERVEDLEKERKLLNDNYDKLLESMLDSSDSSSQPHWSNELIAEQLQQQVSQLQDQLDAELEDKRKVLLELSREKAQNEDLKLEVTNILQKHKQEVELLQNAATISQPPDRQSEPATHPAVLQENTQIEPSEPKNQEEKKLSQVLNELQVSHAETTLELEKTRDMLILQRKINVCYQEELEAMMTKADNDNRDHKEKLERLTRLLDLKNNRIKQLEGILRSHDLPTSEQLKDVAYGTRPLSLCLETLPAHGDEDKVDISLLHQGENLFELHIHQAFLTSAALAQAGDTQPTTFCTYSFYDFETHCTPLSVGPQPLYDFTSQYVMETDSLFLHYLQEASARLDIHQAMASEHSTLAAGWICFDRVLETVEKVHGLATLIGAGGEEFGVLEYWMRLRFPIKPSLQACNKRKKAQVYLSTDVLGGRKAQEEEFRSESWEPQNELWIEITKCCGLRSRWLGTQPSPYAVYRFFTFSDHDTAIIPASNNPYFRDQARFPVLVTSDLDHYLRREALSIHVFDDEDLEPGSYLGRARVPLLPLAKNESIKGDFNLTDPAEKPNGSIQVQLDWKFPYIPPESFLKPEAQTKGKDTKDSSKISSEEEKASFPSQDQMASPEVPIEAGQYRSKRKPPHGGERKEKEHQVVSYSRRKHGKRIGVQGKNRMEYLSLNILNGNTPEQVNYTEWKFSETNSFIGDGFKNQHEEEEMTLSHSALKQKEPLHPVNDKESSEQGSEVSEAQTTDSDDVIVPPMSQKYPKADSEKMCIEIVSLAFYPEAEVMSDENIKQVYVEYKFYDLPLSETETPVSLRKPRAGEEIHFHFSKVIDLDPQEQQGRRRFLFDMLNGQDPDQGHLKFTVVSDPLDEEKKECEEVGYAYLQLWQILESGRDILEQELDIVSPEDLATPIGRLKVSLQAAAVLHAIYKEMTEDLFS
Protein: 50S ribosomal protein L17, putative (Q57YI7)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Large ribosomal subunit protein bL21m
- 40S ribosomal protein S15, putative
- 40S ribosomal protein S5, putative
- 50S ribosomal protein L13, putative
- 30S Ribosomal protein S17, putative
- Ribosomal protein L11, putative
- Large ribosomal subunit protein uL3m
- 60S ribosomal protein L35, putative
- 60S ribosomal protein L17, putative
- 50S ribosomal protein L2, putative
Sequence:
MLRITLLVVGRAPPVIGCTRKARYAGIDDNPTITYKPWDTTEPLMADYGWTRGKLPKFRARSPFHRQQIARRMVTEMIRKDYCIVGGARAPALRILADHVVELAKAGDTDSRQQLAYFLHDPLMVDKAFDEYPRRFKDMNAKYAMMTRLKSRRRTDAVAMYFVEYKNRDMSDNHKGEDYSAGPERFFLPPRIVETEKGIQRPPHMQMAFDRWASKFKTEEFHHWWRLRHAKLRYWGVRNVPHPSDVDPLWTEKEEEEWHNEMLANTGEYEDLDLDDESYTAAGEGGEPSPAGDGPQPQRVG
Protein: Serine/threonine-protein kinase PLK4 (EC 2.7.11.21) (Polo-like kinase 4) (PLK-4) (Serine/threonine-protein kinase Sak) (Q6PAD2)
Organism: Xenopus laevis (African clawed frog)
Function: Serine/threonine-protein kinase that plays a central role in centriole duplication. Able to trigger procentriole formation on the surface of the parental centriole cylinder, leading to the recruitment of centriole biogenesis proteins such as sass6, cenpj/cpap, ccp110, cep135 and gamma-tubulin. When overexpressed, it is able to induce centrosome amplification through the simultaneous generation of multiple procentrioles adjoining each parental centriole during S phase. Its central role in centriole replication suggests a possible role in tumorigenesis, centrosome aberrations being frequently observed in tumors. Also involved in deuterosome-mediated centriole amplification in multiciliated that can generate more than 100 centrioles (By similarity).
Subcellular location: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000250|UniProtKB:O00444}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:O00444}. Note=Associates with centrioles throughout the cell cycle (By similarity). Component of the deuterosome, a structure that promotes de novo centriole amplification in multiciliated cells that can generate more than 100 centrioles. {ECO:0000250, ECO:0000269|PubMed:24075808}.
Interaction partners:
Sequence:
MAGSIGERREDFKVLNLLGKGSFACVYRAQSINTGIDVAIKMIDKKAMQKVGMVQRVRNEVEIHCQLKHPSILELYNYFEDSNYVYLILEMCHNGEVNRYLKNRKKPFAEDEARHFMHQIVTGMLYLHSHGILHRDLTLSNLLLSSDMNIKIADFGLATQLKMPNEKHFTMCGTPNYIAPEIATRSAHGLESDVWSLGCMLYTFLVGRPPFDTDTVKNTLNKIVLADYEMPDFVSREAKDLIFQLLRKNPADRLSLSSVLDHAFMTGFSNVQSKVMGAVEDSMDSGHATISTGFTGSSGVSISGRFQEKRILSGPSLPNKVNIFQFKDKHPTERSNGGSFHNTQRENNDFSEGNGRKPVACEDRPHSRYLRRAHSSDRSGTSQSQTYAKPSSYSERCHSVEMLAKPTHLKGYRTSSPPNSYGDIPQMFTDERSLERHTSPPVKEKTPSEFMGPAKQTAPRSNDKAETVQQWFGAMQLNGQFKNTPDTSSVSNMGGDFYSQQATQNGAPQYAWNDVKRKKNTDSSIESVLLGIKKNPGTGQRKAEKSQFGEQSKSRVPQQAFGSSTLRSIISPLNAERLKPIRQKTKNAVVSILESGEVCMEFLKEQNSQERVKEVLRISCDGNLIYVYHPNEGKGFPLVDRPPSPPENRLSYTFDSLPEKYWKKYQYAAKFIKLVRSKTPKVTYYTRYAKCMLMENSPTADVEVCFYDGAKIHKTSDVIRVIEKSGRSYTLEGSRLSTLSDEVRSYLDHANESHCVCLSLESAINTEEKKGENISLFPITFGRRPALAESPKTQPTPSVDSARERKEEQSYVNRVLHGSAASPPQMPNLNPSLISYDGSVFSATTVQPSPTSNIHNTPDHAQVLKSVFVENVGWASQLNSGAVWVQFNDGSQLVVQPGVSSIIYTAPNGQITRHGENDKLPEYIKSKLQCLSSILMLFASSSSR
Protein: Chromosome 14 open reading frame transcript variant 2 (Protein phosphatase 2 regulatory subunit B''gamma) (Q86US5)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MDWKEVLRRRLATPNTCPNKKKSEQELKDEEMDLFTKYYSEWKGGRKNTNEFYKTIPRFYYRLPAEDEVLLQKLREESRAVFLQRKSRELLDNEELQNLWFLLDKHQTPPMIGEEAMINYENFLKVGEKAGAKCKQFFTAKVFAKLLHTDSYGRISIMQFFNYVMRKGDSFLLCLNSLSGNQVGFWSVLL
Protein: Ras-related protein RABF2a (AtRABF2a) (Ras-related protein Rab5A) (AtRab5A) (Ras-related protein Rha1) (P31582)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in the trafficking of soluble cargo proteins from the prevacuolar compartment to the central vacuole. Involved in vacuolar transport of storage proteins with EREX as effector. Regulates membrane trafficking to protein storage vacuoles (PSVs).
Subcellular location: Endosome membrane {ECO:0000269|PubMed:12724533, ECO:0000269|PubMed:15509844}; Lipid-anchor {ECO:0000305|PubMed:12724533, ECO:0000305|PubMed:15509844}. Prevacuolar compartment membrane {ECO:0000269|PubMed:12724533, ECO:0000269|PubMed:15509844}; Lipid-anchor {ECO:0000305}.
Interaction partners:
- Guanosine nucleotide diphosphate dissociation inhibitor At5g09550
- Guanosine nucleotide diphosphate dissociation inhibitor 2
- Guanosine nucleotide diphosphate dissociation inhibitor 1
- Vacuolar protein sorting-associated protein 9A
- Vacuolar protein sorting-associated protein 45 homolog
- Protein SUPPRESSOR OF K
- Rab escort protein 1
- Vesicle transport v-SNARE 12
- Vesicle-associated membrane protein 727
- Vesicle-associated membrane protein 711
Sequence:
MASSGNKNINAKLVLLGDVGAGKSSLVLRFVKDQFVEFQESTIGAAFFSQTLAVNDATVKFEIWDTAGQERYHSLAPMYYRGAAAAIIVFDITNQASFERAKKWVQELQAQGNPNMVMALAGNKADLLDARKVSAEEAEIYAQENSLFFMETSAKTATNVKDIFYEIAKRLPRVQPAENPTGMVLPNGPGATAVSSSCCA
Protein: 2'-5'-oligoadenylate synthetase 1 (F8VPW7)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MMDLRNTPAKSLDKFIEDYLLPDTCFRMQINHAIDIICGFLKERCFRGSSYPVCVSKVVKGGSSGKGTTLRGRSDADLVVFLSPLTTFQDQLNRRGEFIQEIRRQLEACQRERAFSVKFEVQAPRWGNPRALSFVLSSLQLGEGVEFDVLPAFDALGQLTGGYKPNPQIYVKLIEECTDLQKEGEFSTCFTELQRDFLKQRPTKLKSLIRLVKHWYQNCKKKLGKLPPQYALELLTVYAWERGSMKTHFNTAQGFRTVLELVINYQQLCIYWTKYYDFKNPIIEKYLRRQLTKPRYAIPTWLSSPM
Protein: non-specific serine/threonine protein kinase (EC 2.7.11.1) (Q8IXA3)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MDHPSREKDERQRTTKPMAQRSAHCSRPSGSSSSSGVLMVGPNFRVGKKIGCGNFGELRLGKNLYTNEYVAIKLEPIKSRAPQLHLEYRFYKQLGSAGEGLPQVYYFGPCGKYNAMVLELLGPSLEDLFDLCDRTFTLKTVLMIAIQLLSRMEYVHSKNLIYRDVKPENFLIGRQGNKKEHVIHIIDFGLAKEYIDPETKKHIPYREHKSLTGTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQGLKADTLKERYQKIGDTKRNTPIEALCENFPEEMATYLRYVRRLDFFEKPDYEYLRTLFTDLFEKKGYTFDYAYDWVGRPIPTPVGSVHVDSGASAITRESHTHRDRPSQQQPLRNQVVSSTNGELNVDDPTGAHSNAPITAHAEVEVVEEAKCIMFHKPWHWSQSSAVKMKFVVFLNMNVNFKCI
Protein: V-type proton ATPase subunit F 1 (V-ATPase subunit F 1) (V-ATPase 14 kDa subunit) (Vacuolar H+ ATPase subunit 14-1) (Vacuolar proton pump subunit F 1) (Q24583)
Organism: Drosophila melanogaster (Fruit fly)
Function: Subunit of the V1 complex of vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1) that hydrolyzes ATP and a membrane integral complex (V0) that translocates protons (By similarity). V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments and in some cell types, is targeted to the plasma membrane, where it is responsible for acidifying the extracellular environment (By similarity).
Interaction partners:
- V-type proton ATPase subunit B
- V-type proton ATPase subunit G
- V-type proton ATPase subunit E
- V-type proton ATPase subunit C
- V-type proton ATPase subunit D 1
- V-type proton ATPase subunit H
- V-type proton ATPase 16 kDa proteolipid subunit c
- V-type proton ATPase subunit d 1
- V-type proton ATPase catalytic subunit A isoform 1
- V-type proton ATPase catalytic subunit A isoform 2
Sequence:
MALHSAIKGKLISVIGDEDTCVGFLLGGVGEINKNRHPNFMVVDKNTAVSELEDCFKRFLKRDDIDIILINQNCAELIRHVIDAHTSPVPAVLEIPSKDHPYDASKDSILRRARGMFNPEDLVR
Protein: Beta-amylase 3, chloroplastic (EC 3.2.1.2) (1,4-alpha-D-glucan maltohydrolase) (Beta-amylase 8) (Chloroplast beta-amylase) (CT-BMY) (O23553)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Beta-amylase activity. No alpha-amylase activity. Involved in cold resistance. Mediates the accumulation of maltose upon freezing stress, thus contributing to the protection of the photosynthetic electron transport chain. Plays a role in the circadian-regulated starch degradation and maltose metabolism in chloroplasts, especially at night. More active on phosphorylated glucan. Interacts directly with starch or other alpha-1,4-glucan.
Subcellular location: Plastid, chloroplast {ECO:0000269|PubMed:10652124, ECO:0000269|PubMed:16698902, ECO:0000269|PubMed:18390594}.
Interaction partners:
- 4-alpha-glucanotransferase DPE1, chloroplastic/amyloplastic
- 4-alpha-glucanotransferase DPE2
- Isoamylase 3, chloroplastic
- alpha-D-xyloside xylohydrolase
- Alpha-amylase 3, chloroplastic
- Alpha-amylase 1
- Probable alpha-amylase 2
- Phosphoglucan phosphatase LSF1, chloroplastic
- Alpha-glucan phosphorylase 2, cytosolic
- Isoamylase 2, chloroplastic
Sequence:
MELTLNSSSSLIKRKDAKSSRNQESSSNNMTFAKMKPPTYQFQAKNSVKEMKFTHEKTFTPEGETLEKWEKLHVLSYPHSKNDASVPVFVMLPLDTVTMSGHLNKPRAMNASLMALKGAGVEGVMVDAWWGLVEKDGPMNYNWEGYAELIQMVQKHGLKLQVVMSFHQCGGNVGDSCSIPLPPWVLEEISKNPDLVYTDKSGRRNPEYISLGCDSVPVLRGRTPIQVYSDFMRSFRERFEGYIGGVIAEIQVGMGPCGELRYPSYPESNGTWRFPGIGEFQCYDKYMKSSLQAYAESIGKTNWGTSGPHDAGEYKNLPEDTEFFRRDGTWNSEYGKFFMEWYSGKLLEHGDQLLSSAKGIFQGSGAKLSGKVAGIHWHYNTRSHAAELTAGYYNTRNHDGYLPIAKMFNKHGVVLNFTCMEMKDGEQPEHANCSPEGLVKQVQNATRQAGTELAGENALERYDSSAFGQVVATNRSDSGNGLTAFTYLRMNKRLFEGQNWQQLVEFVKNMKEGGHGRRLSKEDTTGSDLYVGFVKGKIAENVEEAALV
Protein: Fatty acid-binding protein 3, muscle and heart (Fatty acid-binding protein, heart) (Heart-type fatty-acid binding protein) (Q8UVG7)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- Gastrotropin
- Fatty acid binding protein 1-B.1
- Fatty acid binding protein 1-A, liver
- Fatty acid-binding protein 2, intestinal
- Fatty acid binding protein 11a
- Brain-type fatty acid-binding protein
- Adipocyte fatty acid-binding protein
- Brain-type fatty acid-binding protein b
- Fatty acid binding protein 1-B.1
Sequence:
MADAFIGTWNLKESKNFDEYMKGIGVGFATRQVANMTKPTTIISKEGDVFTLKTVSTFKSTEINFKLGEEFDETTADDRKVKSVITLDGGKLLHVQKWDGKETTLLREVSDNNLTLTLTLGDIVSTRHYVKAE
Protein: Mitochondrial adenyl nucleotide antiporter SLC25A24 (Small calcium-binding mitochondrial carrier protein 1) (SCaMC-1) (Solute carrier family 25 member 24) (Q8BMD8)
Organism: Mus musculus (Mouse)
Function: Calcium-dependent mitochondrial solute carrier. Mediates the reversible, electroneutral exchange of Mg-ATP or Mg-ADP against phosphate ions, catalyzing the net uptake or efflux of adenine nucleotides across the mitochondrial inner membrane. Nucleotide transport is inactive when cytosolic calcium levels are low, and is activated by an increase in cytosolic calcium levels. May play a role in protecting cells against oxidative stress-induced cell death, probably by promoting the formation of calcium-phosphate precipitates in the mitochondrial matrix, and thereby buffering calcium levels in the mitochondrial matrix (By similarity).
Subcellular location: Mitochondrion inner membrane {ECO:0000305|PubMed:15054102}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Large ribosomal subunit protein eL18
- NADH-ubiquinone oxidoreductase chain 3
- NADH dehydrogenase iron-sulfur protein 3, mitochondrial
- NADH-ubiquinone oxidoreductase chain 1
- NADH-ubiquinone oxidoreductase chain 4
Sequence:
MLRWLRAFVLPTAACHDAEPPTRYETLFRALDRNGDGVVDIGELQQGLQSLGIPLGQDAEEKIFTTGDVNKDGKLDFEEFMKYLKDHEKKMKLAFKSLDKNNDGKIEPSEIVQSLQMLGLHISEKQAELILQSIDSDGTMTVDWNEWRDYFLFNPVTDIEEIIRFWKHSTGIDIGDSLTIPDEFTEDEKKSGQWWRQLLAGGVAGAVSRTSTAPLDRLKVMMQVHGSKSMNIFGGFRQMVKEGGIRSLWRGNGTNVIKIAPETAVKFWAYEQYKKLLTEEGQKLGTFERFISGSMAGATAQTFIYPMEVLKTRLAVAKTGQYSGIYGCAKKILKHEGFGAFYKGYIPNLLGIIPYAGIDLAVYELLKSYWLDNFAKDSVNPGVMVLLSCGALSSTCGQLASYPLALVRTRMQAQATVEGAPQLSMVGLFQRIVSKEGVSGLYRGITPNFMKVLPAVGISYVVYENMKQTLGVAQK
Protein: Probable carboxyl-terminal protease (Q9HU50)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Interaction partners:
- Peptidase M23 domain-containing protein
- Divergent polysaccharide deacetylase family protein
- LysM domain-containing protein
- Peptidase M23 domain-containing protein
Sequence:
MLHCFRPTTLALALLLGAGAAQAADAPADAAPLANGSSAPLPLDELRTFAEVLDRVKAAYVEPVDDKTLLENAIKGMLSNLDPHSAYLGPEDFAELQESTSGEFGGLGIEVGSEDGFIKVVSPIDDTPAARAGIQPGDLIVQIDGKPTKGQSMTEAVDSMRGKAGSPITLTIVRDGGRPFDVELKRAIIKVKSVKSQVLEPGYAYLRITQFQVNTGEEVVKALNQLRKDNKGRLKGLVLDLRNNPGGVLQSAVEVADAFLTKGLIVYTKGRIANSELRFSADPADPSDKVPLVVLINGGSASAAEIVAGALQDQKRAILMGTDSFGKGSVQTVLPLNNDRALKLTTALYYTPNGRSIQAQGIVPDIEVGRAKVTQERSSFEGFKEADLQGHLANGNGGADRPTGKRAAPSERPQDSDYQLSQALSLLKGLSVTRGN
Protein: Isocitrate dehydrogenase [NADP] (EC 1.1.1.42) (Q7KUB0)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MAQKIKAGPVVDVLGDEMTRIIWDSIKSQLILPFLDIELHTYDLGIENRDKTEDQVTIDCAEAIKKYNVGIKCATITPDEKRVEEFNLKKMWKSPNGTIRNILGGTVFREAIICKNVPRLVTGWQKPIVIGRHAHADQYKAVDYVVPGPGKLTLTWKGTDGQVIDEVINDFKGPGIALGMFNTDDSIVDFAHASFKYALDRKLPLYMSTKNTILKKYDGRFKDIFEDLYNKQYKKEYEAAGIWYEHRLIDDMVAYAMKSEGGFVWACKNYDGDVQSDSVAQGYGSLGLMTSVLLCPDGKTVEAEAAHGTVTRHFRFYQQGKETSTNPIASIFAWTRGLLHRAKLDNNEPLKQFADTLEQVCIDTIESGAMTKDLAICIKGNINAVTRRDYQETFEFINTLAKNLEGALAKNAVAAK
Protein: X-box-binding protein 1 (Q5BI44)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MAPTANTVLITVPRTAITSNNLPKLRPAPLTAALLKVSATPSASPTPSSSGYASSSNMDDDNMAASQPKAKKRRLDHLTWEEKVQRKKLKNRVAAQTSRDRKKARMEEMDYEIKELTDRTEILQNKCDSLQAINESLLAKNHKLDSELELLRQELAELKQQQQHNTRCISQSNASAGAEGCASTNLGSAASKADPLPQGIQQVDTQSSARLLAEQLKSSKSLASLWKVVALCLLYKTCLASTKSSTSSASKSWPKVCSQISQQTWKQALERAAQLLPKMQATQSDCLDQWWGPQQSAWNPTGIELMA
Protein: F-box only protein 33 (Q7Z6M2)
Organism: Homo sapiens (Human)
Function: Substrate recognition component of a SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. Probably recognizes and binds to phosphorylated target proteins. Recognizes YBX1 (By similarity).
Interaction partners:
- Cullin-1
- Ribonuclease inhibitor
- S-phase kinase-associated protein 1
Sequence:
MLLFLSVPQPRPPGARTRAGAARVARWRRLRLQQLRRLRGLLRVLRGRPGAGSRRRGRMALCGQAAGAASLPSELIVHIFSFLPAPDRLRASASCSHWRECLFYPALWPQLRICLRVSPAEQPRLEFLMRKCGWFVRELRVEFAAENYLSGGGPGDGGGADTGTGGEEVEALQLSARWLEVLRTYLELVLCVLVSIRNNRNLQKFSLFGDISVLQQQGSLSNTYLSKVDPDGKKIKQIQQLFEEILSNSRQLKWLSCGFMLEIVTPTSLSSLSNAVANTMEHLSLLDNNIPGNSTLITAVELERFVNLHSLALDFCDFTAEMARVLTDSNHVPLQRLSLLVHNVSVMHKSLDNMPNDEHWKALSRKSTSFRVYIMAFDIKSEDMLKILKPSIPLERIHFDSYITCVSGAIVDLISRQYDKFLTHFILMNDVIDTSGFPDLSDNRNEDPLVLLAWRCTKLSLLAIHGYTVWAHNLIAIARLRGSDLKVLEVTEESIDFDQGELADQDVDPVHNLIEQVSLGLGQPWHAVMDIESLSVFTEPNRHFYREMQSFSEDI
Protein: Inositol-pentakisphosphate 2-kinase (EC 2.7.1.158) (Inositol-1,3,4,5,6-pentakisphosphate 2-kinase) (Ins(1,3,4,5,6)P5 2-kinase) (InsP5 2-kinase) (Q9USK0)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Has kinase activity and phosphorylates inositol-1,3,4,5,6-pentakisphosphate (Ins(1,3,4,5,6)P5) to produce 1,2,3,4,5,6-hexakisphosphate (InsP6), also known as phytate.
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- Inositol polyphosphate multikinase
- Uncharacterized inositol polyphosphate kinase C970.08
- Inositol hexakisphosphate and diphosphoinositol-pentakisphosphate kinase
Sequence:
MPLKNYTKTTSKKEPKQLDIAASDQQIEQWSDQIHKLDKAIRSTIDNSRLFYDAWRCMVCIAPSVTASWISLYRQLPPEKQPAASVGTLVDWNKALERQRREVLLALQNFHVIVIAPCKEVKGYVKKAVEMIKRRDKKVKELEKIQKELLVVYELPDPETKKSKIKALQSQLVRVNGELDDLQKHLTLSFPTLIAKSRVFFGQLMKHFYCLQLQMFRKMHNIVRPWDCFQDDIPQTWLVEFSSVCQAAESISLIAVNNNRPPVELPKSGDVLSNREWEAGKIDAMNSLIAQNLHTSASQVSLSPMASTASSSVTNSPVDTHTPSTPIMSRPPSMKALSSGVESQDESVASSNFQVPIISNPLFKSPAPYSPTSVISNHSSTGKSLVISEWAYLASGSANVVFEYVGKNPYFQDKVIRLRRRGQVFTTEQVYEYYQNVIYPLFAGMESFLIEVFLQPVTRDFLLAAQNASGIYLNLNEQYCLVMKDLKDGIEMKPKWLTQSPAAPPDWVVCRTCALSRMRGRPVGFCPLQLDFNNWPKFLCCLQGFVSPDIAMRLFQSGILRKLRDLQEQYSRTDVALAMTLRDVTLYIGKDHITLLDLDPKDMNTKMSKWERDERNLIEGGWYYGRGMKSTDKACRSSIK
Protein: Tubulin beta chain (B1PBW1)
Organism: Gossypium hirsutum (Upland cotton) (Gossypium mexicanum)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}.
Interaction partners:
Sequence:
MREILHVQGGQCGNQIGSKFWEVVCDEHGIDPTGRYTGNSSLQLERVNVYYNEASCGRFVPRAVLMDLEPGTMDSVRTGPYGQIFRPDNFVFGQSGAGNNWAKGHYTEGAELIDSVLDVVRKEAENCDCLQGFQVCHSLGGGTGSGMGTLLISKIREEYPDRMMLTFSVFPSPKVSDTVVERYNATLSVHQLVENADECMVLDNEALYDICFRTLKLTTPSFGDLNHLISATMSGVTCCLRFPGQLNSDLRKLAVNLIPFPRLHFFMVGFAPLTSRGSQQYRSLTVPELTQQMWDAKNMMCAADPRHGCYLTASAMFRGKMSTKEVDEQMINVQNKNSSYFVEWIPNNVKSSVCDIPPRGLSMASTFVGNSTSIQEMFRRVSEQFTAMFRRKAFLHWYTGEGMDEMEFTEAESNMNDLVSEYQQYQDATAEDELEYEDEDEEAVHEM
Protein: Putative transport protein (Small multi-drug export protein) (O64717)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MAISTLLSISSFTLSSSSSTKTHLLTSIPASRVYSYPISPKWKQIRFLQSQSSSLFYPLRRNFTRFCSSPDGFLRNTKDDEEGNEIIQLPSIGVNPVKFAICVVLWASFSLLWFARSGDAKAATDSIKSSSFGLRIASTLRRFGWPDEAVVFALATLPVIELRGAIPVGYWMQLKPVVLTSFSVLGNMVPVPFIVLYLKTFASFVAGKSQTASKLLDILFKRAKEKAGPVEEFKWLGLMLFVAVPFPGTGAWTGAIIASILDMPFWSAVSSNFCGVVLAGLLVNLLVNLGLKQAIVAGIALFFVSTFMWSVLRNIRKSIKPSLP
Protein: Voltage-dependent calcium channel alpha13 subunit (Q963J2)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
GFSSERNERREREQRELVKKLREETLAENYSDGMYDESRSEADSSTTNDSYYEVRNRWRSAEDVRKLQDSAELIIEAKSNMHRQRLLQPTHDYQINELPASSAAPSASGTSGASAPGERERDRDRDRDRDRERDRDRDRERDREAGGGGKEEGAQHAKPRGGLKKTYSIKERRSEAPRLSKIRLARDPPIITTTAATPQDSPSTTLEPGMSFRQWGDMEPPSPPSPSLLRPPNIFTGGQRSLDEGIPSIDLIPPSPVLSHKPLNILNASQLGVGMGGGVPSTAGSSSSMHSVIIDDISKSSSSTAAATPIYVPTISSTADAQSQSHSLNDVSVGSSPGGEISATGMGRNANTGASTSGSSSSERLPLAPPPQQGSFKQRLRRGSSKKRRASALALATDDNPARRTLDNQARRTQDEEEEQQQLNNGGDNSCLLRNSNAVVSGSSSGTKETNRLSPQNSIRRLSNTLSIGSGPVGSRRASACIFNSQVYQNLNQPPKLRPGSGQRRMSSIELAFSKTSHLNLHNLEANRKSLSYTNSKMDLDKWNKSYGNLNEPDNMLQQYMEARDKRKNSISHYNLKKRLEEKELQQLQQLHQQQLLQQRQDSFSSTTQQQQQQLQQHRLSKDQQQLAMQPHSMVPGGGERYSKLKMLIEQLTPKH