wanglab/gogpt-training-data huggingface dataset:
Protein: Kinesin-like protein (Q57XZ5)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MQDEQHEELPPSPSFETLDSLRQDNDNEAIQPPNAPSPILERRVASSDAFPPQLSSRHRCGEGSNAPSLLNLNRQLEDLSRDIQQLNARCRSDSMPNINKTPLRPQHLLPEKQLQLLKQRLPHLNSALSARGASTPSRTGRESSQRRQDALPTVSPSPPRSRCATSVTRPYQSKQETPCSSRVFPGRASERPIASPSSPSIAANMDSVTPAAVTEDPQADGKQCAIMRTRGGRIRVVVRKRPLPPDENSCDCVSMDPPNVKVAVRKQRVDLTEYADVNDFTFDDAFGEDKHNEHVFNSCCKELLETTLQGGSASCFAYGQTGSGKTHTMLGNSGERGLYILAAAAIFSSLEKDQEVYASLYEIYCNSLFDLLNNRSPVVVREDHNRRMQITGLTWHAVTSAEELQLLINSGADQRSTGSTTANERSSRSHAVLTIQVRDREDNRFCGTLNLVDLAGSERAADTATNDRQTRQEGAEINKSLLALKECIRALDEKKKHVPFRGSKLTEILRDSFIGNSRTVMIANISASSQNYEHTLNTLRYAFRVKGLSIVNFEPSRARNAPRPLKPIVPDVNPAQGVPLMSGVPSRTTPGRRRTASSNVTSHAAAGAAAPPAASHAKGYNSMVPVTTRRNVSSNNTPFNLRNNAGSPFRGGAQGNNVDSRADDEQVAEYVRRLTREKVMNILPQTKLNEAREQPSPKNDYSLQDESCSFSFNHELMKELEDRVVEEIKAELTKAIKDVLLKRDKTFLRLRREKALLMRANTELEKRMADCPHCKGQAIRPVQQQPN
Protein: Metalloreductase STEAP4 (EC 1.16.1.-) (Dudulin-4) (Six-transmembrane epithelial antigen of prostate 4) (Tumor necrosis factor-alpha-induced adipose-related protein) (Q923B6)
Organism: Mus musculus (Mouse)
Function: Integral membrane protein that functions as NADPH-dependent ferric-chelate reductase, using NADPH from one side of the membrane to reduce a Fe(3+) chelate that is bound on the other side of the membrane. Mediates sequential transmembrane electron transfer from NADPH to FAD and onto heme, and finally to the Fe(3+) chelate (By similarity). Can also reduce Cu(2+) to Cu(1+). Plays a role in systemic metabolic homeostasis, integrating inflammatory and metabolic responses. Associated with obesity and insulin-resistance (By similarity). Involved in inflammatory arthritis, through the regulation of inflammatory cytokines. Inhibits anchorage-independent cell proliferation (By similarity).
Subcellular location: Cell membrane {ECO:0000269|PubMed:11443137, ECO:0000269|PubMed:16609065}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q687X5}. Golgi apparatus membrane {ECO:0000305|PubMed:11443137}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q687X5}. Early endosome membrane {ECO:0000269|PubMed:16609065}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q687X5}.
Interaction partners:
Sequence:
MEKAHADEFPLTTDSSEKQGVVCIFGTGDFGKSLGLKMLQCGYSIVFGSRNPQVSSLLPRGAEVLSYSEAASKSDIIILAMHREHYDSLTELVDYLKGKVLVDVSNNRKINQYPESNAEYLAQLEPGAHVVKAFNTISAWALQSGTLDASRQVFVCGNDSKAKQRVMDIARTLGLTPLDQGSLMAASEIENYPLQLFPMWRFPFYLSSVLCVFFFVYCAIREVIYPYVNGKTDATYRLAISIPNRVFPITALILLALVYLPGILAAILQLYRGTKYRRFPNWLDHWMLCRKQLGLVALGFAFLHVIYTLVIPIRYYVRWRLRNATITQALTNKDSPFITSYAWINDSYLALGILGFFLFLLLGITSLPSVSNMVNWREFRFVQSKLGYLTLVLCTAHTLVYGGKRFLSPSILRWSLPSAYILALVIPCAVLVLKCILIMPCIDKTLTRIRQGWERNSKYTQSALNGKSDI
Protein: Zinc finger protein 439 (Q8NDP4)
Organism: Homo sapiens (Human)
Function: May be involved in transcriptional regulation.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
Sequence:
MLSLSPILLYTCEMFQDPVAFKDVAVNFTQEEWALLDISQKNLYREVMLETFWNLTSIGKKWKDQNIEYEYQNPRRNFRSVTEEKVNEIKEDSHCGETFTPVPDDRLNFQKKKASPEVKSCDSFVCEVGLGNSSSNMNIRGDTGHKACECQEYGPKPWKSQQPKKAFRYHPSLRTQERDHTGKKPYACKECGKNIIYHSSIQRHMVVHSGDGPYKCKFCGKAFHCLSLYLIHERTHTGEKPYECKQCGKSFSYSATHRIHERTHIGEKPYECQECGKAFHSPRSCHRHERSHMGEKAYQCKECGKAFMCPRYVRRHERTHSRKKLYECKQCGKALSSLTSFQTHIRMHSGERPYECKTCGKGFYSAKSFQRHEKTHSGEKPYKCKQCGKAFTRSGSFRYHERTHTGEKPYECKQCGKAFRSAPNLQLHGRTHTGEKPYQCKECGKAFRSASQLRIHRRIHTGEKPYECKKCGKAFRYVQNFRFHERTQTHKNALWRKTL
Protein: Helix-loop-helix protein 25 (Q18054)
Organism: Caenorhabditis elegans
Function: Probable transcription factor. Modulates lifespan and also recovery from the developmentally arrested larval state known as dauer, perhaps acting upstream of phosphatase PTEN/daf-18. Regulates expression of genes involved in cell division, cell-cycle regulation, and sexual reproduction, including daf-18.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981}.
Interaction partners:
- Protein mxl-3
- Helix-loop-helix protein 11
- Regulator of fusion ref-1
Sequence:
MPKVIQSSMSDYRSVPYNQTPKSASERKRRNITNELINECKTIVQKSEEEHISQEVVLFRIVKLVTGVNLESNFSSNDLSESTRRKFDTESERRKVKTEREKIRRKKQDDCYAELKFFILNKQMGSYEQRLKLERITILEIIIDYIKHNSDLLYPETIPQILPLLAGKSTATCENKENEKPKTRMEVKDLFPRLTFQEVQESPTSTSPLLTFPCIPMIPTTQFNVLSNYNTVPSIFSAPLRFILPSLQILTPETSDEEENEETLDIIN
Protein: Hsc70-interacting protein (Hip) (Aging-associated protein 2) (Progesterone receptor-associated p48 protein) (Protein FAM10A1) (Putative tumor suppressor ST13) (Renal carcinoma antigen NY-REN-33) (Suppression of tumorigenicity 13 protein) (P50502)
Organism: Homo sapiens (Human)
Function: One HIP oligomer binds the ATPase domains of at least two HSC70 molecules dependent on activation of the HSC70 ATPase by HSP40. Stabilizes the ADP state of HSC70 that has a high affinity for substrate protein. Through its own chaperone activity, it may contribute to the interaction of HSC70 with various target proteins (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Heat shock cognate 71 kDa protein
- Heat shock protein HSP 90-alpha
- Heat shock 70 kDa protein 4
- Heat shock protein HSP 90-beta
- DnaJ homolog subfamily B member 1
- BAG family molecular chaperone regulator 1
- Heat shock 70 kDa protein 1A
- Ataxin-3-like protein
- BAG family molecular chaperone regulator 3
- Ubiquitin-conjugating enzyme E2 D1
Sequence:
MDPRKVNELRAFVKMCKQDPSVLHTEEMRFLREWVESMGGKVPPATQKAKSEENTKEEKPDSKKVEEDLKADEPSSEESDLEIDKEGVIEPDTDAPQEMGDENAEITEEMMDQANDKKVAAIEALNDGELQKAIDLFTDAIKLNPRLAILYAKRASVFVKLQKPNAAIRDCDRAIEINPDSAQPYKWRGKAHRLLGHWEEAAHDLALACKLDYDEDASAMLKEVQPRAQKIAEHRRKYERKREEREIKERIERVKKAREEHERAQREEEARRQSGAQYGSFPGGFPGGMPGNFPGGMPGMGGGMPGMAGMPGLNEILSDPEVLAAMQDPEVMVAFQDVAQNPANMSKYQSNPKVMNLISKLSAKFGGQA
Protein: Cytosolic purine 5'-nucleotidase (EC 3.1.3.5) (EC 3.1.3.99) (Cytosolic nucleoside phosphotransferase 5'N) (EC 2.7.1.77) (Q5ZIZ4)
Organism: Gallus gallus (Chicken)
Function: Broad specificity cytosolic 5'-nucleotidase that catalyzes the dephosphorylation of 6-hydroxypurine nucleoside 5'-monophosphates. In addition, possesses a phosphotransferase activity by which it can transfer a phosphate from a donor nucleoside monophosphate to an acceptor nucleoside, preferably inosine, deoxyinosine and guanosine (By similarity). Has the highest activities for IMP and GMP followed by dIMP, dGMP and XMP. Could also catalyze the transfer of phosphates from pyrimidine monophosphates but with lower efficiency (By similarity). Through these activities regulates the purine nucleoside/nucleotide pools within the cell.
Subcellular location: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P49902}.
Interaction partners:
- Inosine-5'-monophosphate dehydrogenase
- dNK domain-containing protein.
- Adenosine kinase
- Adenosine deaminase
- Purine nucleoside phosphorylase
- Deoxycytidylate deaminase
- Hypoxanthine-guanine phosphoribosyltransferase
- GMP reductase
- A_deaminase domain-containing protein.
- 5',3'-nucleotidase
Sequence:
MTTSWSDRLQNAADLPANMDGHALKKYRREAYHRVFVNRSLAMEKIKCFGFDMDYTLAVYKSPEYESLGFDLTVERLVSIGYPHELLNFVYDPAFPTRGLVFDTHYGNLLKVDAYGNLLVCAHGFNFLRGPETRDQYPNKFIQRDDTDRFYILNTLFNLPETYLLACLVDFFTNCDRYTSCETGFKDGDLFMSFRSMFQDVRDAVDWVHYKGSLKEKTLENLEKYVVKDGKLPLLLSRMNEVGKVFLVTNSDYKYTDKIMTYLFDFPHGPKPGSAHRPWQSYFDLILVDARKPLFFGEGTVLRQVDTVTGKLKIGTYTGPLQHGIVYSGGSSDTVCDLLGAKGKDILYIGDHIFGDILKSKKRQGWRTFLVIPELAQELHVWTDKSALFEELQSLDIFLAELYKHLDSSSNERPDISSIQRRIKKVTHDMDMCYGMMGSLFRSGSRQTLFASQVMRYADLYAASFINLLYYPFSYLFRAAHVLMPHESTVEHTHVDINEKESPMATRNRTSVDFKDSDYKRHQLTRSISEIKPPNLFPQAPQEITHCHDEDDDEEEEEEEVEEEEEEEE
Protein: 60S ribosomal protein L2 (Q8I3T9)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
- 60S ribosomal protein L26, putative
- 60S ribosomal protein L6, putative
- 60S ribosomal protein L35ae, putative
- 40S ribosomal protein S6
- 60S ribosomal protein L13
- 40S ribosomal protein S27
- Small ribosomal subunit protein eS30
- 40S ribosomal protein S23, putative
- 60S ribosomal protein L27
- 40S ribosomal protein S15
Sequence:
MGRVIRGQRKGRGSIFKSHNHHRKGAAKLRHLDYCEKKGYIKGLVKDIIHDPGRGAPLAKVIFKRTEKYGKKEELIIASEGMFTGQYISCGTKAPLSVGNILPIGKMPEGTLICNLEHRTGNRGTLVKASGCYATVVGQSEDGKKTKVRLPSGAKKTIDAKARAMVGVVGAGGRIDKPILKAGVAHHKYRVKRNCWPKVRGVAMNPVEHPHGGGNHQHIGHPSTVSRSAPAGQKVGLIAARRTGLLRGAKKTKLVGKSEE
Protein: Uncharacterized protein, isoform E (EC 3.1.4.2) (M9PI96)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MAMSRTVLILAVALSLQCAAFVDGASITYGTGNELESGSGSSAACKPTLREFNVRLEVPLAAEERLGLTGDVKALGEWQLSRSVALESLDELNWQATVALQSCRQLEYRYFVYVEDLSGYKQIRRWETHFKPRSLGPCTELQCSQLDVFGITSDNSDLKPQVHRGWLNHEAILQLKFNGEKMFQVHDIETFDPQHVQLKIVPVEKTAGLHVEYSKQEYGKSQLELQPTFGVPYTKGDIVIFHITLPLERMMEQHFRLECYSMSNELLGSATLVTSDLTGSEGVLHLPIKSAKNADETLARLRLPYVAVQPYRYSPLDFKNTYAHYWPKSWPNLDVGHRGNGKSYIADAPAERENTIASFLSAHEHHADMIELDVHLTADGVPVIYHDFGLRTAPPGKQISRPDQLEYVLIKDINYELLKRLRIFSVIAGQVREYPSHNAEPRMEHRIFPTLVEVLEKLPKSLGIDVEIKWPQRRQGGGSEAEQTIDKNFFADKVIHQVIQKGCGRPIIFSSFDADMCTMLRFKQNVFPVMFLTQGETKKWQPFLDLRTRTFIAAVNNAQAFELAGTAPHAEDFLGENASEMLRKAKDLGQIAVIWGDDCNSKERVQYFTRIGATATCYDRSDLFMPEGKREAFFKSPALMAEFAAQCRI
Protein: B-cell CLL/lymphoma 7 protein family member B (Q921K9)
Organism: Mus musculus (Mouse)
Function: Positive regulator of apoptosis. Plays a role in the Wnt signaling pathway, negatively regulating the expression of Wnt signaling components CTNNB1 and HMGA1 (By similarity). Involved in cell cycle progression, maintenance of the nuclear structure and stem cell differentiation (By similarity). May play a role in lung tumor development or progression.
Interaction partners:
- Bromodomain-containing protein 9
- SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 1
- SWI/SNF complex subunit SMARCC1
- B-cell CLL/lymphoma 7 protein family member C
- BRD4-interacting chromatin-remodeling complex-associated protein-like
- AT-rich interactive domain-containing protein 1A
- BRD4-interacting chromatin-remodeling complex-associated protein
- SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily E member 1
- SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily B member 1
- Protein SSXT
Sequence:
MSGRSVRAETRSRAKDDIKKVMAAIEKVRKWEKKWVTVGDTSLRIFKWVPVTDSKEKEKSKSNNTAAREPNGFPSDASANSSLLLEFQDENSNQSSVSDVYQLKVDSSTNSSPSPQQSESLSPAHTSDFRTDDSQPPTLGQEILEEPSLPASEVADEPPTLTKEEPVPVETQTTEEEEDSGAPPLKRFCVDQPVVPQTTSES
Protein: tRNA dimethylallyltransferase (EC 2.5.1.75) (Isopentenyl-diphosphate:tRNA isopentenyltransferase) (IPP transferase) (IPPT) (hGRO1) (tRNA isopentenyltransferase 1) (IPTase) (Q9H3H1)
Organism: Homo sapiens (Human)
Function: Catalyzes the transfer of a dimethylallyl group onto the adenine at position 37 of both cytosolic and mitochondrial tRNAs, leading to the formation of N6-(dimethylallyl)adenosine (i6A37). Mediates modification of a limited subset of tRNAs: tRNA(Ser)(AGA), tRNA(Ser)(CGA), tRNA(Ser)(UGA), as well as partial modification of the selenocysteine tRNA(Ser)(UCA). TRIT1 is therefore required for selenoprotein expression.
Subcellular location: [Isoform 1]: Mitochondrion {ECO:0000269|PubMed:24901367}.; SUBCELLULAR LOCATION: [Isoform 4]: Mitochondrion {ECO:0000305}.; SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm {ECO:0000305}.; SUBCELLULAR LOCATION: [Isoform 3]: Cytoplasm {ECO:0000305}.; SUBCELLULAR LOCATION: [Isoform 5]: Cytoplasm {ECO:0000305}.
Interaction partners:
- Ankyrin repeat domain-containing protein 49
- Leukotriene A-4 hydrolase
- tRNA
- tRNA
- rRNA methyltransferase 2, mitochondrial
- Mitochondrial tRNA methylthiotransferase CDK5RAP1
- Putative GTP-binding protein 6
- Mitochondrial tRNA-specific 2-thiouridylase 1
- 5-taurinomethyluridine-[tRNA] synthase subunit GTPB3, mitochondrial
- pre-rRNA 2'-O-ribose RNA methyltransferase FTSJ3
Sequence:
MASVAAARAVPVGSGLRGLQRTLPLVVILGATGTGKSTLALQLGQRLGGEIVSADSMQVYEGLDIITNKVSAQEQRICRHHMISFVDPLVTNYTVVDFRNRATALIEDIFARDKIPIVVGGTNYYIESLLWKVLVNTKPQEMGTEKVIDRKVELEKEDGLVLHKRLSQVDPEMAAKLHPHDKRKVARSLQVFEETGISHSEFLHRQHTEEGGGPLGGPLKFSNPCILWLHADQAVLDERLDKRVDDMLAAGLLEELRDFHRRYNQKNVSENSQDYQHGIFQSIGFKEFHEYLITEGKCTLETSNQLLKKGIEALKQVTKRYARKQNRWVKNRFLSRPGPIVPPVYGLEVSDVSKWEESVLEPALEIVQSFIQGHKPTATPIKMPYNEAENKRSYHLCDLCDRIIIGDREWAAHIKSKSHLNQLKKRRRLDSDAVNTIESQSVSPDHNKEPKEKGSPGQNDQELKCSV
Protein: Meprin A subunit alpha (EC 3.4.24.18) (Endopeptidase-2) (N-benzoyl-L-tyrosyl-P-amino-benzoic acid hydrolase subunit alpha) (PABA peptide hydrolase) (PPH alpha) (Q16819)
Organism: Homo sapiens (Human)
Subcellular location: Membrane; Single-pass type I membrane protein.
Interaction partners:
- Angiotensin-converting enzyme 2
- Xaa-Pro aminopeptidase 2
- Lysosomal Pro-X carboxypeptidase
- Meprin A subunit beta
- Dipeptidyl peptidase 4
- Neprilysin
- Fetuin-B
- Neurotensin/neuromedin N
- Sucrase-isomaltase, intestinal
Sequence:
MAWIRSTCILFFTLLFAHIAAVPIKYLPEENVHDADFGEQKDISEINLAAGLDLFQGDILLQKSRNGLRDPNTRWTFPIPYILADNLGLNAKGAILYAFEMFRLKSCVDFKPYEGESSYIIFQQFDGCWSEVGDQHVGQNISIGQGCAYKAIIEHEILHALGFYHEQSRTDRDDYVNIWWDQILSGYQHNFDTYDDSLITDLNTPYDYESLMHYQPFSFNKNASVPTITAKIPEFNSIIGQRLDFSAIDLERLNRMYNCTTTHTLLDHCTFEKANICGMIQGTRDDTDWAHQDSAQAGEVDHTLLGQCTGAGYFMQFSTSSGSAEEAALLESRILYPKRKQQCLQFFYKMTGSPSDRLVVWVRRDDSTGNVRKLVKVQTFQGDDDHNWKIAHVVLKEEQKFRYLFQGTKGDPQNSTGGIYLDDITLTETPCPTGVWTVRNFSQVLENTSKGDKLQSPRFYNSEGYGFGVTLYPNSRESSGYLRLAFHVCSGENDAILEWPVENRQVIITILDQEPDVRNRMSSSMVFTTSKSHTSPAINDTVIWDRPSRVGTYHTDCNCFRSIDLGWSGFISHQMLKRRSFLKNDDLIIFVDFEDITHLSQTEVPTKGKRLSPQGLILQGQEQQVSEEGSGKAMLEEALPVSLSQGQPSRQKRSVENTGPLEDHNWPQYFRDPCDPNPCQNDGICVNVKGMASCRCISGHAFFYTGERCQAVQVHGSVLGMVIGGTAGVIFLTFSIIAILSQRPRK
Protein: TUSC5 protein (A5PKU2)
Organism: Homo sapiens (Human)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004370}.
Interaction partners:
Sequence:
MAHPVQSEFPSAQESGSAASLDLPEMEILLTKAENKDDKTLNLSKTLSGPLDLEQNGQGLPFKAISEGHLEAPLPRSPSRASSRRASSIATTSYAQDQEAPRDYLILAVVACFCPVWPLNLIPLIISIMSRSSMQQGNVDGARRLGRLARLLSITLIIMGIVIIMVAVTANFTVQKK
Protein: FAD-dependent monooxygenase nvfK (EC 1.14.-.-) (Farnesyl-DMOA epoxidase nvfK) (Novofumigatonin biosynthesis cluster protein K) (A0A2I1BSV1)
Organism: Aspergillus novofumigatus (strain IBT 16806)
Function: FAD-dependent monooxygenase; part of the gene cluster that mediates the biosynthesis of novofumigatonin, a heavily oxygenated meroterpenoid containing a unique orthoester moiety. The first step of the pathway is the synthesis of 3,5-dimethylorsellinic acid (DMOA) by the polyketide synthase nvfA via condensation of one acetyl-CoA starter unit with 3 malonyl-CoA units and 2 methylations. DMOA is then converted to farnesyl-DMOA by the farnesyltransferase nvfB. Epoxydation by FAD-dependent monooxygenase nvfK, followed by a protonation-initiated cyclization catalyzed by the terpene cyclase nvfL leads to the production of asnavolin H. The short chain dehydrogenase nvfC then as a 3-OH dehydrogenase of asnovolin H to yield chemesin D. There are two branches to synthesize asnovolin A from chemesin D. In one branch, chemesin D undergoes Baeyer-Villiger oxidation by nvfH, methylation by nvfJ, and enoyl reduction by the nvfM D enoylreductase that reduces the double bond between C-5'and C-6', to form respectively asnovolin I, asnovolin K, and asnovolin A. In the other branch, the methylation precedes the Baeyer-Villiger oxidation and the enoyl reduction to yield asnovolin A via the asnovolin J intermediate. Asnovolin A is further converted to fumigatonoid A by the Fe(II)/2-oxoglutarate-dependent dioxygenase nvfI that catalyzes an endoperoxidation reaction. The alpha/beta hydrolase nvfD then acts as an epimerase that converts fumigatonoid A to its C-5' epimer, which then undergoes spontaneous or nvfD-catalyzed lactonization. The following step utilizes the ketoreductase nvfG to produce fumigatonoid B. The dioxygenase nvfE further converts fumigatonoid B into fumigatonoid C. Finally the Fe(II)/2-oxoglutarate-dependent dioxygenase nvfF catalyzes two rounds of oxidation to transform fumigatonoid C into the end product, novofumigatonin A.
Subcellular location: Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MEKAKFKVVIVGGSITGLTLAHCLHQANIDHIVLERRHEIAPQEGASIGLWPNGGQILDQLGLYGELEKLTEPLNVMHVVYPDGFSYSNTLFRQIRERFGYPVFFMDRQKLLDVLYKTYPNKSKILVNKLVTELRQSDGAACVMTDDGSTYEGNLIVGADGVHSRLRSEIWRLADINQPGLVTAEEKQSMTVEYSCIFGISSPLPGLASGEHVNAYMNGLTVLTFHGKGGRVYWFVIQKLDRKFTYPNVPRFSLDDAERSCTALAKIRIWRDICIGHLWQAREVASMTALEENIFTTWHYQRAILLGDSIHKMTPNIGQGANSGIEDAALLASLINHLVNIQAIKQPSDLTVNRMLENFEAIRYPRMEKIYRRSKFGVRMHTRDDLFKRILGRYVIPLTKDRLAVMASQLIVDGAVLDFLPQPKRRSGPGWPKPGNCRDGQNGHKRIQYILMSIVLVAPAWVYIFSSLVW
Protein: UDP-glucuronosyltransferase 2A1 (UDPGT 2A1) (UGT2A1) (EC 2.4.1.17) (P0DTE4)
Organism: Homo sapiens (Human)
Function: UDP-glucuronosyltransferase (UGT) that catalyzes phase II biotransformation reactions in which lipophilic substrates are conjugated with glucuronic acid to increase the metabolite's water solubility, thereby facilitating excretion into either the urine or bile. Essential for the elimination and detoxification of drugs, xenobiotics and endogenous compounds. Catalyzes the glucuronidation of endogenous steroid hormones such as androgens (testosterone and epitestosterone) and estrogens (estradiol and epiestriol). Contributes to bile acid (BA) detoxification by catalyzing the glucuronidation of BA substrates, which are natural detergents for dietary lipids absorption. Shows a high affinity to aliphatic odorants such as citronellol as well as olfactory tissue specificity, and therefore may be involved in olfaction. Shows a potential role in detoxification of toxic waste compounds in the amniotic fluid before birth, and air-born chemical after birth.
Subcellular location: Membrane {ECO:0000305|PubMed:10359671}; Single-pass type I membrane protein {ECO:0000255}. Endoplasmic reticulum membrane {ECO:0000305|PubMed:19858781}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MLNNLLLFSLQISLIGTTLGGNVLIWPMEGSHWLNVKIIIDELIKKEHNVTVLVASGALFITPTSNPSLTFEIYKVPFGKERIEGVIKDFVLTWLENRPSPSTIWRFYQEMAKVIKDFHMVSQEICDGVLKNQQLMAKLKKSKFEVLVSDPVFPCGDIVALKLGIPFMYSLRFSPASTVEKHCGKVPYPPSYVPAVLSELTDQMSFTDRIRNFISYHLQDYMFETLWKSWDSYYSKALGGLLLCCPGWSAVADLGSLQPLLPGFKRFSRLSLHCSWDYRLPAGRPTTLCETMGKAEIWLIRTYWDFEFPRPYLPNFEFVGGLHCKPAKPLPKVLWRYKGKKPATLGNNTQLFDWIPQNDLLGHPKTKAFITHGGTNGIYEAIYHGVPMVGVPMFADQPDNIAHMKAKGAAVEVNLNTMTSVDLLSALRTVINEPSYKENAMRLSRIHHDQPVKPLDRAVFWIEFVMRHKGAKHLRVAAHDLTWFQYHSLDVIGFLLVCVTTAIFLVIQCCLFSCQKFGKIGKKKKRE
Protein: DNA polymerase lambda (OsPolL) (Pol Lambda) (EC 2.7.7.7) (EC 4.2.99.-) (Q67VC8)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Repair polymerase involved in base excision repair (BER) and responsible for repair of lesions that give rise to abasic (AP) sites in DNA. Has both DNA polymerase and terminal transferase activities. Has a 5'-deoxyribose-5-phosphate lyase (dRP lyase) activity.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Os01g0737300 protein
- Os01g0685500 protein
- Os06g0144000 protein
- Putative DNA ligase 4
- Transcription factor LAX PANICLE 1
- Os03g0293400 protein
- ATP-dependent DNA helicase 2 subunit KU70
- Proliferating cell nuclear antigen
- DNA ligase
- Exonuclease 1
Sequence:
MAPKRKPPARAAAAKLDPDGMFRGVSAFVVPHAVQSRRLEVWKQRLAQMGGRVQEKLAAKGGGGAVTHVLAADAKALLRELDAAWLHRFRGSVVSFEWLEECLKSGERLPEHKFAINYEEEFKPKKEGGAAGSGVLQSAKRSKISSDGPENRKETAGGNRESRDAIAHPNEDSDVVKGPSTCTSSQSASGDSKETIASQNAFKAEEASSGESSTYAPPDLNRNITEIFGKLINIYRALGDDRRSFSYYKAIPVIEKLPFKIESADQVKDLPAIGKSLKDHINEIVNTGKLSKLEHFENDEKVRTVSLFGEVWGVGPATALKLYDKGHRTLDDLQKDDSLTSAQRIGLKFFDDIKQRIPRHEVSEMEKLLQEVGTDILPGVIIVCGGSYRRGKSSCGDMDIIITHPDGESHVGFLPKFVQRLKGINFLREDLIFSIHSIEGTDCGVDTYFGLCTYPGRELRHRIDLKVYPRNRHAFGLLAWTGNDVLNRRLRILADSKGYILDDTGLYLATPGSGGKRGGRSDAIINCDTEKDVFDTLGFPWLEPHERNL
Protein: Pyridoxal 5'-phosphate synthase-like subunit PDX1.2 (AtPDX1.2) (AtPDX1;3) (Q9ZNR6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: The protein has no function in the formation of pyridoxal 5'-phosphate.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16157873}.
Interaction partners:
- Probable pyridoxal 5'-phosphate synthase subunit PDX2
- Pyridoxal 5'-phosphate synthase subunit PDX1.3
- Pyridoxine/pyridoxamine 5'-phosphate oxidase 1, chloroplastic
- Pyridoxal kinase
- Inorganic pyrophosphatase 1
- Pyridoxal 5'-phosphate synthase subunit PDX1.1
- Thiamine phosphate phosphatase-like protein
- Inorganic pyrophosphatase 2
- Pyridoxine/pyridoxamine 5'-phosphate oxidase 2
- transaldolase
Sequence:
MADQAMTDQDQGAVTLYSGTAITDAKKNHPFSVKVGLAQVLRGGAIVEVSSVNQAKLAESAGACSVIVSDPVRSRGGVRRMPDPVLIKEVKRAVSVPVMARARVGHFVEAQILESLAVDYIDESEIISVADDDHFINKHNFRSPFICGCRDTGEALRRIREGAAMIRIQGDLTATGNIAETVKNVRSLMGEVRVLNNMDDDEVFTFAKKISAPYDLVAQTKQMGRVPVVQFASGGITTPADAALMMQLGCDGVFVGSEVFDGPDPFKKLRSIVQAVQHYNDPHVLAEMSSGLENAMESLNVRGDRIQDFGQGSV
Protein: Casanova (SRY-box containing gene 32) (SRY-box transcription factor 32) (Q90Z46)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MYLDRMLPDLEMRHTTRMPEIQQCHYLQHQNDEQRRTAHCPASGPLSPVSVGSESSCSSPEAKAPVETRVRRPLNAFIIWTKEERRRLAQLNPDLENTDLSKILGKTWKAMSLADKRPYMQEAERLRIQHTIDYPNYKYRPRRRKCNKRSSKMPSSENVSSPNATFDLSYMFQGQAPQRPYNQINSYRLPHNGFSFENHSSSYHFEATSSSGNVFHGGATSMNLSNVHLPRSAYSESLLYSQHSVQQSAVELHDRWGTEGCACVLCLGGPSLEFYLEQVRSDMLDQLDRSEFDQYLNPAQTLDHSKK
Protein: Cadherin 13 (F1M7X3)
Organism: Rattus norvegicus (Rat)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004370}.
Interaction partners:
Sequence:
MAELVIVGGKDIQGSLQDIFKFARTSPVPRQKRSIVVSPILIPENQRQPFPRDVGKVVDSDRPEGSKFRLTGKGVDQDPKGTFRINENTGSVSVTRTLDRETIATYQLFVETTDASGRTLEGPVPLEVIVIDQNDNRPIFREGPYIGHVMEGSPTGTTVMRMTAFDADDPATDNALLRYNIRQQTPDKPSPNMFYIDPEKGDIVTVVSPALLDRETLENPKYELIIEAQDMAGLDVGLTGTATATIVIDDKNDHSPKFTKKEFQATVEEGAVGVIVNLTVEDKDDPATGAWRAAYTIINGNPGQSFEIHTNPQTNEGMLSVVKPLDYEISAFHTLLIKVENEDPLVPDVSYGPSSTATVHITVLDVNEGPVFYPDPMMVTKQENISVGSVLLTVNATDPDSLQHQTIRYSVYKDPAGWLSINPINGTVDTTAVLDRESPFVHNSVYTALFLAIDSGNPPATGTGTLMITLEDVNDNAPVIYPTVAEVCDDARNLSVVILGASDKDLHPNTDPFKFEIHKQTVPDKVWKISKINNTHALVSLLQNLNKANYNLPIMVTDSGKPPMTNITDLRVQVCSCKNSKVDCNAAGTLHLSLSLLLLFSLLSLLSGL
Protein: Biogenesis of lysosome-related organelles complex 1 subunit 2 (BLOC-1 subunit 2) (Q95XD3)
Organism: Caenorhabditis elegans
Function: Component of the biogenesis of lysosome-related organelles complex-1 (BLOC-1) involved in gut granule biogenesis.
Interaction partners:
- Biogenesis of lysosome-related organelles complex 1 subunit 1
- KxDL domain-containing protein
- SNAPIN protein homolog
- Biogenesis of lysosome-related organelles complex 1 subunit 5
- Biogenesis of lysosome-related organelles complex 1 subunit 4
- BLOC-1-related complex subunit 8 homolog
- Dysbindin protein homolog
- Biogenesis of lysosome-related organelles complex 1 subunit 6
- BLOC-1-related complex subunit 7
- ADP-ribosylation factor-like protein 8B
Sequence:
MAEINERASTSSPPVPSTPAPVPHIRQLADNMTDKVGQFFQHQLEGSIEEYKLLETMNNTTAQRYVDMKVVAEKVAGKLDNLNQKYENLRPYLSQIDAMDESTRRLEEATAVLENYVTQLESKLTNIQQQSQ
Protein: Inter-alpha-trypsin inhibitor heavy chain H3 (ITI heavy chain H3) (ITI-HC3) (Inter-alpha-inhibitor heavy chain 3) (Serum-derived hyaluronan-associated protein) (SHAP) (Q06033)
Organism: Homo sapiens (Human)
Function: May act as a carrier of hyaluronan in serum or as a binding protein between hyaluronan and other matrix protein, including those on cell surfaces in tissues to regulate the localization, synthesis and degradation of hyaluronan which are essential to cells undergoing biological processes.
Subcellular location: Secreted.
Interaction partners:
- Protein AMBP
- Apolipoprotein A-I
- Inter-alpha-trypsin inhibitor heavy chain H2
- Beta-2-glycoprotein 1
- Alpha-2-HS-glycoprotein
- Inter-alpha-trypsin inhibitor heavy chain H1
- Apolipoprotein E
Sequence:
MAFAWWPCLILALLSSLAASGFPRSPFRLLGKRSLPEGVANGIEVYSTKINSKVTSRFAHNVVTMRAVNRADTAKEVSFDVELPKTAFITNFTLTIDGVTYPGNVKEKEVAKKQYEKAVSQGKTAGLVKASGRKLEKFTVSVNVAAGSKVTFELTYEELLKRHKGKYEMYLKVQPKQLVKHFEIEVDIFEPQGISMLDAEASFITNDLLGSALTKSFSGKKGHVSFKPSLDQQRSCPTCTDSLLNGDFTITYDVNRESPGNVQIVNGYFVHFFAPQGLPVVPKNVAFVIDISGSMAGRKLEQTKEALLRILEDMQEEDYLNFILFSGDVSTWKEHLVQATPENLQEARTFVKSMEDKGMTNINDGLLRGISMLNKAREEHRIPERSTSIVIMLTDGDANVGESRPEKIQENVRNAIGGKFPLYNLGFGNNLNYNFLENMALENHGFARRIYEDSDADLQLQGFYEEVANPLLTGVEMEYPENAILDLTQNTYQHFYDGSEIVVAGRLVDEDMNSFKADVKGHGATNDLTFTEEVDMKEMEKALQERDYIFGNYIERLWAYLTIEQLLEKRKNAHGEEKENLTARALDLSLKYHFVTPLTSMVVTKPEDNEDERAIADKPGEDAEATPVSPAMSYLTSYQPPQNPYYYVDGDPHFIIQIPEKDDALCFNIDEAPGTVLRLIQDAVTGLTVNGQITGDKRGSPDSKTRKTYFGKLGIANAQMDFQVEVTTEKITLWNRAVPSTFSWLDTVTVTQDGLSMMINRKNMVVSFGDGVTFVVVLHQVWKKHPVHRDFLGFYVVDSHRMSAQTHGLLGQFFQPFDFKVSDIRPGSDPTKPDATLVVKNHQLIVTRGSQKDYRKDASIGTKVVCWFVHNNGEGLIDGVHTDYIVPNLF