wanglab/gogpt-training-data huggingface dataset:
Protein: Cullin-5 (CUL-5) (Vasopressin-activated calcium-mobilizing receptor 1) (VACM-1) (Q93034)
Organism: Homo sapiens (Human)
Function: Core component of multiple SCF-like ECS (Elongin-Cullin 2/5-SOCS-box protein) E3 ubiquitin-protein ligase complexes, which mediate the ubiquitination and subsequent proteasomal degradation of target proteins. As a scaffold protein may contribute to catalysis through positioning of the substrate and the ubiquitin-conjugating enzyme. The functional specificity of the E3 ubiquitin-protein ligase complex depends on the variable substrate recognition component. ECS(SOCS1) seems to direct ubiquitination of JAK2. ECS(KLHDC1) complex is part of the DesCEND (destruction via C-end degrons) pathway and mediates ubiquitination and degradation of truncated SELENOS selenoprotein produced by failed UGA/Sec decoding, which ends with a glycine. As part of a multisubunit complex composed of elongin BC complex (ELOB and ELOC), elongin A/ELOA, RBX1 and CUL5; polyubiquitinates monoubiquitinated POLR2A. May form a cell surface vasopressin receptor.
Subcellular location: Nucleus {ECO:0000269|PubMed:35633597, ECO:0000269|PubMed:38418882}. Note=Localizes to sites of DNA damage in a UBAP2 and UBAP2L-dependent manner. {ECO:0000269|PubMed:35633597}.
Interaction partners:
- Cytokine-inducible SH2-containing protein
- E3 ubiquitin-protein ligase RBX1
- Elongin-C
- Core-binding factor subunit beta
- Elongin-B
- Ubiquitin-like protein NEDD8
- RING-box protein 2
- Suppressor of cytokine signaling 2
- E3 ubiquitin-protein ligase ARIH2
- DNA dC->dU-editing enzyme APOBEC-3G
Sequence:
MATSNLLKNKGSLQFEDKWDFMRPIVLKLLRQESVTKQQWFDLFSDVHAVCLWDDKGPAKIHQALKEDILEFIKQAQARVLSHQDDTALLKAYIVEWRKFFTQCDILPKPFCQLEITLMGKQGSNKKSNVEDSIVRKLMLDTWNESIFSNIKNRLQDSAMKLVHAERLGEAFDSQLVIGVRESYVNLCSNPEDKLQIYRDNFEKAYLDSTERFYRTQAPSYLQQNGVQNYMKYADAKLKEEEKRALRYLETRRECNSVEALMECCVNALVTSFKETILAECQGMIKRNETEKLHLMFSLMDKVPNGIEPMLKDLEEHIISAGLADMVAAAETITTDSEKYVEQLLTLFNRFSKLVKEAFQDDPRFLTARDKAYKAVVNDATIFKLELPLKQKGVGLKTQPESKCPELLANYCDMLLRKTPLSKKLTSEEIEAKLKEVLLVLKYVQNKDVFMRYHKAHLTRRLILDISADSEIEENMVEWLREVGMPADYVNKLARMFQDIKVSEDLNQAFKEMHKNNKLALPADSVNIKILNAGAWSRSSEKVFVSLPTELEDLIPEVEEFYKKNHSGRKLHWHHLMSNGIITFKNEVGQYDLEVTTFQLAVLFAWNQRPREKISFENLKLATELPDAELRRTLWSLVAFPKLKRQVLLYEPQVNSPKDFTEGTLFSVNQEFSLIKNAKVQKRGKINLIGRLQLTTERMREEENEGIVQLRILRTQEAIIQIMKMRKKISNAQLQTELVEILKNMFLPQKKMIKEQIEWLIEHKYIRRDESDINTFIYMA
Protein: tRNA(Thr) (cytosine(32)-N(3))-methyltransferase (EC 2.1.1.268) (Actin-binding protein of 140 kDa) (tRNA methyltransferase of 140 kDa) (Q08641)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: S-adenosyl-L-methionine-dependent methyltransferase that mediates N(3)-methylcytidine modification of residue 32 of the tRNA anticodon loop of tRNA(Thr) and tRNA(Ser). N(3)-methylcytidine methylation of tRNA(Thr) requires the N6-threonylcarbamoylation of tRNA (t6A37) by the EKC/KEOPS complex as prerequisite. N(3)-methylcytidine methylation of tRNA(Ser) requires the formation of N(6)-dimethylallyladenosine(37) (i6A37) by MOD5 as prerequisite. Methylation of tRNA(Ser) is also stimulated by SES1. Binds F-actin and shows weak F-actin cross-linking activity.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:9467951}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:9467951}. Note=Cytoplasmic and cortical cytoskeleton. {ECO:0000269|PubMed:9467951}.
Interaction partners:
- Actin
- Fimbrin
- tRNA
- Actin-binding protein
- BNI1-related protein 1
- Telomere replication protein EST3
- Tropomyosin-1
- Coronin-like protein
- Serine--tRNA ligase, cytoplasmic
- tRNA
Sequence:
MGVADLIKKFESISKEEGDATVDTNSSSKPLKSNDETKELHQQESTAVPQEVDVNEEFENEPETINSSRTAEKPLETNLPKPETNEEDEEEGSMSENKIYSKGENADINVNDFQEYKEMENTGAEVLASSVEESDAIQEGVAEETEGIATPKQKENEKNDESEEESANNASEPAEEYSQSEEDADIEQSNGKETENAENASQQANDGSTSTTTSKNKKKKNKKKNKKKRNGNVNTNANVDDSTKTGENDDTTGDTTSSTTSAIQEVNDLEVVDDSCLGIDQQHNREHLKALTQDVKEETLENIAHEGRGDNTGDQNAVEKSDFEKSDTEGSRIGRDLPFEFGKRNLTEESDVWDHNAWDNVEWGEEQVQQAEEKIKEQFKHPVPEFDKKLYNENPARYWDIFYKNNKENFFKDRKWLQIEFPILYASTRKDAEPVTIFEIGCGAGNTFFPILKDNENENLRIIAADFAPRAVELVKNSEQFNPKYGHATVWDLANPDGNLPDGVEPHSVDIAVMIFVFSALAPNQWDQAMDNLHKILKPGGKIIFRDYGAYDLTQVRFKKNRILEENFYVRGDGTRVYFFSEEKLREIFTKKYFLENKIGTDRRLLVNRKRQLKMYRCWVQAVFDVPQ
Protein: Partner of bursicon (Bursicon subunit beta) (Q9VJS7)
Organism: Drosophila melanogaster (Fruit fly)
Function: Final heterodimeric neurohormone released at the end of the molting cycle, involved in the sclerotization (tanning) of the insect cuticle, melanization and wing spreading. Heterodimer specifically activates the G protein-coupled receptor rk.
Subcellular location: Secreted {ECO:0000269|PubMed:15703293}.
Interaction partners:
- Bursicon
- Cardioactive peptide
- Rickets
- Eclosion hormone
Sequence:
MHVQELLFVAAILVPQCLRALRYSQGTGDENCETLKSEIHLIKEEFDELGRMQRTCNADVIVNKCEGLCNSQVQPSVITPTGFLKECYCCRESFLKEKVITLTHCYDPDGTRLTSPEMGSMDIRLREPTECKCFKCGDFTR
Protein: Dual specificity testis-specific protein kinase 1 (EC 2.7.12.1) (Testicular protein kinase 1) (O70146)
Organism: Mus musculus (Mouse)
Function: Dual specificity protein kinase activity catalyzing autophosphorylation and phosphorylation of exogenous substrates on both serine/threonine and tyrosine residues (By similarity). Regulates the cellular cytoskeleton by enhancing actin stress fiber formation via phosphorylation of cofilin and by preventing microtubule breakdown via inhibition of TAOK1/MARKK kinase activity (By similarity). Inhibits podocyte motility via regulation of actin cytoskeletal dynamics and phosphorylation of CFL1. Positively regulates integrin-mediated cell spreading, via phosphorylation of cofilin (By similarity). Suppresses ciliogenesis via multiple pathways; phosphorylation of CFL1, suppression of ciliary vesicle directional trafficking to the ciliary base, and by facilitating YAP1 nuclear localization where it acts as a transcriptional corepressor of the TEAD4 target genes AURKA and PLK1 (By similarity). Probably plays a central role at and after the meiotic phase of spermatogenesis (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q15569}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q63572}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q15569}. Cell projection, lamellipodium {ECO:0000250|UniProtKB:Q63572}. Note=Colocalizes with SPRY4 in vesicular spots in the cytoplasm (By similarity). Localized to F-actin-rich lamellipodia at the cell periphery following fibronectin-mediated cell adhesion of Schwann cells (By similarity). {ECO:0000250|UniProtKB:Q15569, ECO:0000250|UniProtKB:Q63572}.
Interaction partners:
- Alpha-parvin
Sequence:
MAGERPPLRGPGPGEAPGEGPGGAGGGPGRGRPSSYRALRSAVSSLARVDDFDCAEKIGAGFFSEVYKVRHRQSGQVMVLKMNKLPSNRSNTLREVQLMNRLRHPNILRFMGVCVHQGQLHALTEYMNGGTLEQLLSSPEPLSWPVRLHLALDIAQGLRYLHAKGVFHRDLTSKNCLVRREDRGFTAVVGDFGLAEKIPVYREGTRKEPLAVVGSPYWMAPEVLRGELYDEKADVFAFGIVLCELIARVPADPDYLPRTEDFGLDVPAFRTLVGNDCPLPFLLLAIHCCSMEPSTRAPFTEITQHLEQILEQQPEATPLAKPPLTKAPLTYNQGSVPRGGPSATLPRPDPRLSRSRSDLFLPPSPESPPSWGDNLTRVNPFSLREDLRGGKIKLLDTPCKPATPLPLVPPSPLTSTQLPLVTTPDILVQPETPVRRCRSLPSSPELPRRMETALPGPGPSPMGPTEERMDCEGSSPEPEPPGLAPQLPLAVATDNFISTCSSASQPWSPRSGPPLNNNPPAVVVNSPQGWAREPWNRAQHSLPRAAALERTEPSPPPSAPREPEEGLPCPGCCLGPFSFGFLSMCPRPTPAVARYRNLNCEAGSLLCHRGHHAKPPTPSLQLPGARS
Protein: Amino acid transporter, putative (Q381J1)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MSDKGKCATDVENTTSPVTQQTFPAEPSGIVDASEPIHTDDKNKRVDARGDAPPSVWQSFSAKMKHIAGTVVPYGGLVSSVFNLCSVCIGAGILGLPAAANRSGLVMAMLYLVVIGGLGVFSLHILSLVMEKTGLRTFEHTARGVMGRRFEYFVVVIRWINSFGATVSYVISVGHVLNPIIEKSCGAPEFLRTPGGIRLLTALTWMVFMLPLVLPKRVNSLRYVSGFAIIFVLYFVFAIVIHGAQSGLPKLTSDEEDGVKLFNTGNSAIASVGVFMFAYVCQINCYEVYWEMKKRSCARFTVYAAISMAFCGILYALTILFAYGEFGGAIDNSILLMYNPITEVMMMIGFIGMVVKLCVAYALQTMALRNTIYHVLGWELETLPYWKHFSFVIPLSLVVLLAGLFIPNINTVFGIVGAICGGFLSFIFPSLFYMYSGKWTRRNVGNFHFFGTYFLLCAGVVGLVFGTVSVVSENILALIANKVEVVRVRAPETQC
Protein: DNA-directed RNA polymerases I, II, and III subunit RPABC2 (RNA polymerases I, II, and III subunit ABC2) (RNA polymerase II, I and III subunit F) (RPB6 homolog) (Q24320)
Organism: Drosophila melanogaster (Fruit fly)
Function: DNA-dependent RNA polymerases catalyze the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Common component of RNA polymerases I, II and III which synthesize ribosomal RNA precursors, mRNA precursors and many functional non-coding RNAs, and small RNAs, such as 5S rRNA and tRNAs, respectively. Pol II is the central component of the basal RNA polymerase II transcription machinery. Pols are composed of mobile elements that move relative to each other. In Pol II, RPB6 is part of the clamp element and together with parts of RPB1 and RPB2 forms a pocket to which the RPB4-RPB7 subcomplex binds (By similarity).
Subcellular location: Nucleus.
Interaction partners:
- DNA-directed RNA polymerases I, II, and III subunit RPABC3
- DNA-directed RNA polymerase I subunit RPA1
- DNA-directed RNA polymerases I, II, and III subunit RPABC1
- DNA-directed RNA polymerase II subunit RPB9
- DNA-directed RNA polymerase I subunit RPA2
- DNA-directed RNA polymerase II subunit RPB3
- DNA-directed RNA polymerase III subunit RPC2
- DNA-directed RNA polymerases I, II, and III subunit RPABC4
- DNA-directed RNA polymerase II subunit RPB1
- DNA-directed RNA polymerases I and III subunit RPAC1
Sequence:
MDDADYDNDDVGGDDFDDVDEDVDEDINQEEEADNIEIIAPGGAGGGGVPKSKRITTKYMTKYERARVLGTRALQIAMCAPIMVELDGETDPLQIAMKELKQKKIPIIIRRYLPDHSYEDWSIDELIMVDN
Protein: Succinate dehydrogenase [ubiquinone] iron-sulfur subunit, mitochondrial (EC 1.3.5.1) (Iron-sulfur subunit of complex II) (Ip) (Malate dehydrogenase [quinone] iron-sulfur subunit) (EC 1.1.5.-) (P21913)
Organism: Rattus norvegicus (Rat)
Function: Iron-sulfur protein (IP) subunit of the succinate dehydrogenase complex (mitochondrial respiratory chain complex II), responsible for transferring electrons from succinate to ubiquinone (coenzyme Q).
Subcellular location: Mitochondrion inner membrane {ECO:0000250|UniProtKB:Q9YHT2}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9YHT2}; Matrix side {ECO:0000250|UniProtKB:Q9YHT2}.
Interaction partners:
- Succinate--CoA ligase subunit alpha, mitochondrial
- Succinate dehydrogenase cytochrome b560 subunit, mitochondrial
- Succinate dehydrogenase cytochrome b small subunit, mitochondrial
- Succinate dehydrogenase flavoprotein subunit, mitochondrial
- Fumarate hydratase, mitochondrial
- NADH dehydrogenase 1 beta subcomplex subunit 8, mitochondrial
- Succinate--CoA ligase subunit beta, mitochondrial
- NADH dehydrogenase iron-sulfur protein 2, mitochondrial
- NADH dehydrogenase iron-sulfur protein 3, mitochondrial
- Cytochrome b-c1 complex subunit Rieske, mitochondrial
Sequence:
MAAVVGVSLKRGFSATALGRVGLQFQACREAQTAAAAAPRIKTFAIYRWDPDKAGDKPRMQTYKVDLNKCGPMVLDALIKIKNEIDSTLTFRRSCREGICGSCAMNINGGNTLACTRRIDTDLGKVSKIYPLPHMYVIKDLVPDLSNFYAQYKSIEPYLKKKDESQEGKQQYLQSIEDREKLDGLYECILCACCSTSCPSYWWNGDKYLGPAVLMQAYRWMIDSRDEFTEERLAKLQDPFSLYRCHTIMNCTQTCPKGLNPGKAIAEIKKMMATYKEKRALA
Protein: ST13 Hsp70 interacting protein (F6VDH7)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MGGKVPPATQKAKSEENTKEEKPDSKKVEEDLKADEPSSEESDLEIDKEGVIEPDTDAPQEMGDENAEITEEMMDQANDKKVAAIEALNDGELQKAIDLFTDAIKLNPRLAILYAKRASVFVKLQKPNAAIRDCDRAIEINPDSAQPYKWRGKAHRLLGHWE
Protein: G protein-coupled receptor 54-2 (KISS1 receptor b) (A8CAH4)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
Sequence:
MAETNSTGDAAEHIMCNYDANIYQCNQTDLMRFQSPVPLTDTWLVPLFFTLIMFVGLVGNLIVIYVVIKNQQMKTVTNLYIVNLATTDILFLVCCVPFTATVYVLPSWIFGDFMCRLVNYLQQVTAQATCITLSAMSVDRFYVTVYPLQSLHHRTPQMALSVCTTIWICSSLLSVPIALYQHTESSYWFGPQTYCTETFPSVIHKRVYLLYSFLAVYLLPLITICMCYTFMLKRMAQATVQPVQGCNQISLQTSSERAEAVRSRVSRMVVVMVLLFLLCWGPIQILILLQAFCAEDVSRSYTLYKLKIWAHGMSYSNSSINPVIYAFMGANFRKAFRSVCPLIFKRRSTEPLATYNREMNFLSS
Protein: Mitogen-activated protein kinase kinase kinase (EC 2.7.11.25) (F1LRA7)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MESSRSLLGCLASAAAAPPGEDATGAGAEEEEDEEEAAAELGSHATLPYWTAVFEYEAAGEDELTLRLGDVVEVLSKDSQVSGDEGWWTGQLNQRVGIFPSNYVTPRSAFSSRCQPGTEDPSCYPPIQLLEIDFAELTLEEIIGIGGFGKVYRAFWVGDEVAVKAARHDPDEDISQTIENVRQEAKLFAMLKHPNIIALRGVCLKEPNLCLVMEFARGGPLNRVLSGKRVPPDILVNWAVQIARGMNYLHDEAIVPVIHRDLKSSNILILQKVENGDLSNKTLKITDFGLAREWHRTTKMSAAGTYAWMAPEVIRASMFSKGSDVWSYGVLLWELLTGEVPFRGIDGLAVAYGVAMNKLALPIPSTCPEPFAKLMEDCWNPDPHSRPSFSSILDQLTTIEESGFFEMPKDSFHCLQDDWKHEIQEMFDQLRAKEKELRTWEEELTRAALQQKNQEELLRRREQELAEREIDILERELNIIIHQLCQEKPRVKKRKGKFRKSRLKLKDGNRISLPSDFQHKFTVQASPTMDKRKSLISNRSSPPASPTIIPRLRAIQLTPGESSKTWGRSSVVPKEEGEEEEKRAPKKKGRTWGPGTLGQKELTSGDEGSPQRREKANGLSTPSESPHFHLGLKSLVDGYKQWSSSAPNLGKGPRSSPALPGFTSLMEIEDEDSEGPGSGENHLQHSPNQSYLCIPFPRGEDGDGPSSDGIHEEPTPVNSATSTPQLTPTNSLKRSGTHHRRCEVALLGCGAVLAATGLGFDLLEAGKCQLLPPEEPEPPAREEKKRREGLFQRASRPRRSTSPPSRKLFKKEEPMTLLGDPSASLTLLSLSSISECNSTRSLLRSDSDEIVVYEMPVSPVEAPPLTQCTQNPLVNVRVERFKRDPNQSLTPTHVTLTAPTQPSGHRRTPSDGALKPASVPPALGSRSPSSNGVSPGPGAGMLKTPSPSRDPGEFPRLPDPNVVFPPTPRRWNTQRDSTLERPKTLEFLPRPRPSANRQRLDPWWFVSPSHARSASPANSSSTETPSNLDSCFASSSSTVEERPGLPALLPLQAGPLPPAERTLLDLDAEGQSQDSTVPLCRAELNAHGPSPYEIQQEFWS
Protein: COUP transcription factor 2 (COUP-TF2) (Apolipoprotein AI regulatory protein 1) (ARP-1) (COUP transcription factor II) (COUP-TF II) (Nuclear receptor subfamily 2 group F member 2) (P43135)
Organism: Mus musculus (Mouse)
Function: Ligand-activated transcription factor. Activated by high concentrations of 9-cis-retinoic acid and all-trans-retinoic acid, but not by dexamethasone, cortisol or progesterone (in vitro). Regulation of the apolipoprotein A-I gene transcription. Binds to DNA site A. May be required to establish ovary identity during early gonad development.
Subcellular location: Nucleus {ECO:0000269|PubMed:7947324}.
Interaction partners:
- Nuclear receptor corepressor 2
- Transcription factor SOX-18
- Histone acetyltransferase p300
- Nuclear receptor corepressor 1
Sequence:
MAMVVSTWRDPQDEVPGSQGSQASQAPPVPGPPPGAPHTPQTPGQGGPASTPAQTAAGGQGGPGGPGSDKQQQQQHIECVVCGDKSSGKHYGQFTCEGCKSFFKRSVRRNLSYTCRANRNCPIDQHHRNQCQYCRLKKCLKVGMRREAVQRGRMPPTQPTHGQFALTNGDPLNCHSYLSGYISLLLRAEPYPTSRFGSQCMQPNNIMGIENICELAARMLFSAVEWARNIPFFPDLQITDQVALLRLTWSELFVLNAAQCSMPLHVAPLLAAAGLHASPMSADRVVAFMDHIRIFQEQVEKLKALHVDSAEYSCLKAIVLFTSDACGLSDVAHVESLQEKSQCALEEYVRSQYPNQPTRFGKLLLRLPSLRTVSSSVIEQLFFVRLVGKTPIETLIRDMLLSGSSFNWPYMAIQ
Protein: Uncharacterized protein YER158C (P40095)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Interaction partners:
- Uncharacterized protein YAL065C
Sequence:
MLQQGSSSRRSLHGNDFHTLTSPSRRDSLSIPRAVDARSASTIDLFYIPDATVSRRHSTLVANRSDNNGNGAPMRQYNKPNFASSSTSSLPSTRNRPSRYDNMNMNMNMNMNMNMNMNMNMNNHTTSDHNAHPQYRCRPNPSRRHSLMTIPEKYSGSRYSLRSSPPTYSNPRVRKELTPFQLQRKQMKSAFQFPNGENFTPRNQIARLPPSSTFPDSPSSSSLPLTQTGGPSSADNDSIATGTNNRSPQQTKAADANQKSESESPKAIRSNSKKISRFFRKIWSSKSSNSADSVEENSKTKQKRKNPERVVPEPITSLDQPVEIIKQSFSTVNNHETAVPSIKDSGIVQELTALGDNNRIPVLPPPRSPNRPTLSDKRTTKLYYCSQDSSNEDIAPEEKSTVFLKRLQDEWSTVYLNKLPLTASVPSSLSTTTDAANSSFINSSISSPAPSSSSSSSLVSRGPMQSISSSPTPAPSSGSSKSKNAVKSLRFADEIYVNDTWSAADYCRCDNTFLNNFFKGKSQDITNPSTFVGNNLSSTKNISNIEIKMEVNEFKRKEMRVHQDSAKYTHYYL
Protein: Cytoplasmic tRNA 2-thiolation protein 2 (O65628)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Plays a central role in 2-thiolation of mcm(5)S(2)U at tRNA wobble positions of tRNA(Lys), tRNA(Glu) and tRNA(Gln). May act by forming a heterodimer with NCS6/CTU1 that ligates sulfur from thiocarboxylated URM1 onto the uridine of tRNAs at wobble position.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03054}.
Interaction partners:
- Cytoplasmic tRNA 2-thiolation protein 1
- 2-thiocytidine tRNA biosynthesis protein, TtcA
- tRNA
- Adenylyltransferase and sulfurtransferase MOCS3
- Nucleobase-ascorbate transporter 12
- Acetylornithine deacetylase
- Purine-uracil permease NCS1
- DNA replication licensing factor MCM5
- Nucleobase-ascorbate transporter 3
- Nucleobase-ascorbate transporter 1
Sequence:
MACNSSGCESGCYDREKDNGSKIVDDAVSGGGNHESVCVKCKCNAPMTFGDGGFDDGRFCADCFRNNVFGKFRLAVTSHAMITPSDNVLVAFSGGSSSRVSLQFVHELQIKALKNYEASRDRSLPVFGVGVAFVDETAAFPALSTEMIDAIEWVRYTVSCLSPPAKDLHVVPVESIFGSDSLDARDRLLKLLDSVPDDTGKEDLLLHLKMLSLQKVAAENGYNRLVLGSCTSRIASHVLTATVKGRGYSLSADIQHVDARWKVPIVLPLRDCVRLEITRLCLLDGLKTVELACRSQCGINDLVSSFVALLQEENPSRECTIVRTAAKLTPFYFNKIPETDDSNVPMATQRRLKRFNLKYDGSMTTEAFCPICNGPLNRSDSSELDTFEEGQESDVLYAACCSSCRFQILPQDGSSLEQFSSFLPDHMISQVKHQKVDSQAYLREKIKDCLLLDDEEVV
Protein: Cullin-3 (Cullin-B) (P53202)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: As part of the CRL3 E3 ubiquitin ligase complex; polyubiquitylates monoubiquitylated RNA polymerase II subunit RPO21 to trigger its proteolysis; plays a role in global genomic repair.
Interaction partners:
- RING-box protein HRT1
- Elongin-C
- DNA repair protein RAD7
- Suppressor of kinetochore protein 1
- DNA repair protein RAD16
- Elongin-A
- COP9 signalosome complex subunit 5
- UBX domain-containing protein 5
- NEDD8-like protein RUB1
- Cullin-8
Sequence:
MITNKKIKISVPEKLGLSEESFEESWETVKYAIDHIYSDDMADLSFEQVYKTIYTIVLNKKGPILYNRLKDYLIQKLALLRETIVKDNTHDYEFLGTMARLWEVQCHCFKITGDLMMYMDKVYCKPNRCMEVYDMCLDLFRIEILQKCSSSLISALISDIERIRNLGSVDSEHTSLWKVLIGMMETLHDNRDSFFLTDFEPVLISATEEYYNKAIDIELLTPIESLEKIRKLRQFESMLDSSFLNVDSHNKLKTVLENVLIWGKLSDIIEDLTHEAMVISNGKLLQEIYDLSSEEKYRVTVIESIKSYINKNAINIPFNEGNRKKGQNAITWSSEIVELYRSQHSFLESIDFGSVRLNNLTGDVSNAILGDVFSMYFSKEGALPSEYLSTYVDHCMKRTKEKDAEIVKIKQDLLDSTKLIGLLTEKDIFEKIYKKQLSRRLLQQRSLVEIEKWMVQMIKKVLGTFFTSKLEIMLRDISLSSEMYQAFQHSTINSIEYLSFAPQVLTRTSWPFQSTNPIDEGISLPPRMSQILAGFEGYYSLKYKERVLKWAHHLSVIEIGCQFNSGYYEISFSVYAGVIFLLFEDYEELTLGEIYELTHIPIDDVKSLVMSMSTIPRCKILKKSSSSGNMKFSVNYFFSSPNRKVKVPVIACPLPSQKSDNLATASSVDTYDNEIVMELSAIIVRIMKTEGKLSHQQLLERTTKRTQSRLSLTPSILKRSIQLLIEKEYIQRNADDPSYYHYLS
Protein: Collagen type V alpha 2 chain (F1LQ00)
Organism: Rattus norvegicus (Rat)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
- Collagen alpha-1
- Collagen alpha-1
- Collagen alpha-1
- Collagen alpha-2
- Fibrillin-1
- Lumican
- Collagen alpha-1
- Alpha 4 type V collagen
- Serpin H1
- Procollagen C-endopeptidase enhancer 1
Sequence:
MMANWVVARPLLILFVLLGYCVSIKAQEQENDDYDEEIACTQHGQMYLNRDIWKPSPCQICVCDNGAILCDKIECQEVLNCANPVTPPGECCPACPQTSGGGDTSFGKTAQSWTKRRTRISSCCKYICVCMLYYGPPGSQGPRGDRGPKGRPGPRGPQGIDGEPGVPGQPGAPGPPGHPSHPGPDGMSRPFSAQMAGLDEKSGLGSQVGLMPGSVGPIGPRGPQGLQGQQGGVGPAGPPGEPGEPGPMGPIGARGPEGPPGKPGEDGEPGRNGNTGEVGFSGSPGARGFPGAPGLPGLKGHRGNKGLEGPKGEVGAPGAKGEAGPTGPMGAMGPLGPRGMPGERGRLGPQGAPGQRGAHGMPGKPGPMGPLGIPGSSGFPGNPGVKGEAGPTGARGPEGPQGQRGETGPPGPAGSHGLPGAVGTDGTPGAKGPTGSPGTSGPPGLAGPPGSPGPQGSTGPQGIRGQLGDPGVPGFKGEAGPKGEPGPHGIQGPIGPPGEEGKRGPRGDPGTVGPPGPMGERGAPGNRGFPGSDGLPGPKGAQGERGPIGSSGPKGGQGDPGRPGEPGLPGARGLTGNPGVQGPEGKLGPLGAPGEDGRPGPPGSIGIRGQPGSMGLPGPKGSSGDLGKPGEAGNAGVPGQRGAPGKDGEVGPSGPVGPPGLAGERGEQGPPGPTGFQGLPGPPGPPGEGGKPGDQGVPGEPGAVGPLGPRGERGNPGERGEPGITGLPGEKGMAGGHGPDGPKGNPGPTGTIGDTGPPGLQGMPGERGIAGTPGPKGDRGGVGEKGAEGTAGNDGARGLPGSLGPPGPAGPTGEKGEPGPRGLVGPPGSRGNPGSRGENGPTGAVGFAGPQGPDGQPGVKGEPGEPGQKGDAGSPGPQGLAGSPGPHGPHGVPGLKGGRGTQGPPGATGFPGSAGRVGPPGPAGAPGPAGPIGEPGKEGPPGLRGDPGSHGRVGDRGPAGPPGSPGDKGDPGEDGQPGPDGPPGPAGTTGQRGIVGMPGQRGERGMPGLPGPAGTPGKVGPTGATGDKGPPGPVGPPGSNGPVGEPGPEGPAGNDGTPGRDGAVGERGDRGDPGPAGLPGSQGAPGTPGPVGAPGDAGQRGEPGSRGPVGPPGRAGKRGLPGPQGPRGDKGDNGDRGDRGQKGHRGFTGLQGLPGPPGPNGEQGSAGIPGPFGPRGPPGPVGPSGKEGNPGLLGPIGPPGVRGSVGEAGPEGPPGEPGPPGPPGPPGHLTAALGDIMGHYDENMPDPLPEFTEDQAAPDDTNKTDPGVHATLKSLSSQIETMRSPDGSKKHPARTCDDLKLCHPTKQSGEYWIDPNQGSAEDAIKVYCNLETGETCISANPASVPRKTWWASKSPDNKPVWYGLDMNRGSQFTYGDYKSPNTAITQMTFLRLLSKEASQNLTYICKNTVGYMDDQTKNLKKAVVLKGSNDLEIKGEGNIRFRYTVLQDTCSKRNGNVGKTVFEYRTQNVARLPIIDIGPVDIGNADQEFGFEIGPVCFM
Protein: Putative RNA polymerase II subunit B1 CTD phosphatase rtr1 (EC 3.1.3.16) (RNA polymerase II-associated protein 2 homolog rtr1) (O42853)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Putative RNA polymerase II subunit B1 C-terminal domain (CTD) phosphatase involved in RNA polymerase II transcription regulation.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000305|PubMed:16823372}.
Interaction partners:
- RNA polymerase II subunit A C-terminal domain phosphatase
- DNA-directed RNA polymerase II subunit rpb7
- DNA-directed RNA polymerase II subunit rpb4
- RNA polymerase II subunit A C-terminal domain phosphatase ssu72
- GPN-loop GTPase 1
- DNA-directed RNA polymerases I, II, and III subunit RPABC1
- DNA-directed RNA polymerase II subunit rpb1
- DNA-directed RNA polymerase II subunit RPB2
- DNA-directed RNA polymerase II subunit RPB11
- DNA-directed RNA polymerase II subunit RPB3
Sequence:
MNKKSILKKPKNAQSTQEKQLITWSKSLIDEARSRLQYDFFALEWIEKLVDPVSLETLEEARKYLRKSDYDQVVKERKLVNLCGYPVCPYEPKQQTRYKLEDSGMKVYGGLNYYCSKDCFLKSCQYMVELSDEPLWIREDAREAMKQHLDPRQDEAFRKELENKKIEDVRLLLQALPVGYKAKVGEIVEHPLANEQS
Protein: Photosystem I reaction center subunit IV A, chloroplastic (PSI-E A) (Q9S831)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Stabilizes the interaction between PsaC and the PSI core, assists the docking of the ferredoxin to PSI and interacts with ferredoxin-NADP oxidoreductase.
Subcellular location: Plastid, chloroplast thylakoid membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.
Interaction partners:
- Photosystem I reaction center subunit V, chloroplastic
- Photosystem I reaction center subunit II-1, chloroplastic
- Photosystem I reaction center subunit III, chloroplastic
- Photosystem I chlorophyll a/b-binding protein 3-1, chloroplastic
- Photosystem I reaction center subunit VI-2, chloroplastic
- Photosystem I P700 chlorophyll a apoprotein A1
- Photosystem I reaction center subunit psaK, chloroplastic
- Photosystem I iron-sulfur center
- Photosystem I P700 chlorophyll a apoprotein A2
- Photosystem I reaction center subunit II-2, chloroplastic
Sequence:
MAMTTASTVFVLPANVTSVAGASSSRSSVSFLPMRNAGSRLVVRAAEDPAPASSSSKDSPAAAAAPDGATATKPKPPPIGPKRGSKVKILRRESYWFKNVGSVVAVDQDPKTRYPVVVRFAKVNYANISTNNYALDEVEEVAA
Protein: La protein homolog (La autoantigen homolog) (La ribonucleoprotein) (P40796)
Organism: Drosophila melanogaster (Fruit fly)
Function: May be involved in transcription termination by RNA polymerase III. Binds RNA and DNA. Binds to precursors of RNA polymerase III transcripts. May play a specialized role during fly development.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- CG6459 protein
- Zinc finger CCCH domain-containing protein 15 homolog
- Methionine aminopeptidase 2
- GH25737p
- Probable small nuclear ribonucleoprotein Sm D2
- T-complex protein 1 subunit theta
- Small nuclear ribonucleoprotein Sm D3
- Nucleolar protein 58
Sequence:
MAEVAETPSVEAQEEVAQPAEAQVLEAKNGDAKKDPAPAAEEAAGGFTKQERAIIRQVEYYFGDANLNRDKFLREQIGKNEDGWVPLSVLVTFKRLASLSTDLSEIVAALNKSEEGLVEISEDKLSLRRHPERPIPEHNEERRKEIQERTAYAKGFPLDSQISELLDFAANYDKVVNLTMRKHYDKPTKSYKFKGSIFLTFETKDQAKAFLEQEKIVYKERELLRKWQVDYLKEKQEEYAQKNEKRKNKKEAKPEPAFELPKNAIVVFEGAPETSSREEIREAFEKIKDFEVAYIEFAKGETKGSVRLTEADAAEKYIAKVEEGKLKFKDEVSLSLRKATEEEEKEFIDKAIEFMKKRRDFTRNKGKRFNRKRHGGNDHKHGGGKKARGD
Protein: CinA-like protein (P9WPE3)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- Probable nicotinate-nucleotide adenylyltransferase
- Nicotinate phosphoribosyltransferase pncB1
- Nicotinate-nucleotide pyrophosphorylase [carboxylating]
- Nicotinate phosphoribosyltransferase pncB2
- NAD-capped RNA hydrolase NudC
- Possible transcriptional regulatory protein NadR
- Glutamine-dependent NAD
- Probable phosphatidylglycerophosphate synthase
- Phosphatidylinositol phosphate synthase
- Putative cardiolipin synthase
Sequence:
MAVSARAGIVITGTEVLTGRVQDRNGPWIADRLLELGVELAHITICGDRPADIEAQLRFMAEQGVDLIVTSGGLGPTADDMTVEVVARYCGRELVLDDELENRIANILKKLMGRNPAIEPANFDSIRAANRKQAMIPAGSQVIDPVGTAPGLVVPGRPAVMVLPGPPRELQPIWSKAIQTAPVQDAIAGRTTYRQETIRIFGLPESSLADTLRDAEAAIPGFDLVEITTCLRRGEIEMVTRFEPNAAQVYTQLARLLRDRHGHQVYSEDGASVDELVAKLLTGRRIATAESCTAGLLAARLTDRPGSSKYVAGAVVAYSNEAKAQLLGVDPALIEAHGAVSEPVAQAMAAGALQGFGADTATAITGIAGPSGGTPEKPVGTVCFTVLLDDGRTTTRTVRLPGNRSDIRERSTTVAMHLLRRTLSGIPGSP