wanglab/gogpt-training-data huggingface dataset:
Protein: Ajuba LIM protein (LIM domain-containing protein ajuba) (E7FFI0)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- Wilms tumor protein 1-interacting protein homolog
- Protein aurora borealis
Sequence:
MDRLGIKLKQKLKLSDSGSVKFSKKKNDLVNTNNNSNTNNANNGIVPQINAPANTSQFPLSTSVEACGQSAGRPGKVGSSQRIAPPNNTAVPVAEDCGPGIEHHPSTLAPLRRRSPQQRASCYLPDTLEGRGTCDQMRRGGEGDPQGAYSPNSRAALKQRRYSLELQQLVRRQQLLAQPPPLSSVPPPYPTHSSAARLSAVEPSFLHEMERHKRLSLQEALFYKRLSSGGEPWDSGRPASLSHPPQRTHDSSVGGFFFPSAPALSPCSSFSLQESVLASPRSSFASSTASGGGGGGGSPMGSRCSSNRTSGISLGYDNRHTPGPAQQLQLSSTQLSGTTLGQAHPAPGKTGAPPIEVWRDCLEGVSGDSRHSYPPALSTHTVTFHRAEPDWGPIDQRGSRGDGVGERARHSDLLGTRYQQELTRLLLRDAALEGEALLGGLTLKEQPVSATILPSSTSTPAPTAAPGKPPEEPAAGVDRQEYFGTCVKCGKGVYGADNACQALDSLYHTRCFTCVSCGRTLRNKDFYNVNGSVYCKEDYMFSGFQEAAEKCSVCGHLILEQILQALGNSYHPGCFRCTVCSKALDGVPFTVDYLNNVYCVSDYNRTFAPKCAACLQPILPAEGSEEILRVVSMNKDYHFECYHCEECGKQLSDEPGSQCFPLDAHLLCHSCHMSRVCVTHNLPPHNTH
Protein: Deubiquitinating protein VCPIP1 (EC 3.4.19.12) (Valosin-containing protein p97/p47 complex-interacting protein 1) (Valosin-containing protein p97/p47 complex-interacting protein p135) (VCP/p47 complex-interacting 135-kDa protein) (Q8CDG3)
Organism: Mus musculus (Mouse)
Function: Deubiquitinating enzyme involved in DNA repair and reassembly of the Golgi apparatus and the endoplasmic reticulum following mitosis (By similarity). Necessary for VCP-mediated reassembly of Golgi stacks after mitosis. Plays a role in VCP-mediated formation of transitional endoplasmic reticulum (tER). Mediates dissociation of the ternary complex containing STX5A, NSFL1C and VCP (By similarity). Also involved in DNA repair following phosphorylation by ATM or ATR: acts by catalyzing deubiquitination of SPRTN, thereby promoting SPRTN recruitment to chromatin and subsequent proteolytic cleavage of covalent DNA-protein cross-links (DPCs). Hydrolyzes 'Lys-11'- and 'Lys-48'-linked polyubiquitin chains (By similarity).
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q96JH7}. Cytoplasm {ECO:0000250|UniProtKB:Q96JH7}. Endoplasmic reticulum {ECO:0000250|UniProtKB:Q8CF97}. Golgi apparatus, Golgi stack {ECO:0000250|UniProtKB:Q8CF97}. Note=Associated with Golgi stacks and endoplasmic reticulum (By similarity). Displays cytoplasmic to nuclear translocation in response to DNA-protein cross-links (DPCs)-inducing agents (By similarity). {ECO:0000250|UniProtKB:Q8CF97, ECO:0000250|UniProtKB:Q96JH7}.
Interaction partners:
- Transitional endoplasmic reticulum ATPase
- Ubiquitin recognition factor in ER-associated degradation protein 1
- Nuclear protein localization protein 4 homolog
- UBX domain-containing protein 2B
- NSFL1 cofactor p47
- UBX domain-containing protein 7
- UBX domain-containing protein 2A
- Cyclin-dependent kinase 1
- Syntaxin-5
Sequence:
MSQPPPPPPLPPPPPPPEAPQTSSSLAAAASPGGLSKRRDRRILSGSCPDPKCQARLFFPASGSVSIECTECGQRHEQQQLLGVEEVTDPDVVLHNLLRNALLGVTGAPKKNTELVKVMGLSNYHCKLLSPILARYGMDKQTGRAKLLRDMNQGELFDCALLGDRAFLIEPEHVNTVGYGKDRSGSLLYLHDTLEDIKRANKSQECLIPVHVDGDGHCLVHAVSRALVGRELFWHALRENLKQHFQQHLARYQALFHDFIDAAEWEDIINECDPLFVPPEGVPLGLRNIHIFGLANVLHRPIILLDSLSGMRSSGDYSATFLPGLIPAEKCTGRDGHLNKPICIAWSSSGRNHYIPLVGIKGAALPKLPMNLLPKAWGVPQDLIKKYIKLEEDGGCVIGGDRSLQDKYLLRLVAAMEEVFMDKHGIHPSLVADVHQYFYRRTGVIGVQPEEVTAAAKKAVMDNRLHKCLLYGALSELHVPSEWLAPGGKLYNLAKSTHGQLRPDKNYSFPLNNLVCSYDPVKDVLLPDYGLSNLTACNWCHGSSVRRVRGDGSIVYLDGDRTNSRSTGGKCGCGFKHFWEGKEYDNLPEAFPITLEWGGRVVRETVYWFQYESDPSLNSNVYDVAMKLVTKHFPGEFGSEILVQKVVHTILHQTAKKNPDDYTPVNIDGAHAQRVGDVQGQELESQLPTKIILTGQKTKTLHKEELNMSKTERTIQQNITEQASVMQKRKTEKLKQEQKGQPRTVSPSTIRDGPSSAPATPTKAPYSPTTSKEKKIRITTNDGRQSMVTLKPSTTFFELQESIAREFNIPPYLQCIRYGFPPKELMPPQAGMEKEPVPLQHGDRITIEILKGRAEGGPSTAAHSAHTVKQEEIAVTGKLSSKELQEQADKEMYSLCLLATLMGEDVWSYAKGLPHMFQQGGVFYNIMKKTMGMADGKHCTFPHLPGKTFVYNASEDRLELCVDAAGHFPIGPDVEDLVKEAVSQVRAEATTRSRESSPSHGLLKLGSGGVVKKKSEQLHNVTAFQGKGHSLGTASSHPHIDPRARETLAVRKHNTGTDFSNSSIKTEPPVFTAASSNSELIRIAPGVVTMRDGRQIDPDVVEAQRKKLQEMVSSIQASMDKHLRDQSAEQAPSDLSQRKVEVVSSVRPVNLQTGLPEPFSLTGGTENLNTETTDSHVADVLGAAFATRSKAQKENSMEEPEEMDSQDAETTNTTEPMDHS
Protein: UPF0739 protein C1orf74 (Q96LT6)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MLLLDLMSSPSPQLLVAAAQQTLGMGKRRSPPQAICLHLAGEVLAVARGLKPAVLYDCNCAGASELQSYLEELKGLGFLTFGLHILEIGENSLIVSPEHVCQHLEQVLLGTIAFVDVSSCQRHPSVCSLDQLQDLKALVAEIITHLQGLQRDLSLAVSYSRLHSSDWNLCTVFGILLGYPVPYTFHLNQGDDNCLALTPLRVFTARISWLLGQPPILLYSFSVPESLFPGLRDILNTWEKDLRTRFRTQNDFADLSISSEIVTLPAVAL
Protein: Sorting nexin MVP1 (P40959)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Required for vacuolar protein sorting.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:7862158}. Endosome membrane {ECO:0000269|PubMed:24567361}; Peripheral membrane protein {ECO:0000269|PubMed:24567361}; Cytoplasmic side {ECO:0000269|PubMed:24567361}. Note=Localizes throughout the endosomal system binding to phosphatidylinositol 3-phosphate (PtdIns3P). Enriched on retromer SNX-BAR-decorated endosomes. {ECO:0000269|PubMed:24567361}.
Interaction partners:
- DNA mismatch repair protein MSH3
- Vacuolar protein sorting-associated protein 35
- Vacuolar protein sorting-associated protein 17
- Sorting nexin-3
- Vacuolar protein sorting-associated protein 5
- Vacuolar protein sorting-associated protein 29
- Uncharacterized protein YKR078W
- Vacuolar protein sorting-associated protein 1
- Carboxypeptidase Y-deficient protein 8
- Mannose 6-phosphate receptor-like protein 1
Sequence:
MDNYEGSDPWNTSSNAWTKDDDHVVSTTNSEPSLNGISGEFNTLNFSTPLDTNEEDTGFLPTNDVLEESIWDDSRNPLGATGMSQTPNIAANETVIDKNDARDQNIEESEADLLDWTNNVRKTYRPLDADIIIIEEIPEREGLLFKHANYLVKHLIALPSTSPSEERTVVRRYSDFLWLREILLKRYPFRMIPELPPKRIGSQNADQLFLKKRRIGLSRFINLVMKHPKLSNDDLVLTFLTVRTDLTSWRKQATYDTSNEFADKKISQEFMKMWKKEFAEQWNQAASCIDTSMELWYRITLLLERHEKRIMQMVHERNFFETLVDNFSEVTPKLYPVQQNDTILDINNNLSIIKKHLETTSSICKQETEEISGTLSPKFKIFTDILLSLRSLFERYKIMAANNVVELQRHVELNKEKLESMKGKPDVSGAEYDRIKKIIQKDRRSIIEQSNRAWLIRQCILEEFTIFQETQFLITRAFQDWAKLNSNHAGLKLNEWEKLVTSIMDMPISRE
Protein: Extracellular superoxide dismutase [Cu-Zn] (EC-SOD) (EC 1.15.1.1) (P34461)
Organism: Caenorhabditis elegans
Function: Protects cells against oxidative stress by converting superoxide radicals to hydrogen peroxide. Oxidative stress is involved in various biological dysfunctions and senescence.
Subcellular location: [Isoform 1]: Secreted, extracellular space {ECO:0000269|PubMed:9628580}.; SUBCELLULAR LOCATION: [Isoform 2]: Membrane {ECO:0000269|PubMed:9628580}; Peripheral membrane protein {ECO:0000305}.
Interaction partners:
- Superoxide dismutase 2, mitochondrial
- Superoxide dismutase 1, mitochondrial
- Superoxide dismutase
- Superoxide dismutase
- Catalase-2
- Glutathione-independent glyoxalase DJR-1.1
- Glutathione-independent glyoxalase DJR-1.2
- Glutathione peroxidase
- Thioredoxin domain-containing protein
- Glutathione peroxidase
Sequence:
MKTRVVLILALSVCIEAASEVIRARAYIFKAEAGKIPTELIGTIDFDQSGSFLKLNGSVSGLAAGKHGFHIHEKGDTGNGCLSAGGHYNPHKLSHGAPDDSNRHIGDLGNIESPASGDTLISVSDSLASLSGQYSIIGRSVVIHEKTDDLGRGTSDQSKTTGNAGSRLACGTIGTVEERILETTTASLPPVTQSQPIGSSSYYYSTFYLPIILYFLLSRIL
Protein: RIM-binding protein, isoform I (A0A0B4KG12)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MPYESMHHHQSAAAAVAAGTTPNGMLDALSLQLRDAEMRRTEIERAHQETLAQIRNLSGSARPDAEAVENLQSRARELEKKVALENVRCEELQIELTSALKAKQASRSACSGMGSVSSGGGATIPTSASSSTVTWAPTISHQDQGSEIDIIMAKIEQDNRVLAELEQPRTSASASMSALPPSSMLSTVNSEFRTISKSELEEELNRYKRAVLGGSGGGGGGVGGGGGGVSALSSGYSSLPQSLASTLPNGGASTSLSGTSLGSHSAAAAAAAHSVSAGSGGVVGGGGQGGLSSISALVPNSISGISSSLSSHAIQSMQYGTGQTSVEKLLSGTSGITGIPPLPVNIHTMKAMPTALSQRGTIQLYNLQSTTMPLLSLNSHNLPPAGSTSYSALGAGGGTSLTHPTMANLGLLDTGTLLGSTGLSGLGVGPSVGGITGATSLYGLSGGGGGAGGLGSSYGPPFLDVASSASYPFTAAALRQASKMKMLDEIDIPLTRYNRSSPCSPIPPNNWGLDEFTDGLSVSMMHNRGGLALGALDLDTRNHGLNGASEPQVDMLDIPGKGRCCVFIARFPYDPPDVHNEFLSMPCREAEGELSLCAGDYLLVWTSGEPQGGYLDAELLDGRRGLVPASFVQRLVGDDLLEFHQAVLSTLRDAEDGSMQCDTTSLPSLPPHNPLLTHTHEDLARLSETHTDLEHDQDDISDNAPKHLTLERQLNKSVLIGWSPPEPVGYNLIDSYHVYVDGVLKVTVKANERTRALIEGVDSTRPHRISVRSVTQNRQTSRDAACTMIIGRDTAHLGPSAVRASHITCSSAVISWLPANSNHQHVVCVNNVEVRTVKPGMYRHTITGLAPSTQYRVTVRAKHLRAVGQHAANVGQTGGAGRPGQEEAPGAYADFRTLTKGLPDPPQEIQLEAGPQDGTILVTWQPVNRPTSTGPVTGYAVYADGKKVTDINSPTGDHALIDIGKLGVFNPRAVTIRTKSRDSQSADSAPILIPNTVRNAVARRGPNQMGMGPQLPQGPHGMTVQQQMGGMPGQPGQQGQHMMGGQQDHGQYDPNQMQQQQQQQGQPGQPGHQPDAGSGLLGGLLGGLFSKPTQNQVNQNGYQPGQPGAQRGMVPIPGRPQGPQQQQQQPYGPQGPMGGPRFRGPVPGQLNMQGQQMQGQMQGQMQGQMQGQMSGQMPGQMPGQMPGQMPGQMAGQMAGQMPGQMPGQMPGQMSGQMPGQMMGPRGPLNQQQQQQQQMQQGQMMPGQQAGQQQAQPGQPGQPGQMPGAQKKPRYFVAMFDYDPSTMSPNPDGCDEELPFQEGDTIKVFGDKDADGFYWGELRGRRGYVPHNMVSEVEDTTASMTAGGQMPGQMPGQMGQGQGVGVGGTAQVMPGQGAPQQSMRNVSRDRWGDIYANMPVKRMIALYDYDPQELSPNVDAEQVELCFKTGEIILVYGDMDEDGFYMGELDGVRGLVPSNFLADAPDQYNNQMGPGGVAGRGGLSQRGRGQGPGARGPPPPPRDNMMPGMGGRGQPGKNARPASPTLLDNTGHPAPDHQTQGMIGRVGNVGLQQQQQQQQQQQQLQQQQQYGQQQTQMGQQQQQQQQMGQPGMMGQQMGQPMGQQMGQMGQMGQMGQQQMGQQQMGQQQQPPTTQAQTGGLFSGATSLLSGATSAATGGLFGSKQPPKTDPMQPQGGVQPAQQQANAFGAQQPGMGMQQQGGMQSGMQQGMQQGMQQGMQQGMQQGMQQGMQQGMQQGMQPGMQQQQQQPQQVPPQAQAPPPGPGAGLLGGLKGIAAAAPGGDVLSKGKDLFGKFGFGFGK
Protein: Myc box-dependent-interacting protein 1 (Amphiphysin II) (Amphiphysin-like protein) (Box-dependent myc-interacting protein 1) (Bridging integrator 1) (O00499)
Organism: Homo sapiens (Human)
Function: Is a key player in the control of plasma membrane curvature, membrane shaping and membrane remodeling. Required in muscle cells for the formation of T-tubules, tubular invaginations of the plasma membrane that function in depolarization-contraction coupling. Is a negative regulator of endocytosis (By similarity). Is also involved in the regulation of intracellular vesicles sorting, modulation of BACE1 trafficking and the control of amyloid-beta production. In neuronal circuits, endocytosis regulation may influence the internalization of PHF-tau aggregates (By similarity). May be involved in the regulation of MYC activity and the control cell proliferation. Has actin bundling activity and stabilizes actin filaments against depolymerization in vitro.
Subcellular location: [Isoform BIN1]: Nucleus {ECO:0000269|PubMed:8782822}. Cytoplasm {ECO:0000269|PubMed:9182667}. Endosome {ECO:0000250|UniProtKB:O08539}. Cell membrane, sarcolemma, T-tubule {ECO:0000250|UniProtKB:O08839}.; SUBCELLULAR LOCATION: [Isoform IIA]: Cytoplasm {ECO:0000269|PubMed:9182667}.
Interaction partners:
- Ras and Rab interactor 3
- Myc proto-oncogene protein
- Synaptojanin-1
- Dynamin-2
- Dynamin-1
- Amphiphysin
- Clusterin
- Microtubule-associated protein tau
- Bridging integrator 3
- Synaptojanin-2
Sequence:
MAEMGSKGVTAGKIASNVQKKLTRAQEKVLQKLGKADETKDEQFEQCVQNFNKQLTEGTRLQKDLRTYLASVKAMHEASKKLNECLQEVYEPDWPGRDEANKIAENNDLLWMDYHQKLVDQALLTMDTYLGQFPDIKSRIAKRGRKLVDYDSARHHYESLQTAKKKDEAKIAKPVSLLEKAAPQWCQGKLQAHLVAQTNLLRNQAEEELIKAQKVFEEMNVDLQEELPSLWNSRVGFYVNTFQSIAGLEENFHKEMSKLNQNLNDVLVGLEKQHGSNTFTVKAQPSDNAPAKGNKSPSPPDGSPAATPEIRVNHEPEPAGGATPGATLPKSPSQLRKGPPVPPPPKHTPSKEVKQEQILSLFEDTFVPEISVTTPSQFEAPGPFSEQASLLDLDFDPLPPVTSPVKAPTPSGQSIPWDLWEPTESPAGSLPSGEPSAAEGTFAVSWPSQTAEPGPAQPAEASEVAGGTQPAAGAQEPGETAASEAASSSLPAVVVETFPATVNGTVEGGSGAGRLDLPPGFMFKVQAQHDYTATDTDELQLKAGDVVLVIPFQNPEEQDEGWLMGVKESDWNQHKELEKCRGVFPENFTERVP
Protein: tRNA(Phe) (4-demethylwyosine(37)-C(7)) aminocarboxypropyltransferase (EC 2.5.1.114) (MjTYW2) (tRNA wyosine derivatives biosynthesis protein Taw2) (Q58952)
Organism: Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) (Methanococcus jannaschii)
Function: S-adenosyl-L-methionine-dependent transferase that acts as a component of the wyosine derivatives biosynthesis pathway. Catalyzes the transfer of the alpha-amino-alpha-carboxypropyl (acp) group from S-adenosyl-L-methionine to 4-demethylwyosine (imG-14), forming 7-aminocarboxypropyl-demethylwyosine (wybutosine-86) at position 37 of tRNA(Phe).
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01922}.
Interaction partners:
- tRNA
- S-adenosyl-L-methionine-dependent tRNA 4-demethylwyosine synthase
- Probable sulfurtransferase
- Uncharacterized protein MJ1556
- Aspartate--tRNA
Sequence:
MGIKYQKIGDVVIVKKELSEDEIREIVKRTKCKAILLYTTQITGEFRTPHVKILYGKETETIHKEYGCLFKLDVAKIMWSQGNIEERKRMAFISNENEVVVDMFAGIGYFTIPLAKYSKPKLVYAIEKNPTAYHYLCENIKLNKLNNVIPILADNRDVELKDVADRVIMGYVHKTHKFLDKTFEFLKDRGVIHYHETVAEKIMYERPIERLKFYAEKNGYKLIDYEVRKIKKYAPGVWHVVVDAKFERI
Protein: Bifunctional protein RIB2 [Includes: tRNA pseudouridine(32) synthase, cytoplasmic (EC 5.4.99.28) (tRNA pseudouridine synthase 8) (tRNA pseudouridylate synthase 8) (tRNA-uridine isomerase 8); Diaminohydroxyphosphoribosylaminopyrimidine deaminase (DRAP deaminase) (EC 3.5.4.26) (Riboflavin-specific deaminase)] (Q12362)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Responsible for synthesis of pseudouridine from uracil-32 in cytoplasmic transfer RNAs.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:15466869}.
Interaction partners:
- 2,5-diamino-6-ribosylamino-4
- tRNA-specific adenosine deaminase subunit TAD3
- Multisubstrate pseudouridine synthase 7
- 3,4-dihydroxy-2-butanone 4-phosphate synthase
- GTP cyclohydrolase-2
- Riboflavin synthase
- Cytidine deaminase
- tRNA-specific adenosine deaminase 1
- tRNA-specific adenosine deaminase subunit TAD2
- tRNA pseudouridine
Sequence:
MEDSNNEASDDFNNLLNKEIESAKEVKLRKFANRNNNRNENSSKVKDASGFRLRVIQTDGHKTKKTDPDYEVTIDGPLRKIEPYFFTYKTFCKERWRDRKLVDVFVSEFRDREPSYYSKTIAEGKVYLNDEPANLDTIIRDGDLITHKVHRHEPPVTSKPIDIVFEDEDILVIDKPSSIPVHPTGRYRFNTITKMLERQLGYSVHPCNRLDKPTSGLMFLAKTPLGADRMGDQMKAREVTKEYVARVKGEFPIGIVEVDKPVRSVNPKVALNAVCEMSDENAKHAKTVFQRVSYDGQTSIVKCKPLTGRTHQIRVHLQYLGFPIANDPIYSNPDIWGPDLGRGGLQNYDDIVLKLDAIGKTNPAESWIHPHSEGEYLLGRQCEECEAEMYTDPGTNDLDLWLHAFRYESLERNSDTQKPLWSYRTKYPEWALEPHRRYMEMAVKEAGKCGPTKTAFSVGAVLVHGTQVLATGYSRELPGNTHAEQCALIKYSQLHPNCPTIVPMGTVLYTTMEPCSFRLSGNEPCCDRILATQGAIGTVFVGVMEPDTFVKNNTSLNKLESHGVNYIQIPGYEEECTIIAFKGHDNSDDKA
Protein: Sperm axonemal maintenance protein CFAP97D1 (CFAP97 domain-containing protein 1) (Q9DAN9)
Organism: Mus musculus (Mouse)
Function: Required for male fertility through its role in axonemal doublet stabilization which is essential for sperm motility and fertilization.
Interaction partners:
Sequence:
MNNSLDYLAYPVIVSNHRQSTTFRKKLDFGHYILHKNRVQIVKPAVDTKPPMAHTHYILKLSKIQGEQKRIDKIEYENRQLCQKIANAYRGPAKVDCWNEYLSKSLNRESRNRELVRITMENQGILRRLSDRKPNYDRRSSEMDWQNSRRYIRNTTRYLLFQED
Protein: DNA-directed RNA polymerase (EC 2.7.7.6) (Plastid-encoded RNA polymerase subunit alpha) (Q2LIP3)
Organism: Oryza officinalis
Subcellular location: Plastid, chloroplast {ECO:0000256|ARBA:ARBA00004229}.
Interaction partners:
Sequence:
RVDSKRLYYGRFILSPLRKGQADTVGIALRRALLGETEGTCITHAKFGSVPHEYSTIAGIEESVQEILLNLKEIVLRSNLYGVRNASICVKGPRYITAQDIILPPSVEIVDTAQPIANLTEPTDFRIELRIKRDRGYHTEVRKNTQDGSYPIDAVSMPVRNVNYSIFSCGNGNAKYEILFLEIWTNGSLTPKEALYEASRNLIDLFLPFLHTEEEGTRFQENKNRFTSPLLSFQKRLTNLKKNKKRIPLNCIFIDQLELPSRTYNCLKRANIHTLLDLLSKTEEDLMRIDSFRMQDGKQIWDTLEKHLPMDLPKNKF
Protein: HTH-type transcriptional regulatory protein TyrR (Q9I133)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
- RNA polymerase sigma-54 factor
- aminomethyltransferase
- Glycine dehydrogenase
- Glycine dehydrogenase
- Glycine cleavage system H protein 1
Sequence:
MRIHVSFIDRVGITQEVLALLGGRNLNLDAVEMVPPNVYIDAPTLSPEVLEELRAALLGIRGVQAMTVVDILPGQRRRLQLDALLAAMADPVLAVDGKGLVLLANPAFSERCGRDPAGERLASLFDDETLEDALVEQGFRLPLREVTFMGQALLLDATPITEGPGEGERHLAGGLLTLYEPNRIGERLAALHHDHAEGFEMLLGDSQPIRTLKTRAQRVAALDAPLLIHGETGTGKELVARGCHALSARHNSPFLALNCAALPENLAESELFGYAPGAFTGAQRGGKPGLLELAHQGTVFLDEIGEMSPYLQAKLLRFLSDGSFRRVGGDREVRVDVRILSATHRNLEKMVAEGSFREDLFYRLNVLSLEVPPLRERGHDILLLARHFMQQACAQIQRPVCRLAPGTYPALLSNRWPGNVRQLQNVIFRAAAICESSLVDIGDLEIAGTAVARQNDGEVGSLEEAVEGFEKALLEKLYVSYPSTRQLAARLQTSHTAIAHRLRKYGIGPRA
Protein: Neurexin-3-beta (E9P875)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MVFLEHLRGGTPRGTTTVSPILCLMNWNDEQCRQQLKSYIPKFASNFDAPRHVPQPPSSPSYDYEGDEDEEKKEEKDHGIADRSMNDVSGETTGFFSPVLPTVANFPTTRQTEREFLNIWIRVL
Protein: Mdm2-binding protein (hMTBP) (Q96DY7)
Organism: Homo sapiens (Human)
Function: Inhibits cell migration in vitro and suppresses the invasive behavior of tumor cells (By similarity). May play a role in MDM2-dependent p53/TP53 homeostasis in unstressed cells. Inhibits autoubiquitination of MDM2, thereby enhancing MDM2 stability. This promotes MDM2-mediated ubiquitination of p53/TP53 and its subsequent degradation.
Interaction partners:
- Treslin
- E3 ubiquitin-protein ligase Mdm2
- DNA topoisomerase 2-binding protein 1
- ATP-dependent DNA helicase Q4
Sequence:
MDRYLLLVIWGEGKFPSAASREAEHGPEVSSGEGTENQPDFTAANVYHLLKRSISASINPEDSTFPACSVGGIPGSKKWFFAVQAIYGFYQFCSSDWQEIHFDTEKDKIEDVLQTNIEECLGAVECFEEEDSNSRESLSLADLYEEAAENLHQLSDKLPAPGRAMVDIILLLSDKDPPKLKDYLPTVGALKHLREWYSAKITIAGNHCEINCQKIAEYLSANVVSLEDLRNVIDSKELWRGKIQIWERKFGFEISFPEFCLKGVTLKNFSTSNLNTDFLAKKIIPSKDKNILPKVFHYYGPALEFVQMIKLSDLPSCYMSDIEFELGLTNSTKQNSVLLLEQISSLCSKVGALFVLPCTISNILIPPPNQLSSRKWKEYIAKKPKTISVPDVEVKGECSSYYLLLQGNGNRRCKATLIHSANQINGSFALNLIHGKMKTKTEEAKLSFPFDLLSLPHFSGEQIVQREKQLANVQVLALEECLKRRKLAKQPETVSVAELKSLLVLTRKHFLDYFDAVIPKMILRKMDKIKTFNILNDFSPVEPNSSSLMETNPLEWPERHVLQNLETFEKTKQKMRTGSLPHSSEQLLGHKEGPRDSITLLDAKELLKYFTSDGLPIGDLQPLPIQKGEKTFVLTPELSPGKLQVLPFEKASVCHYHGIEYCLDDRKALERDGGFSELQSRLIRYETQTTCTRESFPVPTVLSPLPSPVVSSDPGSVPDGEVLQNELRTEVSRLKRRSKDLNCLYPRKRLVKSESSESLLSQTTGNSNHYHHHVTSRKPQTERSLPVTCPLVPIPSCETPKLATKTSSGQKSMHESKTSRQIKESRSQKHTRILKEVVTETLKKHSITETHECFTACSQRLFEISKFYLKDLKTSRGLFEEMKKTANNNAVQVIDWVLEKTSKK
Protein: ATPase, putative (Q38AF7)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MRASLCTRNMWRAHVSDRRTVEEMYNCLVQKGVLREEPGQRLMVQACTKLANSIKVRESSSGKKGAEPPLAKGSGGKGTFANSGGYSGITSSYARLETCRALAQSLWHAGSHFLRRASPDTVTRDIKVHWPENLGVDKRTGLYLWGDVGIGKTLVMDLFELSEIPHVSKRRVHLHSFMCDLVKRLQKAETELRDHRLRPMDTVVNDILQESPILCLDEFQTIDVTHASLLAGFFSIALPRGLILFATSNRPPQDLTSISDSFARCVPLLWYYCDIVHCENIRDYRENASTGHHDAIFLHPNTIEAAAQLVRRVERGISGSRTWVKGATIWLYGRELVVPYHCGGIALFDFRDICGALGPPDFQCLAKTFHTVIITNIPQISRLNRNAAQQFVILVDELYQFNVKLLFTSEVPWGQLLRDGLGESPSVADSCYSEGEDERSGYAAYYGFRNEEELLSFNRIASRLKEMGCRHYLLRDHNHFVVLDYNFAALLE
Protein: RCC1-like G exchanging factor-like protein (RCC1-like protein) (Williams-Beuren syndrome chromosomal region 16 protein homolog) (Q9CYF5)
Organism: Mus musculus (Mouse)
Function: Guanine nucleotide exchange factor (GEF) for mitochondrial dynamin-related GTPase OPA1. Activates OPA1, by exchanging bound GDP for free GTP, and drives OPA1 and MFN1-dependent mitochondrial fusion. Plays an essential role in mitochondrial ribosome biogenesis. As a component of a functional protein-RNA module, consisting of RCC1L, NGRN, RPUSD3, RPUSD4, TRUB2, FASTKD2 and 16S mitochondrial ribosomal RNA (16S mt-rRNA), controls 16S mt-rRNA abundance and is required for intra-mitochondrial translation of core subunits of the oxidative phosphorylation system (By similarity).
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:28746876}.
Interaction partners:
- Neugrin
- Pseudouridylate synthase RPUSD4, mitochondrial
- Mitochondrial mRNA pseudouridine synthase Rpusd3
- Retinal rod rhodopsin-sensitive cGMP 3',5'-cyclic phosphodiesterase subunit delta
- FAST kinase domain-containing protein 2
- Pseudouridylate synthase TRUB2, mitochondrial
Sequence:
MLAAARALRGPRPRWPTPAREHWTPAGRSRSRREAAEAEADVPVFQYVGERAARADRVFVWGFSFSGALGVPSFVVPSSGPGPRAGLRPRRRIQPVPYRLELDHKISSAACGYGFTLLSSKTKDVTKVWGMGLNKDSQLGFHRSRKDKTRGYEYVLEPSPVPLPLDRPQETKVLQVSCGRAHSLVLTDREGVFSMGNNSHGQCGRKVVEDEVYSESHKVHRMQDFDGQVVQVVCGQDHSLFLTDKGEVYSCGWGADGQTGLGHYNITSTPSKLGGDLAGVTVVQVATYGDCCLALSADGGVFGWGNSEYLQLASVTDSTQVNVPRCLPFSGVGKVKQVACGGTGCAVLNAEGHVFVWGYGILGKGPKLLETAIPEMIPPTLFGLTEFNPEVQVSQIRCGLSHFAALTNKGELFVWGKNIRGCLGIGRLEDQYFPWRVTMPGEPVDVACGVDHMVTLAKSFI
Protein: Gremlin-2 (Cysteine knot superfamily 1, BMP antagonist 2) (Protein related to DAN and cerberus) (PRDC) (O88273)
Organism: Mus musculus (Mouse)
Function: Cytokine that inhibits the activity of BMP2 and BMP4 in a dose-dependent manner, and thereby modulates signaling by BMP family members. Contributes to the regulation of embryonic morphogenesis via BMP family members. Antagonizes BMP4-induced suppression of progesterone production in granulosa cells.
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
- Growth/differentiation factor 5
- Gremlin-1
- Bone morphogenetic protein 4
- Bone morphogenetic protein 2
- Bone morphogenetic protein 7
- Bone morphogenetic protein 5
- Bone morphogenetic protein 6
- Growth/differentiation factor 6
Sequence:
MFWKLSLTLLLVAVLVKVAETRKNRPAGAIPSPYKDGSSNNSERWHHQIKEVLASSQEALVVTERKYLKSDWCKTQPLRQTVSEEGCRSRTILNRFCYGQCNSFYIPRHVKKEEDSFQSCAFCKPQRVTSVIVELECPGLDPPFRIKKIQKVKHCRCMSVNLSDSDKQ
Protein: BBG-LP15 (Q15K29)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MELLSSNTGTTTTTTTATHHLHQATTTKQLLVQDYLSYASPPTYSRLPPDGHEFPPNFSEPLIMHSHPLKVTTELSYEIQKGGKDESSAPPLPKTGPPATVPRKVYRQDLVINVEPAPSLTRDYQRSLSGGTPRKPSDWRKDEKSEKSVRDKIAMFSSNNELDAIPPAPATAPI
Protein: Probable imidazolonepropionase (EC 3.5.2.7) (Amidohydrolase domain-containing protein 1) (Q96NU7)
Organism: Homo sapiens (Human)
Interaction partners:
- Formimidoyltransferase-cyclodeaminase
- Histidine ammonia-lyase
- Uracil phosphoribosyltransferase homolog
- Urocanate hydratase
- 5'-nucleotidase
- S-methyl-5'-thioadenosine phosphorylase
- Vitamin D 25-hydroxylase
- Purine nucleoside phosphorylase
- Protein transport protein Sec23A
Sequence:
MASGHSLLLENAQQVVLVCARGERFLARDALRSLAVLEGASLVVGKDGFIKAIGPADVIQRQFSGETFEEIIDCSGKCILPGLVDAHTHPVWAGERVHEFAMKLAGATYMEIHQAGGGIHFTVERTRQATEEELFRSLQQRLQCMMRAGTTLVECKSGYGLDLETELKMLRVIERARRELDIGISATYCGAHSVPKGKTATEAADDIINNHLPKLKELGRNGEIHVDNIDVFCEKGVFDLDSTRRILQRGKDIGLQINFHGDELHPMKAAELGAELGAQAISHLEEVSDEGIVAMATARCSAILLPTTAYMLRLKQPRARKMLDEGVIVALGSDFNPNAYCFSMPMVMHLACVNMRMSMPEALAAATINAAYALGKSHTHGSLEVGKQGDLIIINSSRWEHLIYQFGGHHELIEYVIAKGKLIYKT
Protein: D-threonine aldolase (EC 4.1.2.42) (O82872)
Organism: Arthrobacter sp
Function: Catalyzes the reversible cleavage of D-threonine or D-allothreonine into glycine and acetaldehyde. Can also cleave D-beta-phenylserine, D-beta-hydroxy-alpha-aminovaleric acid, D-beta-3,4-dihydroxyphenylserine and D-beta-3,4-methylenedioxyphenylserine into glycine and the corresponding aldehyde compounds. Inactive towards D-serine, beta-hydroxyaspartate and O-phospho-DL-threonine.
Interaction partners:
Sequence:
MSQEVIRGIALPPPAQPGDPLARVDTPSLVLDLAPFEANLRAMQAWADRHDVALRPHAKAHKCPEIALRQLALGARGICCQKVSEALPFVAAGIQDIHISNEVVGPAKLALLGQLARVAKISVCVDNAHNLSQVSQAMVQAGAQIDVLVEVDVGQGRCGVSDDALVLALAQQARDLPGVNFAGLQAYHGSVQHYRTREERAEVCRQAARIAASYAQLLRESGIACDTITGGGTGSAEFDAASGVYTELQAGSYAFMDGDYGANEWDGPLAFENSLFVLATVMSKPAPDRVILDAGLKSTTAECGPPAIFGEPGLTYTAINDEHGVVRVEPGAQAPDLGAVLRLVPSHVDPTFNLHDGLVVVRDGVVEDIWEISARGFSR
Protein: Golgin candidate 2 (AtGC2) (B0F9L7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Golgi matrix protein playing a role in tethering of vesicles to Golgi membranes and in maintaining the overall structure of the Golgi apparatus.
Subcellular location: Golgi apparatus membrane {ECO:0000269|PubMed:18182439}; Multi-pass membrane protein {ECO:0000269|PubMed:18182439}. Note=Probably located to cisternal rims of cis or medial Golgi.
Interaction partners:
- Golgin candidate 3
- Golgin candidate 4
- Golgin candidate 6
- Golgin candidate 5
Sequence:
MANWISSKLKAAETILQQLDQQAADSLRKDEKSETHDEVFETSPKSGSSPVSLKDQLRKKTYEGSDSGSGSQRNSTEQKPSYLSSSKKVRKPDQSHERTSAPSQSLTQDNTKLTDNDWTELLSTPNQRTSTSTSRSPGGTSAIRGLKKDGKRHGNLGKNPLVSDGKKSSSSNVVNSRGRPQKQTNKEPSDKEVSSPSDADMKNRNAPRDIFVNSTHKESEKDVSGKTPPLDDSRRSANETLPRETSPSVGKRDGRESRRSSVWGKQVREEVSQSNVSDGLTRKESSLSSDESESDYESDSSTDSERERQREERRRRRERVFAEKVATKAVAVIKERENMVARLEGEKLSLEKIVEERAKQQAQEAAELQTNMMETLEAADLEKQKHNNTRMEVLTRLAGLEAENAELTRSLAAGQKKLETQIDQVAVLKQQVELKESTLEELKRNTFNIGGRGTTLKQLDTSRGDKFEHQMLEAEISLLTDKIGRLQDKATKLEADIEMMRKELEEPTEVEIELKRRLNQLTDHLIQKQSQVEALSSEKATILFRIEAVSRLIEENKGMSATEASSQDLEAGDWELSGSKFKPAFQDKIRSGKKHLGWLVMQLNAIFISGTVFLRRNPTAKIWAVVYLVCLHLWVLYILLSHSDASSSGELRSGAVISLENFSNSSLQ