wanglab/gogpt-training-data huggingface dataset:
Protein: Conserved protein (O53836)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- ER-bound oxygenase mpaB/mpaB'/Rubber oxygenase catalytic domain-containing protein
- Putative acyl-[acyl-carrier-protein] desaturase DesA1
Sequence:
MQTGQNRGRWSGVPLESRHALRRDNLVAAGVQLLGGAGGPALTVRAVCRHAGLTERYFYESFADREHFVRAVYDDVCTRAMATLTSAQTPREAVEQFVELMVDDPVRGRVLLLAPAVEPALTRSGAEWMPNFIELLQRKLSRIVDPVLQKLVATSLIGALTGLFTAYLNGRLGATRKQFIDYCVNMLLSTAATYAPHRERGESEHSIPAGPHN
Protein: Smooth, isoform AC (A0A0B4KEV0)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MLESQPPLLGPGAAFPPFGAPEYHTTTPENWKGAAIHPTGLMKEPAGVVPGRNAPVAFTPQGQAQGAVMMVYGLDHDTSNTDKLFNLVCLYGNVARIKFLKTKEGTAMVQMGDAVAVERCVQHLNNIPVGTGGKIQIAFSKQNFLSEVINPFLLPDHSPSFKEYTGSKNNRFLSPAQASKNRIQPPSKILHFFNTPPGLTEDQLIGIFNIKDVPATSVRLFPLKTERSSSGLIEFSNISQAVLAIMKCNHLPIEGKGTKFPFIMKLCFSSSKSMNGAWNNAASEGMIEKENEVDTKVDIYN
Protein: Tumor necrosis factor-inducible gene 6 protein (EC 3.1.1.-) (Hyaluronate-binding protein) (TNF-stimulated gene 6 protein) (TSG-6) (Tumor necrosis factor alpha-induced protein 6) (TNF alpha-induced protein 6) (P98066)
Organism: Homo sapiens (Human)
Function: Major regulator of extracellular matrix organization during tissue remodeling. Catalyzes the transfer of a heavy chain (HC) from inter-alpha-inhibitor (I-alpha-I) complex to hyaluronan. Cleaves the ester bond between the C-terminus of the HC and GalNAc residue of the chondroitin sulfate chain in I-alpha-I complex followed by transesterification of the HC to hyaluronan. In the process, potentiates the antiprotease function of I-alpha-I complex through release of free bikunin. Acts as a catalyst in the formation of hyaluronan-HC oligomers and hyaluronan-rich matrix surrounding the cumulus cell-oocyte complex, a necessary step for oocyte fertilization. Assembles hyaluronan in pericellular matrices that serve as platforms for receptor clustering and signaling. Enables binding of hyaluronan deposited on the surface of macrophages to LYVE1 on lymphatic endothelium and facilitates macrophage extravasation. Alters hyaluronan binding to functionally latent CD44 on vascular endothelium, switching CD44 into an active state that supports leukocyte rolling. Modulates the interaction of chemokines with extracellular matrix components and proteoglycans on endothelial cell surface, likely preventing chemokine gradient formation. In a negative feedback mechanism, may limit excessive neutrophil recruitment at inflammatory sites by antagonizing the association of CXCL8 with glycosaminoglycans on vascular endothelium. Has a role in osteogenesis and bone remodeling. Inhibits BMP2-dependent differentiation of mesenchymal stem cell to osteoblasts. Protects against bone erosion during inflammation by inhibiting TNFSF11/RANKL-dependent osteoclast activation.
Subcellular location: Secreted {ECO:0000269|PubMed:1730767}.
Interaction partners:
- Pentraxin-related protein PTX3
- CD44 antigen
- Interleukin-8
- Thrombospondin-1
- Aggrecan core protein
- Fibronectin
- Versican core protein
- Hyaluronan synthase 2
- Fibroblast growth factor 2
- C-C motif chemokine 5
Sequence:
MIILIYLFLLLWEDTQGWGFKDGIFHNSIWLERAAGVYHREARSGKYKLTYAEAKAVCEFEGGHLATYKQLEAARKIGFHVCAAGWMAKGRVGYPIVKPGPNCGFGKTGIIDYGIRLNRSERWDAYCYNPHAKECGGVFTDPKQIFKSPGFPNEYEDNQICYWHIRLKYGQRIHLSFLDFDLEDDPGCLADYVEIYDSYDDVHGFVGRYCGDELPDDIISTGNVMTLKFLSDASVTAGGFQIKYVAMDPVSKSSQGKNTSTTSTGNKNFLAGRFSHL
Protein: Protein FAM171A1 (Astroprincin) (APCN) (Q5VUB5)
Organism: Homo sapiens (Human)
Function: Involved in the regulation of the cytoskeletal dynamics, plays a role in actin stress fiber formation.
Subcellular location: Cell membrane {ECO:0000269|PubMed:30312582}; Single-pass type I membrane protein {ECO:0000305|PubMed:30312582}.
Interaction partners:
Sequence:
MSRSATLLLCLLGCHVWKAVTKTLREPGAGAQEVTLKVHISDASTHQPVADALIEIFTNQASIASGTSGTDGVAFIKFQYKLGSQLIVTASKHAYVPNSAPWKPIRLPVFSSLSLGLLPERSATLMVYEDVVQIVSGFQGARPQPRVHFQRRALRLPENTSYSDLTAFLTAASSPSEVDSFPYLRGLDGNGTGNSTRHDLTPVTAVSVHLLSSNGTPVLVDGPIYVTVPLATQSSLRHNAYVAAWRFDQKLGTWLKSGLGLVHQEGSQLTWTYIAPQLGYWVAAMSPPIPGPVVTQDITTYHTVFLLAILGGMAFILLVLLCLLLYYCRRKCLKPRQHHRKLQLPAGLESSKRDQSTSMSHINLLFSRRASEFPGPLSVTSHGRPEAPGTKELMSGVHLEMMSPGGEGDLHTPMLKLSYSTSQEFSSREELLSCKEEDKSQISFDNLTPSGTLGKDYHKSVEVFPLKARKSMEREGYESSGNDDYRGSYNTVLSQPLFEKQDREGPASTGSKLTIQEHLYPAPSSPEKEQLLDRRPTECMMSRSVDHLERPTSFPRPGQLICCSSVDQVNDSVYRKVLPALVIPAHYMKLPGDHSYVSQPLVVPADQQLEIERLQAELSNPHAGIFPHPSSQIQPQPLSSQAISQQHLQDAGTREWSPQNASMSESLSIPASLNDAALAQMNSEVQLLTEKALMELGGGKPLPHPRAWFVSLDGRSNAHVRHSYIDLQRAGRNGSNDASLDSGVDMNEPKSARKGRGDALSLQQNYPPVQEHQQKEPRAPDSTAYTQLVYLDDVEQSGSECGTTVCTPEDSALRCLLEGSSRRSGGQLPSLQEETTRRTADAPSEPAASPHQRRSAHEEEEDDDDDDQGEDKKSPWQKREERPLMAFNIK
Protein: FIS1-related protein fis-1 (Mitochondrial fission 1 protein fis-1) (Q20291)
Organism: Caenorhabditis elegans
Function: Involved in the fragmentation of the mitochondrial network (By similarity). Involved in perinuclear clustering of the mitochondrial network (By similarity). Plays a role in removal of ultraviolet C radiation-induced mitochondrial DNA damage. May act, redundantly with fis-2, downstream of mitochondrial fission, before the fission products participate in either mitochondrial homeostasis, mitophagy, or apoptosis.
Subcellular location: Mitochondrion outer membrane {ECO:0000250|UniProtKB:Q9Y3D6}; Single-pass membrane protein {ECO:0000250|UniProtKB:Q9Y3D6}. Peroxisome membrane {ECO:0000250|UniProtKB:Q9Y3D6}; Single-pass membrane protein {ECO:0000250|UniProtKB:Q9Y3D6}.
Interaction partners:
- Dynamin-1-like protein drp-1
- Transmembrane GTPase fzo-1
- Dynamin
- Serine/threonine-protein kinase pink-1, mitochondrial
- Dynamin-like GTPase OPA1, mitochondrial
- Mitochondrial Rho GTPase 1
- Probable voltage-dependent anion-selective channel
- E3 ubiquitin-protein ligase parkin
- TBC1 domain family member 15
- Endoplasmic reticulum transmembrane protein
Sequence:
MEPESILDFHTEQEEILAARARSVSRENQISLAIVLVGSEDRREIKEGIEILEDVVSDTAHSEDSRVCVHYLALAHARLKNYDKSINLLNALLRTEPSNMQATELRRAVEKKMKREGLLGLGLLGGAVAVVGGLVIAGLAFRK
Protein: MIP18 family-like domain-containing protein (Q38DX6)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Probable cytosolic iron-sulfur protein assembly protein CIAO1 homolog
- MMS19 nucleotide excision repair protein
- MMS19 nucleotide excision repair protein
Sequence:
MTDRLTAEDVFYELSTIRDPERPDCTLADLDVVAMNRCRVEYIESSADFQSLRGQGCNDSGKPSVVVKVILQPTVPHCSLMEFICLCVYVRLREVFSLSNNAKFDITLVDGSHVRQRELEKQVADKERLAAAMEDKALLQEVERHINCE
Protein: GTP cyclohydrolase 1 feedback regulatory protein (GTP cyclohydrolase I feedback regulatory protein) (H0YNX7)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm, cytosol {ECO:0000256|ARBA:ARBA00004514}. Nucleus membrane {ECO:0000256|ARBA:ARBA00004126}.
Interaction partners:
Sequence:
MVGDEQSDPELMQHLGASKRRALGNNFYEYYVDDPPRIVLDKLERRGFRVLSMTGVGQTLVWCLHKE
Protein: Protein disulfide-isomerase EUG1 (PDI) (EC 5.3.4.1) (Endoplasmic reticulum protein EUG1) (P32474)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Probably interacts with nascent polypeptides in the endoplasmic reticulum. It is an essential gene only in the absence of PDI. Its native disulfide isomerase activity is very low.
Subcellular location: Endoplasmic reticulum lumen.
Interaction partners:
- Repressor ROX1
- Endoplasmic oxidoreductin-1
- Endoplasmic reticulum chaperone BiP
- Heat shock protein 70 homolog LHS1
- Protein disulfide isomerase MPD2
- Protein disulfide-isomerase
- ER-retained PMA1-suppressing protein 1
- Peptidyl-prolyl cis-trans isomerase FPR2
- Tryptophan synthase
- Tubulin beta chain
Sequence:
MQVTTRFISAIVSFCLFASFTLAENSARATPGSDLLVLTEKKFKSFIESHPLVLVEFFAPWCLHSQILRPHLEEAASILKEHNVPVVQIDCEANSMVCLQQTINTYPTLKIFKNGRIFDGQVYRGVKITDEITQYMIQLYEASVIYLNSEDEIQPYLENATLPVVINRGLTGLNETYQEVALDLAEDYVFLSLLDSEDKSLSIHLPNTTEPILFDGNVDSLVGNSVALTQWLKVVILPYFTDIEPDLFPKYISSNLPLAYFFYTSEEELEDYTDLFTQLGKENRGQINFIALNSTMFPHHVRFLNMREQFPLFAIHNMINNLKYGLPQLPEEEYAKLEKPQPLDRDMIVQLVKDYREGTAKPIVKSEEIPKEQKSNVYKIVGKTHDDIVHDDDKDVLVKYYATWCIHSKRFAPIYEEIANVLASDESVRDKILIAEVDSGANDILSFPVTGYPTIALYPAGNNSKPIIFNKIRNLEDVFEFIKESGTHHIDGQAIYDKLHQAKDSEVSTEDTVHDEL
Protein: Thioredoxin reductase (PfTrxR) (EC 1.8.1.9) (P61076)
Organism: Plasmodium falciparum (isolate 3D7)
Function: Catalyzes the transfer of electrons from NADPH to thioredoxins TRX1, TRX2 and TRX3, which in turn act as reductants of disulfide containing proteins. Able to reduce nitroglutathione (GSNO), a compound involved in the transport of nitric oxide (NO); however, TRX1 is more efficient in reducing GSNO. Has no catalytic activity towards oxidized glutathione (GSSG).
Subcellular location: [Isoform 1]: Mitochondrion {ECO:0000269|PubMed:21203490}.; SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm {ECO:0000269|PubMed:21203490}.
Interaction partners:
- Thioredoxin 1
- Selenide water dikinase, putative
- Thioredoxin reductase.
- 2-oxoglutarate dehydrogenase E1 component
- Bifunctional dihydrofolate reductase-thymidylate synthase
- Pyruvate dehydrogenase E1 component subunit beta
- 3-methyl-2-oxobutanoate dehydrogenase
- Thioredoxin-like protein 2
- PH domain-containing protein
- Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex
Sequence:
MNNVISFIGNSSNKYFQINQLHFIRIINKNIHSKNNLINSNSSYNVFYNKYFIKNTFQNKNKLSSIYSKLNFSIKNMCKDKNEKKNYEHVNANEKNGYLASEKNELTKNKVEEHTYDYDYVVIGGGPGGMASAKEAAAHGARVLLFDYVKPSSQGTKWGIGGTCVNVGCVPKKLMHYAGHMGSIFKLDSKAYGWKFDNLKHDWKKLVTTVQSHIRSLNFSYMTGLRSSKVKYINGLAKLKDKNTVSYYLKGDLSKEETVTGKYILIATGCRPHIPDDVEGAKELSITSDDIFSLKKDPGKTLVVGASYVALECSGFLNSLGYDVTVAVRSIVLRGFDQQCAVKVKLYMEEQGVMFKNGILPKKLTKMDDKILVEFSDKTSELYDTVLYAIGRKGDIDGLNLESLNMNVNKSNNKIIADHLSCTNIPSIFAVGDVAENVPELAPVAIKAGEILARRLFKDSDEIMDYSYIPTSIYTPIEYGACGYSEEKAYELYGKSNVEVFLQEFNNLEISAVHRQKHIRAQKDEYDLDVSSTCLAKLVCLKNEDNRVIGFHYVGPNAGEVTQGMALALRLKVKKKDFDNCIGIHPTDAESFMNLFVTISSGLSYAAKGGCGGGKCG
Protein: Cell shape-determining protein MreB (Actin-like MreB protein) (Rod shape-determining protein MreB) (P0A9X4)
Organism: Escherichia coli (strain K12)
Function: Forms membrane-associated dynamic filaments that are essential for cell shape determination. Acts by regulating cell wall synthesis and cell elongation, and thus cell shape. A feedback loop between cell geometry and MreB localization maintains elongated cell shape by targeting cell wall growth to regions of negative cell wall curvature. Filaments rotate around the cell circumference in concert with the cell wall synthesis enzymes. The process is driven by the cell wall synthesis machinery and does not depend on MreB polymerization. Rotation may contribute to the robust maintenance of rod shape.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:15612918}. Note=Membrane-associated (PubMed:15612918). Preferentially localizes to regions of negative curvature (PubMed:24550515). May associate with the membrane via MreC (PubMed:15612918). Localization depends on MreC, MreD and RodA (PubMed:15612918). {ECO:0000269|PubMed:15612918, ECO:0000269|PubMed:24550515}.
Interaction partners:
- Cytoskeleton protein RodZ
- Cell shape-determining protein MreC
- Cell division protein FtsZ
- Peptidoglycan D,D-transpeptidase MrdA
- Peptidoglycan glycosyltransferase MrdB
- Rod shape-determining protein MreD
- Probable peptidoglycan glycosyltransferase FtsW
- UDP-N-acetylglucosamine--N-acetylmuramyl-
- Peptidoglycan D,D-transpeptidase FtsI
- Cell division protein FtsA
Sequence:
MLKKFRGMFSNDLSIDLGTANTLIYVKGQGIVLNEPSVVAIRQDRAGSPKSVAAVGHDAKQMLGRTPGNIAAIRPMKDGVIADFFVTEKMLQHFIKQVHSNSFMRPSPRVLVCVPVGATQVERRAIRESAQGAGAREVFLIEEPMAAAIGAGLPVSEATGSMVVDIGGGTTEVAVISLNGVVYSSSVRIGGDRFDEAIINYVRRNYGSLIGEATAERIKHEIGSAYPGDEVREIEVRGRNLAEGVPRGFTLNSNEILEALQEPLTGIVSAVMVALEQCPPELASDISERGMVLTGGGALLRNLDRLLMEETGIPVVVAEDPLTCVARGGGKALEMIDMHGGDLFSEE
Protein: FCP1 homology domain-containing protein (Q389A7)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MKATKAKSGNTATNAVPFNNAPLKIVFLDCDGVVSPFGGPLFAPRQMKFLADIINGSGAQIVLSSSWRTTDFGRKEVARQLTQFGMPVFIDCTPTLPDKPRSVEILSWIDSNKRKYNIVNFVALDDINLPLSAPDRNFFARHAIVTNATTGLTEANVKQALQMLSDTNNI
Protein: Reverse transcriptase/RNaseH (Q72547)
Organism: Human immunodeficiency virus type 1 (HIV-1)
Interaction partners:
Sequence:
PISPIETVPVKLKPGMDGPKVKQWPLTEEKIKALVEICTEMEKEGKISKIGPENPYNTPVFAIKKKDSTKWRKLVDFRELNKRTQDFWEVQLGIPHPAGLKKRKSVTVLDVGDAYFSVPLDEDFRKYTAFTIPSINNETPGIRYQYNVLPQGWKGSPAIFQSSMTKILEPFRKQNPDIVIYQYMDDLYVGSDLEIGQHRTKIEELRQHLLRWGLTTPDKKHQKEPPFLWMGYELHPDKWTVQPIVLPEKDSWTVNDIQKLVGKLNWASQIYPGIRVRQLCKLLRGTKALTEVIPLTEEAELELAENREILKEPVHGVYYDPSKDLIAEIQKQGQGQWTYQIYQEPFKNLRTGKYARMRGAHTNDVKQLTEAVQKITTESIVIWGKTPKFKLPIQKETWETWWTEYWQATWIPEWEFVNTPPLVKLWYQLEKEPIVGAETFYVDGAANRETKLGKAGYVTNRGRQKVVTLTDTTNQKTELQAIYLALQDSGLEVNIVTDSQYALGIIQAQPDQSESELVNQIIEQLIKKEKVYLAWVPAHKGIGGNEQVDKLVSAGIRKVLFLDGID
Protein: Zinc finger protein 3 (Q86U76)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MLAAALLKAKSQELVTFEDVAVYFIRKEWKRLEPAQRDLYRDVMLENYGNVFSLDRETRTENDQEISEDTRSHGVLLGRFQKDISQGLKFKEAYEREVSLKRPLGNSPGERLNRKMPDFGQVTVEEKLTPRGERSEKYNDFGNSFTVNSNLISHQRLPVGDRPHKCDECSKSFNRTSDLIQHQRIHTGEKPYECNECGKAFSQSSHLIQHQRIHTGEKPYECSDCGKTFSCSSALILHRRIHTGEKPYECNECGKTFSWSSTLTHHQRIHTGEKPYACNECGKAFSRSSTLIHHQRIHTGEKPYECNECGKAFSQSSHLYQHQRIHTGEKPYECMECGGKFTYSSGLIQHQRIHTGENPYECSECGKAFRYSSALVRHQRIHTGEKPLNGIGMSKSSLRVTTELNIREST
Protein: Pre-mRNA-splicing factor 38 (Q7JVL3)
Organism: Drosophila melanogaster (Fruit fly)
Function: Required for pre-mRNA splicing.
Subcellular location: Nucleus {ECO:0000269|PubMed:18765666, ECO:0000269|PubMed:18981222, ECO:0000269|PubMed:24244416}.
Interaction partners:
- Microfibrillar-associated protein 1
- Pleiotropic regulator 1
- LD44732p
- Pre-mRNA-processing-splicing factor 8
- Ubiquitin-like protein 5
- Pre-mRNA-splicing factor 38
- Uncharacterized protein, isoform C
- Regulatory protein zeste
- LD21442p
- Splicing factor 3A subunit 3
Sequence:
MANRTVKEAKNVHGTNPQYLIEKIIRSRIYDSKYWKEQCFALTAELLVDKAMELRFVGGVYGGNIKPTQFLCLTLKMLQIQPEKDIVVEFIKNEEFKYVRALGAFYLRLTGAALDCYKYLEPLYIDNRKLRRQNRAGQFEIVYMDEYIDELLRNDRVCDIILPRIQKRSILEENNEIEPKVSVLDEDLDDELPSDEEKADETNRPKENSTAVRRPRRVRSKSRSRSRERERRSGQGNSARSRDYYDELEDYDRQRNRVRNRDTHNEDYDRRQNNGRHDRERERQDRDSIRERERDGDRDRRDRERERERDRGRHDQRERDSRGERDRRRY
Protein: Uncharacterized protein (Q386T4)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MYNNDSAAGGDALQETCVDAITNMARRLDPQALTKVTQSLQDMLEENRQQVANRRGRGGYQQHQHHQQPHHFGHRGNARPPHANRQWGSNNNSRNYYQSSNGYDNGKYQRGGRPHQHNDWNASSRRHQSRGGGRDYGNRDEERVSNTNRDHSNRDGDRSPVAGNRSPPRGHREGAGARSSGPHNSKVEEENERGATEKPCEGGNERPHHGRHWGGGRGAGRVRRGERRPNGHNDAKADGPS
Protein: palmitoyl-protein hydrolase (EC 3.1.2.22) (Q9I7R0)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MAAPVIVEATVKQTATLIFMHGLGDTGHGWSSALAAIRPPFMKVICPTAPTQPVSLNAGFRMPSWFDLKTLDIGGPEDEPGIQSARDSVHGMIQKEISAGIPANRIVLGGFSQGGALALYSALTYDQPLAGVVALSCWLPLHKQFPGAKVNSDDVPIFQAHGDYDPVVPYKFGQLSASLLKSFMKNVTFKTYSGLSHSSSDDEMDDVKDIISKWVN
Protein: Auxin-responsive protein IAA7 (Auxin resistant 2) (Indoleacetic acid-induced protein 7) (Q38825)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Aux/IAA proteins are short-lived transcriptional factors that function as repressors of early auxin response genes at low auxin concentrations. Repression is thought to result from the interaction with auxin response factors (ARFs), proteins that bind to the auxin-responsive promoter element (AuxRE). Formation of heterodimers with ARF proteins may alter their ability to modulate early auxin response genes expression.
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- Protein TRANSPORT INHIBITOR RESPONSE 1
- SKP1-like protein 1A
- Auxin response factor 7
- Auxin response factor 5
- Protein AUXIN SIGNALING F-BOX 2
- Auxin transporter protein 1
- NEDD8-activating enzyme E1 regulatory subunit AXR1
- Auxin response factor 19
- Cullin-1
- Protein TOPLESS
Sequence:
MIGQLMNLKATELCLGLPGGAEAVESPAKSAVGSKRGFSETVDLMLNLQSNKEGSVDLKNVSAVPKEKTTLKDPSKPPAKAQVVGWPPVRNYRKNMMTQQKTSSGAEEASSEKAGNFGGGAAGAGLVKVSMDGAPYLRKVDLKMYKSYQDLSDALAKMFSSFTMGNYGAQGMIDFMNESKLMNLLNSSEYVPSYEDKDGDWMLVGDVPWEMFVESCKRLRIMKGSEAVGLAPRAMEKYCKNRS
Protein: Protein SYC1 (Q08553)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the cleavage and polyadenylation factor (CPF) complex, which plays a key role in polyadenylation-dependent pre-mRNA 3'-end formation and cooperates with cleavage factors including the CFIA complex and NAB4/CFIB. Component of the APT complex, which may be involved in polyadenylation-independent transcript 3'-end formation, including snoRNAs and snRNAs.
Subcellular location: Nucleus {ECO:0000269|PubMed:12819204, ECO:0000269|PubMed:14562095}.
Interaction partners:
- RNA end formation protein 2
- Serine/threonine-protein phosphatase PP1-2
- Pre-tRNA-processing protein PTA1
- RNA polymerase II subunit A C-terminal domain phosphatase SSU72
- Protein PTI1
- COMPASS component SWD2
- mRNA 3'-end-processing protein YTH1
- Protein MPE1
- Protein CFT1
- Cleavage factor two protein 2
Sequence:
MDLPKDKSDRTHQRINLNNSGTDRTNDLYLHIVQTFGCIETTATENATKLLMLGDVEVEISASSVSIEWTQKSMISQTIADSIVIMIIGLCASDKNVLSESELKERNHNVWKIQELQNLFREQFGDSFSIDEGIGKKENVKNGSVTIGKSKATIDFSTMKLIDCNSNPLKGRVESILSIGQKLTTPLC
Protein: DCN1-like protein 3 (DCNL3) (DCUN1 domain-containing protein 3) (Defective in cullin neddylation protein 1-like protein 3) (Squamous cell carcinoma-related oncogene 3) (Q8IWE4)
Organism: Homo sapiens (Human)
Function: Contributes to the neddylation of all cullins by transferring NEDD8 from N-terminally acetylated NEDD8-conjugating E2s enzyme to different cullin C-terminal domain-RBX complexes and may play a role in the cell cycle progression by regulating the SCF ubiquitin E3 ligase complex, after UV damage. At the cell membrane, can promote and as well inhibit cullins neddylation.
Subcellular location: Cell membrane {ECO:0000269|PubMed:19617556, ECO:0000269|PubMed:25349211, ECO:0000269|PubMed:26906416}. Cytoplasm {ECO:0000269|PubMed:18823379, ECO:0000269|PubMed:26906416}. Nucleus {ECO:0000269|PubMed:18823379, ECO:0000269|PubMed:26906416}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:18823379}. Note=After UVC treatment, the protein enters to the nucleus gradually (PubMed:18823379). Cell membrane localization is essential for CUL3 neddylation (PubMed:19617556). {ECO:0000269|PubMed:18823379, ECO:0000269|PubMed:19617556}.
Interaction partners:
- NEDD8-conjugating enzyme UBE2F
- NEDD8-conjugating enzyme Ubc12
- Cullin-1
- Cullin-3
- E3 ubiquitin-protein ligase RBX1
- Cullin-associated NEDD8-dissociated protein 1
- Cullin-2
- Pumilio homolog 2
- NEDD8-activating enzyme E1 catalytic subunit
- Ubiquitin-like protein NEDD8
Sequence:
MGQCVTKCKNPSSTLGSKNGDREPSNKSHSRRGAGHREEQVPPCGKPGGDILVNGTKKAEAATEACQLPTSSGDAGRESKSNAEESSLQRLEELFRRYKDEREDAILEEGMERFCNDLCVDPTEFRVLLLAWKFQAATMCKFTRKEFFDGCKAISADSIDGICARFPSLLTEAKQEDKFKDLYRFTFQFGLDSEEGQRSLHREIAIALWKLVFTQNNPPVLDQWLNFLTENPSGIKGISRDTWNMFLNFTQVIGPDLSNYSEDEAWPSLFDTFVEWEMERRKREGEGRGALSSGPEGLCPEEQT
Protein: Lipid transfer protein EARLI 1 (Protein EARLY ARABIDOPSIS ALUMINUM INDUCED 1) (pEARLI1) (Q39176)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probable lipid transfer protein (LTP). May improve freezing survival. Seems to control the flowering process and lignin synthesis. Has an auxiliary role for germinability and early seedling development under low temperature and salt stress conditions, probably in an abscisic acid- (ABA) dependent manner. Confers resistance to Botrytis cinerea and exhibits anti-fungal activity, at least against S.cerevisiae, B.cinerea and Fusarium oxysporum, probably by increasing their membrane permeability.
Subcellular location: Secreted, cell wall {ECO:0000269|PubMed:17786468}.
Interaction partners:
- Uncharacterized protein AT4g12540
- S-adenosyl-L-methionine-dependent methyltransferases superfamily protein
- At5g15780
- Subtilisin-like protease SBT2.3
- ATPase family AAA domain-containing protein At1g05910
Sequence:
MASKNSASIALFFALNIIFFTLTAATDCGCNPSPKHKPVPSPKPKPVPSPKPKPVPSPSVPSPSVPSPNPRPVTPPRTPGSSGNCPIDALRLGVCANVLSSLLNIQLGQPSAQPCCSLIQGLVDLDAAICLCTALRANVLGINLNVPISLSVLLNVCNRKVPSGFQCA
Protein: Propanediol dehydratase-reactivating factor large subunit (DDR large subunit) (Propanediol utilization protein PduG) (O31043)
Organism: Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Function: Large subunit of the propanediol dehydratase-reactivating factor (DDR), which reactivates suicidally inhibited adenosylcobalamin-dependent propanediol dehydratase (diol dehydratase, DDH) found in the bacterial microcompartment (BMC) dedicated to 1,2-propanediol (1,2-PD) degradation. Reactivates inactivated DDH in the presence of ATP, Mg(2+) and free adenosylcobalamin (AdoCbl), by mediating the exchange of the tightly bound damaged cofactor AdoCbl for a free intact one. This subunit contains the adenosine nucleotide binding site.
Subcellular location: Bacterial microcompartment {ECO:0000269|PubMed:12923081}.
Interaction partners:
- Propanediol dehydratase-reactivating factor small subunit
- Propanediol dehydratase medium subunit
- Propanediol dehydratase large subunit
- Bacterial microcompartment shell protein PduB
- Propanediol dehydratase small subunit
- Corrinoid adenosyltransferase PduO
- Propanal dehydrogenase
- Phosphate propanoyltransferase
- Propanediol utilization protein PduV
- Bacterial microcompartment shell protein PduA
Sequence:
MRYIAGIDIGNSSTEVALARQDETGALTITHSALAETTGIKGTLRNVFGIQEALALVAKRAGINVRDISLIRINEATPVIGDVAMETITETIITESTMIGHNPKTPGGAGLGVGITITPEELLTRPADSSYILVVSSAFDFADIANVINASMRAGYQITGVILQRDDGVLVSNRLEKSLPIVDEVLYIDRIPLGMLAAIEVAVPGKVIETLSNPYGIATVFNLNADETKNIVPMARALIGNRSAVVVKTPSGDVKARAIPAGNLELQAQGRTVRVDVAAGAEAIMKAVDGCGKLDNVTGEAGTNIGGMLEHVRQTMAELTNKPSSEIFIQDLLAVDTSVPVSVTGGLAGEFSLEQAVGIASMVKSDRLQMAMIAREIEQKLNIDVQIGGAEAEAAILGALTTPGTTRPLAILDLGAGSTDASIINPKGEIIATHLAGAGDMVTMIIARELGLEDRYLAEEIKKYPLAKVESLFHLRHEDGSVQFFPTPLPPAVFARVCVVKPDELVPLPGDLALEKVRAIRRSAKERVFVTNALRALRQVSPTGNIRDIPFVVLVGGSSLDFEVPQLVTDALAHYRLVAGRGNIRGSEGPRNAVATGLILSWHKEFAHGQ
Protein: Iroquois homeobox 4a (Iroquois homeobox protein 4a) (Iroquois-class homeodomain protein IRX-4a) (Q6NZU4)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PROSITE-ProRule:PRU00108}.
Interaction partners:
- Nucleoside diphosphate kinase
Sequence:
MSYPQFGYPYSSAPQFLMTTNSLTSCCESSTRSIPDSSAQTPVYCPVYESRLLATARHELSSAAALGVYGSPYTGGQGYGNYVTYGADASAFYSLGTFDAKDGSASAHAGITPAAAYYPYDPTLGQYQYDRYGSMEGGTRRKNATRETTSTLKAWLQEHRKNPYPTKGEKIMLAIITKMTLTQVSTWFANARRRLKKENKMTWPPRNKGSDEKKYDDDEDGSPEEQIKSETNDDESKDREDKDLQLSDLEDFDPLESESPECELKHRFQISAHMETKDPQKLSIPGLLEEAKSCLKSPEDCELELRHSKACFQQQQQQSHPILDSKPRIWSLAQTATSLNPAEFPSCMLRCPASPSPAGGPDRQQDSPVTTLRNWVDGVFHDPLFRHSSLNQTNTTVSWTNKGSILETGALGRSVADSGKQEAGKDTMTFPKGVNKIFCS
Protein: Acetyltransferase, putative (Q4GYC9)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MTSAYRIRDAAPADAGIMVRMLMSLASETENVELDEGEVRRGVTTLFEQGSLGRLYVAEEVPKGDTNIKGPSDGNRSSPQIVGVMTVTYEWSDWRGKLFLWIQSVYIIPSKRKQGIFQKFYDHLIRIMAEDPKYCGLRLAVNSKNEKAIRAYKQVGMKREKYQLMGRMKSKY
Protein: AT-rich interactive domain protein (F4HS13)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- soluble epoxide hydrolase
Sequence:
MALTVSSGGGGARIRCNDLTDSSRNPFSTFRLVNFPNPSRTEQQEEGNEGFDGENPPSQIVINDEDGDRTVVNTRFRGDPKDAPKFAIKDLPGLEPDPFEGEKWDGLGFFVQYLWAFGILFALISGGLAAGTYNEGATDFKETPVYKEAIQSRDLLDEAESSNSEDVFESNPTEVAPTIFQVDLELVVFIML