wanglab/gogpt-training-data huggingface dataset:
Protein: COL25A1 protein (Q8NE08)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MLLKKHAGKGGGREPRSEDPTPAEQHCARTMPPCAVLAALLSVVAVVSCLYLGVKTNDLQARIAALESAKGAPSIHLLPDTLDHLKTMVQEKVERLLAQKSYEHMAKIRIAREAPSECNCPAGPPGKRGKRGRRGESGPPGQPGPQGPPGPKGDKGEQGDQGPRGPLGPPGQKGSIGAPGIPGMNGQKGEPGLPGAVGQNGIPGPKGEPGEQGEKGDAGENGPKGDTGEKGDPGSSAAGIKGEPGESGRPGQKGEPGLPGLPGLPGIKGEPGFIGPQGEPGLPGLPGTKGERGEAGPPGRGERGEPGAPGPKGKQGESGTRGPKGSKGDRGEKGDSGAQGPRGPPGQKGDQGATEIIDYNGNLHEALQRITTLTVTGPPGPPGPQGLQGTKGEQGSPGIPGMDGEQGLKGSKGDMGDPGSQWNERRKRRFWNAGSTGSFYHRPTRPTRSPWPTWPHGTSWTSWTKGSIWLRRKARIPGYRWSYGTPWPCRSQRRKR
Protein: Uncharacterized protein (Q38AN6)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MFFVFPFPTSPRQRVERVMRVLYQLGAAIFVISYVVLLTEADVRLQAGMHGSFSAPGANLSDSLEMVMSNCEYEGIMPIYGVGVVVGVNAKSLPFAIISMLQHMRAVLVVQFLAALNGVAGGYCYSTNIRHMHLFGLHVPVHLILNVLAYVLTVTIIALVAVSGPVRSYYSASLEFCAAKLAEEDNEKLLESGFDGFHLFGTRLEWAMGAAIVNLIIYTIGLVTRVYKSHDPAIALFSMSDVPWEKTGIRLSVDKAALSIHTAARERIISEARDAIGRGERVRIVRSYALMTEADYNEQVEEMRRLFATRAQEEQFKNMHSLLEDEPHAGGSAMHWGSSGLQKAEPLRPDGTPVVQGVGDTVPPFGSGMMGRGADNLADVFNVDNLSDLSLNRAGLAPGAVGGFDASVGDNQAATVQQWQRPGSIGYPDVFGGERQNESTAFGDGGTAFTPDALQGNDDFSHAFTNISDTRRVVSRRRTATGAVAGTRANGSHEPHNLSGEELWDVSNFGDDNALSPRIDSPDAL
Protein: Ribosomal protein S19 (Ribosomal protein small subunit 19) (Q2F968)
Organism: Oryza sativa subsp. indica (Rice)
Interaction partners:
Sequence:
MPRRSIWKGSFVDAFLFRIKKNRESLMSRKIWSRRSSISPEFVDCSVLIYNGKTPVRCKITEGKVGHKFGEFAFTRRRRPYQTNRGKGRKGKK
Protein: DAB adaptor protein 2 (Disabled homolog 2 isoform X2) (Disabled homolog 2 isoform b) (F6NGQ6)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
- Growth factor receptor-bound protein 2
- F-BAR domain only protein 1
Sequence:
MSQSPEAETVTVVPAEPASTTESASVTITTAPVTRTSFWKERRKIPEKTDEFLLARFQGDGVRYKAKLIGVDDVQDARGDKMCQDSMMKLKGMAIAARSQGKHKQRIWINISLTGIKIVDEKTGVIEHEHVVNKISFIARDVTDNRAFGYVCGAEGQHQFFAIKTAQQAEPLVIDLKDLFQLIFNMKKKEQEAGQKGEGNGTENGGDALLAVDGNENPVKSVEQMNLFGDMSTPPDIHSPTSPGNDLFGSGLFAPPAQNESQASNQNASIPADLFNSTPSSTINAFGSMSLGHAPGTAPVSWGQTPTMFPPQAGVQVTIPGPPRPFPQPSAFGGLSAPAWGQQGASPFGPPAGTQAWGQPGAAAPVGTWPAPGPVASPFQPNQFAPMMPPNAMMGMQQGAVAPPRPPPRPPVKEEPPVVKSAFTALDPLGEKESKSGKDMFKNFQMVKPQKPEPGPDPNTNGSFDQYFSNKVGLAQDAADHDDFEINQISANSNGTSKPASQLIPTMDAIPQAAGLIPAPATGLLDVAFSSNPVPAPTNPAPAAGTDLFDDTFGVNPFGAPLMNTSTPATQNAALADAFGDPFGGNPFA
Protein: Vacuolar protein sorting-associated protein 41 homolog (D3ZVH6)
Organism: Rattus norvegicus (Rat)
Subcellular location: Endosome membrane {ECO:0000256|PIRNR:PIRNR028921}; Peripheral membrane protein {ECO:0000256|PIRNR:PIRNR028921}. Late endosome membrane {ECO:0000256|PIRNR:PIRNR028921}; Peripheral membrane protein {ECO:0000256|PIRNR:PIRNR028921}. Early endosome membrane {ECO:0000256|PIRNR:PIRNR028921}; Peripheral membrane protein {ECO:0000256|PIRNR:PIRNR028921}. Lysosome membrane {ECO:0000256|PIRNR:PIRNR028921}; Peripheral membrane protein {ECO:0000256|PIRNR:PIRNR028921}. Golgi apparatus, trans-Golgi network {ECO:0000256|PIRNR:PIRNR028921}. Cytoplasmic vesicle, clathrin-coated vesicle {ECO:0000256|PIRNR:PIRNR028921}.
Interaction partners:
- Vacuolar protein sorting-associated protein 11 homolog
- Vacuolar protein sorting-associated protein 16 homolog
- Vacuolar protein sorting-associated protein 18 homolog
- VPS39 subunit of HOPS complex
- Transforming growth factor, beta receptor associated protein 1
- Vacuolar protein sorting-associated protein 33A
- Syntaxin-17
- Vesicle-associated membrane protein 8
- CCZ1 homolog, vacuolar protein trafficking and biogenesis associated
- Vesicle transport through interaction with t-SNAREs homolog 1A
Sequence:
MAEAEEQETESLEESTDESEEESEEEPKLKYERLSNGVTEILQKDAASCMTVHDKFLALGTHYGKVYLLDVQGNITQKFDVSPVKINQISLDESGEHMGVCSEDGKLQVFGLYSGEEFHETFDCPIKVSIYTCVFLYPQLLLFERTWMNRWKSSVLHEGEGNIRSVKWRGHLIAWANNMGVKIFDITSKQRITNVPRDDISLRPDMYPCSLCWKDAVTLIIGWGTSIKICSVKERHASEMRDLPSRYVEIVSQFETEFYISGLAPLCDQLVVLSYVKEVSEKTEREYCARPRLDIIQPLPETCEEISSDALTVRGFQENECRDYHLEYSEGESLFYVVSPRDVVVAKERDQDDHIDWLLEKKKYEEALMAAEISHRNIKRHKILEIGLAYVNHLVERGEYDMAARKCQKILGKNASLWEYEVYKFKEIGQLKAISPYLPRGDPVLKPLIYEMILHEFLESDYEGFATLIREWPGDLYNNSVIVQAVRDHLKKDSQNKTLLKTLAELYTYDKNYGNALEIYLTLRHKDVFQLIHKHNLFSSIKDKIVLLMDFDSEVMFFLLLCINCSNIKKVVEELEDRPELQHVYLHKLFKRDHHKGQRYHEKQISLYAEYDRPNLLPFLRDSTHCPLEKALEICQQRNFVEETVYLLSRMGNSRSALKMIMEELHDVDKAIEFAKEQDDGELWEDLILYSIDKPPFITGLLNNIGTHVDPILLIHRIKEGMEIPNLRDSLVKILQDYNLQVSILTQMSCKKNMMM
Protein: Ras-related protein Rap-2a (EC 3.6.5.2) (RbBP-30) (P10114)
Organism: Homo sapiens (Human)
Function: Small GTP-binding protein which cycles between a GDP-bound inactive and a GTP-bound active form. In its active form interacts with and regulates several effectors including MAP4K4, MINK1 and TNIK. Part of a signaling complex composed of NEDD4, RAP2A and TNIK which regulates neuronal dendrite extension and arborization during development. More generally, it is part of several signaling cascades and may regulate cytoskeletal rearrangements, cell migration, cell adhesion and cell spreading.
Subcellular location: Recycling endosome membrane; Lipid-anchor; Cytoplasmic side. Midbody. Note=May also localize to the Golgi (PubMed:7962206) and the gelatinase-containing granules of neutrophils (PubMed:8391995). Colocalizes with RASGEF1B to midbody at telophase (PubMed:23894443). {ECO:0000269|PubMed:23894443, ECO:0000269|PubMed:7962206, ECO:0000269|PubMed:8391995}.
Interaction partners:
- TRAF2 and NCK-interacting protein kinase
- Rho GTPase-activating protein 29
- Rap guanine nucleotide exchange factor 4
- Rap guanine nucleotide exchange factor 6
- RUN domain-containing protein 3A
- Rap guanine nucleotide exchange factor 3
- Rap guanine nucleotide exchange factor 2
- Apolipoprotein A-V
- Ral guanine nucleotide dissociation stimulator
- Alpha-2-macroglobulin receptor-associated protein
Sequence:
MREYKVVVLGSGGVGKSALTVQFVTGTFIEKYDPTIEDFYRKEIEVDSSPSVLEILDTAGTEQFASMRDLYIKNGQGFILVYSLVNQQSFQDIKPMRDQIIRVKRYEKVPVILVGNKVDLESEREVSSSEGRALAEEWGCPFMETSAKSKTMVDELFAEIVRQMNYAAQPDKDDPCCSACNIQ
Protein: Peptidyl-prolyl cis-trans isomerase FKBP17-1, chloroplastic (PPIase FKBP17-1) (EC 5.2.1.8) (FK506-binding protein 17-1) (AtFKBP17-1) (Immunophilin FKBP17-1) (Rotamase) (O81864)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides (By similarity).
Subcellular location: Plastid, chloroplast thylakoid lumen {ECO:0000250}.
Interaction partners:
- Peptidyl-prolyl cis-trans isomerase FKBP17-3, chloroplastic
- Peptidyl-prolyl cis-trans isomerase CYP28, chloroplastic
- PsbP domain-containing protein 7, chloroplastic
- Peptidyl-prolyl cis-trans isomerase CYP26-2, chloroplastic
- Thylakoid lumenal protein TL20.3
- PsbP domain-containing protein 6, chloroplastic
- PsbQ-like protein 3
- Thylakoid lumenal 19 kDa protein, chloroplastic
- Photosynthetic NDH subunit of lumenal location 2, chloroplastic
- Photosynthetic NDH subunit of lumenal location 5, chloroplastic
Sequence:
MIRCFAWTPLVGAPLITTVHFTSPPSLRIFASRSSAPSSSSSSSSTVAAASRRSISLSIIAVTSSVVSSFCFSSPALADFSEIPNSGGVKALDLRIGDGDVPIEGDQIEIHYYGRLAAKQGWRFDSTYDHKDSNGEAVPFTFVLGSSKVIPGIETAVRSMKVGGIRRVVIPPSQGYQNTSQEPLPPNFFDRQRLFTTIFNPTRLANGEGSTLGTLVFDIELVSTRRLHR
Protein: Cytochrome c oxidase subunit 7B, mitochondrial (Cytochrome c oxidase polypeptide VIIb) (IHQ) (P13183)
Organism: Bos taurus (Bovine)
Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix. Plays a role in proper central nervous system (CNS) development in vertebrates (By similarity).
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:27605664, ECO:0000269|PubMed:31533957}; Single-pass membrane protein {ECO:0000269|PubMed:27605664, ECO:0000269|PubMed:31533957}.
Interaction partners:
- Cytochrome c oxidase subunit 6C
- Cytochrome c oxidase subunit 5B, mitochondrial
- Cytochrome c oxidase subunit 7C, mitochondrial
- Cytochrome c oxidase subunit 2
- Cytochrome c oxidase subunit 6B1
- Cytochrome c oxidase subunit 4 isoform 1, mitochondrial
- Cytochrome c oxidase subunit 6A2, mitochondrial
- Cytochrome c oxidase subunit 5A, mitochondrial
- Cytochrome c oxidase subunit 1
- Cytochrome c oxidase subunit 7A1, mitochondrial
Sequence:
MFPLAKNALSRLRVQSIQQAVARQIHQKRAPDFHDKYGNAVLASGATFCVAVWVYMATQIGIEWNPSPVGRVTPKEWREQ
Protein: Cytochrome b5 type B (Cytochrome b5 outer mitochondrial membrane isoform) (O43169)
Organism: Homo sapiens (Human)
Function: Cytochrome b5 is a membrane-bound hemoprotein functioning as an electron carrier for several membrane-bound oxygenases.
Subcellular location: Mitochondrion outer membrane {ECO:0000250|UniProtKB:P04166}.
Interaction partners:
- NADH-cytochrome b5 reductase 3
- NADPH--cytochrome P450 reductase
- Cytochrome c
- NADH-cytochrome b5 reductase 1
- NADH-cytochrome b5 reductase-like
- NADH-cytochrome b5 reductase 2
- Myoglobin
- Stearoyl-CoA desaturase
- Steroid 17-alpha-hydroxylase/17,20 lyase
- Cytochrome b5 reductase 4
Sequence:
MSGSMATAEASGSDGKGQEVETSVTYYRLEEVAKRNSLKELWLVIHGRVYDVTRFLNEHPGGEEVLLEQAGVDASESFEDVGHSSDAREMLKQYYIGDIHPSDLKPESGSKDPSKNDTCKSCWAYWILPIIGAVLLGFLYRYYTSESKSS
Protein: Humanin-like protein (HNr) (Rattin) (C0HLU6)
Organism: Rattus norvegicus (Rat)
Function: Plays a role as a neuroprotective factor. Protects against neuronal cell death induced by amyloid-beta peptides. Also protects against excitotoxic cell death. Prevents amyloid-beta peptide-induced spatial learning and memory impairments, protects against amyloid-beta peptide-induced suppression of hippocampal long-term potentiation, and inhibits amyloid-beta peptide-induced activation of STAT3 and inhibition of CASP3. Prevents glutamate-induced dendritic atrophy in hippocampal neurons and also prevents glutamate-induced decrease in SYP puncta number and total puncta area. Protects anterior pituitary cells from TNF-induced apoptosis. Plays a role in ovarian follicle development by acting as a cryoprotective factor for granulosa cells in the antral follicle. Increases androgen production in Leydig cells and promotes Leydig cell survival by preventing apoptosis.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:26116236}. Secreted {ECO:0000269|PubMed:16619233, ECO:0000269|PubMed:31214013}. Cytoplasm {ECO:0000269|PubMed:25360890}. Note=Detected in the cytoplasm of anterior pituitary cells. {ECO:0000269|PubMed:25360890}.
Interaction partners:
Sequence:
MAKRGFNCLLLSISEIDLPVKRLESPNKTRRPYGASIY
Protein: FhuG protein (Q8Y5U8)
Organism: Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
- FhuC protein
- FhuB protein
- Lmo2182 protein
- Lmo2429 protein
- Lmo1959 protein
- Lmo0541 protein
- Lmo2431 protein
- Lmo1073 protein
- High-affinity heme uptake system protein IsdE
Sequence:
MYMTIAEKRKKSRRIWTLIILSVLIFCTFTYSVNAGYSKLPFLEVIKSFFGMADAGTQLIVTEFRLPRIVIALLVGAGLAVSGTILQGISGNGLADPGILGINNGAGLAVMLYISFFPSTMDVPVLFMPFIGFIGAILTAFVVYGLSYSRSEGLLPNRLLLTGIAVAAAIAALITLLTVRLDPQNYQRYAEWMAGNIWASSWQYVFALLPWLIVLGAIAFMKVKTLDVLSFGDQVATGLGVRVEREKFVLLIVAVGLAAACVSVSGGIAFIGLIGPHIARKLVGSAHRWVMVTAALSGGLLLLLADTIGRLIIQPSEIFAGIVVAIIGAPYFLFLLAKAK
Protein: Class II, major histocompatibility complex, transactivator (A0A0G2K9Q5)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MRCQVPGPSGSYLQGHTLCATMELGSPEGSYLELLNSDADPLHLYHLYDQMDLAGEEEIELNSETDMDTINCDQFSKLLQDMEMDEETREAYANIAELDQYVFQDTQLEGLSKDLFIQHIGPEEGFGENVEGPAESGEKPQKRRFPEEHAMDSKHRKLVPPSRTSLNYLDLPAGHIQIFTTLPQGLWQISGVGTGLSSVLVYHGEMPQVNQLLSSSSPTVPSLPESPDRPGSTSPFAPSTADLPGMPEPALTSRVNETEDTTPPSPCQEDPEPSIKLPKWPESVERFQHSLQDKYQALPGSPSGPLVAMELVRARLERGSNKSQERELATPDWTERQLAHGGLAEVLRVVGDSRRSRETQVVAVLGKAGQGKSHWARTVSHIWAQGQLPQYDFVFYVPCQCLDRPGDTYHLRDLLCPPNLQPLAMDDEVIDHIVRQPDRVLLILDAFEELEAQDSLLHGPCGPLSPEPCSLRGLLAGLFQRKLLRGCTLLLTARPRGRLAQSLSKADAIFEVPSFSTKQAQIYMRHYFENSGTAGSHDKALGLLEGQPFLLTHSHSPVLCSAVCQLSKALLDQGAEAQLPCTLTGLYVGLLGPAAQNSPPGALVELAKLAWELGRRHQSTLQETQFPSVEVKTWAVAQGLMQQTTEAQLAFSSFLLQCFLGAVWLAQCNEMKDKELPQYLALTPRKKRPYDNWLEGVPRFLAGLVFQPRAHCLGALVEPAMAAVADRKRKVLTRYLKRLKLGTLRAGRLLELLHCAHETQEPGIWKHVSHQLPGHLSFLGTRLTAPDVYVLGRALETASQDFSLDLRQTGIEPSRLGDLVGLSCVTSFRASLSDTMALWESLQHQGETQLLQAAEEKFTIEPFKAKSPKDVEDLDSLVQTQRLRNPSADAAKDLPAIRDLKKLEFALGPVLGPQAFPTLAKILPAFSSLQHLDLDSLSENKIGDKGVSKLSATFPQLKALETLNLSQNSITDVGACKLAEALPALAKSLLRLSLYNNCICDEGAKSLARVLPDMVSLRVMDVQFNKFTAVGAQQLTSSLQKCPQVETLAMWTPTIPFGVQEHLQQLDARISLR
Protein: Deoxyuridine 5'-triphosphate nucleotidohydrolase (dUTPase) (EC 3.6.1.23) (Q9CQ43)
Organism: Mus musculus (Mouse)
Function: Catalyzes the cleavage of 2'-deoxyuridine 5'-triphosphate (dUTP) into 2'-deoxyuridine 5'-monophosphate (dUMP) and inorganic pyrophosphate and through its action efficiently prevents uracil misincorporation into DNA and at the same time provides dUMP, the substrate for de novo thymidylate biosynthesis (By similarity). Inhibits peroxisome proliferator-activated receptor (PPAR) activity by binding of its N-terminal to PPAR, preventing the latter's dimerization with retinoid X receptor (By similarity). Essential for embryonic development.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:P33316}.
Interaction partners:
Sequence:
MPCSEDAAAVSASKRARAEDGASLRFVRLSEHATAPTRGSARAAGYDLFSAYDYTISPMEKAIVKTDIQIAVPSGCYGRVAPRSGLAVKHFIDVGAGVIDEDYRGNVGVVLFNFGKEKFEVKKGDRIAQLICERISYPDLEEVQTLDDTERGSGGFGSTGKN
Protein: Taste receptor type 2 member 41 (T2R41) (T2R12) (T2R26) (P59532)
Organism: Mus musculus (Mouse)
Function: Receptor that may play a role in the perception of bitterness and is gustducin-linked. May play a role in sensing the chemical composition of the gastrointestinal content. The activity of this receptor may stimulate alpha gustducin, mediate PLC-beta-2 activation and lead to the gating of TRPM5 (By similarity).
Subcellular location: Membrane; Multi-pass membrane protein.
Interaction partners:
- Taste receptor type 1 member 1
- Taste receptor type 1 member 3
- Taste receptor type 1 member 2
- Guanine nucleotide-binding protein G
Sequence:
MLPTLSVFFMLTFVLLCFLGILANGFIVLMLSREWLLRGRLLPSDMILFSLGTSRFFQQCVGLVNSFYYFLHLVEYSGSLARQLISLHWDFLNSATFWFCTWLSVLFCIKIANFSHPAFLWLKWRFPALVPWFLLGSILVSVIVTLLFFWGNHTIYQAFLRRKFTGNTTFKEWNRRLEIDYFMPLKVVTMSIPCSLFLVSILLLISSLRRHSLRMQHNTHSLQDPNVQAHSRALKSLISFLVLYAVSFVSMIIDATVFISSDNVWYWPWQIILYFCMSVHPFILITNNLRFRGTFRQLLLLARGFWVA
Protein: tRNA N6-adenosine threonylcarbamoyltransferase, mitochondrial (EC 2.3.1.234) (N6-L-threonylcarbamoyladenine synthase) (t(6)A synthase) (O-sialoglycoprotein endopeptidase-like protein 1) (t(6)A37 threonylcarbamoyladenosine biosynthesis protein Osgepl1) (tRNA threonylcarbamoyladenosine biosynthesis protein Osgepl1) (Q6PEB4)
Organism: Mus musculus (Mouse)
Function: Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in mitochondrial tRNAs that read codons beginning with adenine. Probably involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37. Involved in mitochondrial genome maintenance.
Subcellular location: Mitochondrion {ECO:0000255|HAMAP-Rule:MF_03179}.
Interaction partners:
- EKC/KEOPS complex subunit Lage3
- Threonylcarbamoyl-AMP synthase
- EKC/KEOPS complex subunit Tprkb
- EKC/KEOPS complex subunit Tp53rkb
- tRNA dimethylallyltransferase
- non-specific serine/threonine protein kinase
- Mitochondrial tRNA-specific 2-thiouridylase 1
Sequence:
MLMLRRTAGAIPKPPKSKVYGFLRRFSVHPRTLSCHKLVLGIETSCDDTGAAVVDETGNVLGEALHSQTQVHLKTGGIVPPVAQQLHRENIQRIVEETLSACRITPSDLSAIATTIKPGLALSLGVGLSFSLQLVNQFKKPFIPIHHMEAHALTIRLTNKVEFPFLVLLISGGHCLLALVQGVSDFLLLGKSLDIAPGDMLDKVARRLSLIKHPECSTMSGGKAIEQLAKDGNRFHFTINPPMQNAKNCDFSFTGLQHITDKLITHKEKEEGIEKGQILSSAADIAAAVQHATACHLAKRTHRAILFCKQKNLLSPANAVLVVSGGVASNLYIRKALEIVANATQCTLLCPPPRLCTDNGIMIAWNGIERLRAGLGVLHDVEDIRYEPKCPLGVDISREVAEAAIKVPRLKMAL
Protein: F-box/LRR-repeat protein 3 (Q8RWU5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Potassium transporter 4
- Protein NRT1/ PTR FAMILY 8.2
- Two-pore potassium channel 1
- Zinc transporter 11
Sequence:
MKKVKQIRVLKPFDLLSEELVFIILDLISPNPSDLKSFSLTCKSFYQLESKHRGSLKPLRSDYLPRILTRYRNTTDLDLTFCPRVTDYALSVVGCLSGPTLRSLDLSRSGSFSAAGLLRLALKCVNLVEIDLSNATEMRDADAAVVAEARSLERLKLGRCKMLTDMGIGCIAVGCKKLNTVSLKWCVGVGDLGVGLLAVKCKDIRTLDLSYLPITGKCLHDILKLQHLEELLLEGCFGVDDDSLKSLRHDCKSLKKLDASSCQNLTHRGLTSLLSGAGYLQRLDLSHCSSVISLDFASSLKKVSALQSIRLDGCSVTPDGLKAIGTLCNSLKEVSLSKCVSVTDEGLSSLVMKLKDLRKLDITCCRKLSRVSITQIANSCPLLVSLKMESCSLVSREAFWLIGQKCRLLEELDLTDNEIDDEGLKSISSCLSLSSLKLGICLNITDKGLSYIGMGCSNLRELDLYRSVGITDVGISTIAQGCIHLETINISYCQDITDKSLVSLSKCSLLQTFESRGCPNITSQGLAAIAVRCKRLAKVDLKKCPSINDAGLLALAHFSQNLKQINVSDTAVTEVGLLSLANIGCLQNIAVVNSSGLRPSGVAAALLGCGGLRKAKLHASLRSLLPLSLIHHLEARGCAFLWKDNTLQAELDPKYWKQQLEEMAP
Protein: 3-deoxy-manno-octulosonate cytidylyltransferase, mitochondrial (EC 2.7.7.38) (CMP-2-keto-3-deoxyoctulosonic acid synthase) (AtCKS) (CMP-KDO synthase) (Q9C920)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes the production of the sugar nucleotide CMP-3-deoxy-D-manno-octulosonate (CMP-KDO). CTP is the preferred nucleotide donor, but it can partially be replaced with UTP. Activates KDO during the biosynthesis of rhamnogalacturonan II (RG-II), a structurally complex pectic polysaccharide of the primary cell wall. RG-II is essential for the cell wall integrity of rapidly growing tissues and pollen tube growth and elongation.
Subcellular location: Mitochondrion outer membrane {ECO:0000305|PubMed:21893514, ECO:0000305|PubMed:21896887}; Peripheral membrane protein {ECO:0000305|PubMed:21893514, ECO:0000305|PubMed:21896887}.
Interaction partners:
- 2-dehydro-3-deoxyphosphooctonate aldolase 2
- 2-dehydro-3-deoxyphosphooctonate aldolase 1
- Probable 3-deoxy-D-manno-octulosonic acid transferase, mitochondrial
- Probable arabinose 5-phosphate isomerase
- Probable acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase, mitochondrial
- Cyclin-dependent kinases regulatory subunit 1
- Probable UDP-3-O-acylglucosamine N-acyltransferase 1, mitochondrial
- Probable UDP-3-O-acylglucosamine N-acyltransferase 2, mitochondrial
Sequence:
MSVCSSSSSSQKTWIVNGILAGTAIAAAIGARAYLGRSKKFRSRVVGIIPARYASSRFEGKPLVQILGKPMIQRTWERSKLATTLDHIVVATDDERIAECCRGFGADVIMTSESCRNGTERCNEALEKLEKKYDVVVNIQGDEPLIEPEIIDGVVKALQVTPDAVFSTAVTSLKPEDGLDPNRVKCVVDNRGYAIYFSRGLIPYNKSGKVNPDFPYMLHLGIQSFDSKFLKVYSELQPTPLQQEEDLEQLKVLENGYKMKVIKVDHEAHGVDTPDDVEKIESLMRERNMS
Protein: Leucine aminopeptidase 2 (EC 3.4.11.-) (Epoxide hydrolase) (EC 3.3.2.10) (Leukotriene A-4 hydrolase homolog) (LTA-4 hydrolase) (O94544)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Aminopeptidase that preferentially cleaves di- and tripeptides. Also has low epoxide hydrolase activity (in vitro). Can hydrolyze the epoxide leukotriene LTA(4) but it forms preferentially 5,6-dihydroxy-7,9,11,14-eicosatetraenoic acid rather than the cytokine leukotriene B(4) as the product compared to the homologous mammalian enzyme (in vitro).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Meiotically up-regulated gene 61 protein
- Lap-Emerin-Man domain protein 2
- Aminopeptidase 1
- Autophagy receptor Nbr1
- Transcription initiation factor TFIID subunit 2
Sequence:
MKLRLDPSTQSNYHDVSISKLDWHARIDFDQELLHGKVSFVIQSARVSQALSHIILDTSYLEIKNVTINDIPTPFRVDKRRGFLGSALHIVPADEIPSSKSCILTILYSTTKDCTALQFLKPEQTIGGKFPYVFSECQAIHARSFIPCQDTPSVKVPCTFKIRSKLPVIASGIPCGTANFCNGSLEYLFEQKNPIPSYLFCILSGDLASTNIGPRSSVYTEPGNLLACKYEFEHDMENFMEAAEQLTLPYCWTRYDFVILPPSFPYGGMENPNATFATPTLIAGDRSNVNVIAHELAHSWSGNLVTNESWQCFWLNEGMTVFLERKILGRLYGEPTRQFEAIIGWGELEESVKLLGEDSEYTKLIQNLEGRDPDDAFSTVPYEKGSNFLYEIERVIGGPSVFEPFLPFYFRKFAKSTVNEVKFKHALYEYFSPLGLASKLDSIDWDTWYHAPGMPPVKPHFDTTLADPCYKLAESWTNSAKNSDDPSKFSSKDIENWSAGQKSLFLDVVYEAVSFPHNYIKRMGDVYSFAESKNAELSFRFFKLALKSKYKPLYNTIAERVGSVGRMKFVRPIFRLLNEADRAFAIETFEKYKHFYHKICASQVEKDLGLSE
Protein: Pituitary-specific positive transcription factor 1 (PIT-1) (Growth hormone factor 1) (GHF-1) (Q08478)
Organism: Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri)
Function: Transcription factor that activates growth hormone and prolactin genes. Specifically binds to the consensus sequence 5'-TAAAT-3'.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:P28069}.
Interaction partners:
Sequence:
MSCQAFSADSFTTLAGDSLPLLMHHASAADCLPSSASTHTHNMVSAVPSGLSLLQSSKRSHMHLSTSTLGNALSNGPPGLHYPVTPCHYSNQQTTYGMMAAQEMLSASISQTRILQTCSVPHPNMVNGANTLQGSLAPCLYKFPEHGLGGGSCSLSHSFPPLPPAVLSEEPPLGGTKDLRLRSRPPDDPPDMDSPQIRELEKFANDFKLRRIKLGYTQTNVGEALAAVHGSEFSQTTICRFENLQLSFKNACTLKAILAKWLDEAEQAGALFNEKMGMNERKRKRRTTISLGAKEALERSFGEKIKPSSQEIVRMAEGLHLEKEVVRVWFCNRRQREKRVKTSLHHSSYLTKDSPTYR
Protein: Clamp-binding protein CrfC (Clamp-binding sister replication fork colocalization protein) (P0DM85)
Organism: Escherichia coli (strain K12)
Function: Important for the colocalization of sister nascent DNA strands after replication fork passage during DNA replication, and for positioning and subsequent partitioning of sister chromosomes. Does not have GTPase activity on its own.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:23994470}. Note=About half the protein co-localizes with beta sliding clamp (DnaN) at midcell, the rest without clamp in quarter-cell positions when chromosomes are condensed during DNA replication.
Interaction partners:
- Uncharacterized protein YjcZ
- Uncharacterized protein YkfB
- Cyclic di-GMP phosphodiesterase PdeH
- Fructoselysine 3-epimerase
- Fructoselysine 6-phosphate deglycase
- Putative colanic acid biosynthesis glycosyl transferase WcaC
Sequence:
MYTQTLYELSQEAERLLQLSRQQLQLLEKMPLSVPGDDAPQLALPWSQPNIAERHAMLNNELRKISRLEMVLAIVGTMKAGKSTTINAIVGTEVLPNRNRPMTALPTLIRHTPGQKEPVLHFSHVAPIDCLIQQLQQRLRDCDIKHLTDVLEIDKDMRALMQRIENGVAFEKYYLGAQPIFHCLKSLNDLVRLAKALDVDFPFSAYAAIEHIPVIEVEFVHLAGLESYPGQLTLLDTPGPNEAGQPHLQKMLNQQLARASAVLAVLDYTQLKSISDEEVREAILAVGQSVPLYVLVNKFDQQDRNSDDADQVRALISGTLMKGCITPQQIFPVSSMWGYLANRARYELANNGKLPPPEQQRWVEDFAHAALGRRWRHADLADLEHIRHAADQLWEDSLFAQPIQALLHAAYANASLYALRSAAHKLLNYAQQAREYLDFRAHGLNVACEQLRQNIHQIEESLQLLQLNQAQVSGEIKHEIELALTSANHFLRQQQDALKVQLAALFQDDSEPLSEIRTRCETLLQTAQNTISRDFTLRFAELESTLCRVLTDVIRPIEQQVKMELSESGFRPGFHFPVFHGVVPHFNTRQLFSEVISRQEATDEQSTRLGVVRETFSRWLNQPDWGRGNEKSPTETVDYSVLQRALSAEVDLYCQQMAKVLAEQVDESVTAGMNTFFAEFASCLTELQTRLRESLALRQQNESVVRLMQQQLQQTVMTHGWIYTDAQLLRDDIQTLFTAERY
Protein: Uncharacterized protein C3orf38 (Q5JPI3)
Organism: Homo sapiens (Human)
Function: May be involved in apoptosis regulation.
Interaction partners:
- Zinc finger protein 654
Sequence:
MEMSGLSFSEMEGCRNLLGLLDNDEIMALCDTVTNRLVQPQDRQDAVHAILAYSQSAEELLRRRKVHREVIFKYLATQGIVIPPATEKHNLIQHAKDYWQKQPQLKLKETPEPVTKTEDIHLFQQQVKEDKKAEKVDFRRLGEEFCHWFFGLLNSQNPFLGPPQDEWGPQHFWHDVKLRFYYNTSEQNVMDYHGAEIVSLRLLSLVKEEFLFLSPNLDSHGLKCASSPHGLVMVGVAGTVHRGNTCLGIFEQIFGLIRCPFVENTWKIKFINLKIMGESSLAPGTLPKPSVKFEQSDLEAFYNVITVCGTNEVRHNVKQASDSGTGDQV