wanglab/gogpt-training-data huggingface dataset:
Protein: Aspartic protease 3 (EC 3.4.23.-) (P55956)
Organism: Caenorhabditis elegans
Function: Aspartic protease (Probable). Part of the necrosis cell death pathway. Involved in neuronal cell degeneration. Involved in heat stress response.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:12410314}. Lysosome {ECO:0000269|PubMed:12410314}. Secreted {ECO:0000305}.
Interaction partners:
- Peptidase C1A papain C-terminal domain-containing protein
- Peptidase A1 domain-containing protein
- Gut-specific cysteine proteinase
- Cathepsin B-like cysteine proteinase 4
- Cathepsin B-like cysteine proteinase 5
- Cathepsin B-like cysteine proteinase 6
- Peptidase C1A papain C-terminal domain-containing protein
- Peptidase C1A papain C-terminal domain-containing protein
- Cathepsin B-like cysteine proteinase 3
- Peptidase C1A papain C-terminal domain-containing protein
Sequence:
MSGRVFLLLALVALASAIQRIKLEKRTYTREQYKFGSIQEHLKAKYVPGYIPNKDAFNEGLSDYSNAQYYGPVTIGTPPQNFQVLFDTGSSNLWVPCANCPFGDIACRMHNRFDCKKSSSCTATGASFEIQYGTGSMKGTVDNDVVCFGHDTTYCTDKNQGLACATSEPGITFVAAKFDGIFGMGWDTISVNKISQPMDQIFANSAICKNQLFAFWLSRDANDITNGGEITLCDTDPNHYVGNIAWEPLVSEDYWRIKLASVVIDGTTYTSGPIDSIVDTGTSLLTGPTDVIKKIQHKIGGIPLFNGEYEVECSKIPSLPNITFNLGGQNFDLQGKDYILQMSNGNGGSTCLSGFMGMDIPAPAGPLWILGDVFIGRFYSVFDHGNKRVGFATSRTGK
Protein: C2H2 and C2HC zinc fingers superfamily protein (Q9FF62)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Chloride conductance regulatory protein ICln
- E3 ubiquitin-protein ligase MPSR1
Sequence:
MLSSDSNYASDISDDASATGSIENPIYKCKYCPRKFDKTQALGGHQNAHRKEREVEKQQKAFLAHLNRPEPDLYAYSYSYHHSFPNQYALPPGFEQPQYKVDRSYKMSMVYNQYVGSSSSSFAGLQSDPSQGMNQDWTFTGIPFLPQSQPQPLSSPICLDLCLGIGSSQTQPQPQEPNDATEEMDAEKENDGSSLSLSLKL
Protein: Uncharacterized protein C22F8.03c (Q9UUI9)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Interaction partners:
Sequence:
MSTVLIPTFVPYGKNLLNTSFSFSSLLCILCFYKDGPLLFLYSPLSASYYCLLYASYTWNFVLSDEAYFQAAPGRSVRFAVLCLKPMATKKANKMHVFMQAACFHFRIATMTVIGNMARSDHDTALNCVKRIN
Protein: Combgap, isoform F (A8DYD3)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MCAAQNPPPFGYTWGFADNGNRAAESVLEISPNINYTVSGESMPYLLSTDGSLAVQKDVKGLTAGGKNNVVRRMFVVNDPSFPPGTQRVITAGGASTVVKKQDNNQQVLSLDKNYLLVDPATAAAAAAAAGGDSGLAHHHTLTNGSIVDAKTGQTVLTAGSAAAKSHFSSIGALHLTQEECNEILIKRAIAAGHHQTHTITAADGSHHHASGGTPIQVQKVIQGLEDNEDSQGEAPNLKLEPGTLELSPKTELQESMHFSETDATIKKERPYSCDECGKSFLLKHHLTTHARVHTGERPHICTHCGKSFAHKHCLNTHLLLHSTERPYQCQECKKSFTLKHHLLTHSRVHSRERPFVCQECGRAFPLKRHLVTHSKFHAGERPYVCEECGESFAQENHLIMHSRFHGSLNPFVCAECGASFPRKFQLVNHGRIHGKIPHSCTVCGKEFLQKRTLVSHMRRVHTGEQAHPCVSCGEGFLTKAELHQHVRTAHNGVNPNTSSATIIANQQLQQAHHHQAGQQTHPQTITVVSNPGNSTLLTVSTTDANGVARPQFVCRECGSAFNSREALALHLRLHTGDKSLMTDLCALTAALPGHFLSTASLNPGTVVTANPNLVGQSPVPVQIISSTGQVMSQTTLVQAANSTHPQAVVTAVPTMPVHGQQQHLQHVAQQQQQQQQQQQQQQQHVVSVAPANKPKSHFCASCGKGFAAKHGLMQHNRRHPNGGCTVRTHVCECGKAFFQKNHLMLHQRQHLETKPAISQQQLVVPTTSY
Protein: Lipoxygenase 4, chloroplastic (AtLOX4) (EC 1.13.11.12) (LOX3-like protein) (Q9FNX8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Plant lipoxygenases may be involved in a number of diverse aspects of plant physiology including growth and development, pest resistance, and senescence or responses to wounding. Catalyzes the hydroperoxidation of lipids containing a cis,cis-1,4-pentadiene structure (By similarity). 13S-lipoxygenase that can use linolenic acid as substrates.
Subcellular location: Plastid, chloroplast {ECO:0000305}.
Interaction partners:
- Allene oxide synthase, chloroplastic
- Probable inactive linolenate hydroperoxide lyase
- Alpha-dioxygenase 1
- Allene oxide cyclase 3, chloroplastic
- Alpha-dioxygenase 2
- Phospholipase A
- 12-oxophytodienoate reductase 3
- Allene oxide cyclase 1, chloroplastic
- Allene oxide cyclase 2, chloroplastic
- Allene oxide cyclase 4, chloroplastic
Sequence:
MALANEIMGSRLIFERSSSLASPFHSRFSIKKKTQRTQFSINPFDPRPMRAVNSSGVVAAISEDLVKTLRISTVGRKQEKEEEEEKSVKFKVRAVATVRNKNKEDFKETLVKHLDAFTDKIGRNVVLELMSTQVDPKTNEPKKSKAAVLKDWSKKSNSKAERVHYTAEFTVDSAFGSPGAITVTNKHQKEFFLESITIEGFACGPVHFPCNSWVQSQKDHPSKRILFTNQPYLPSETPSGLRTLREKELENLRGNGKGERKLSDRIYDYDVYNDIGNPDISRELARPTLGGREFPYPRRCRTGRSSTDTDMMSERRVEKPLPMYVPRDEQFEESKQNTFAACRLKAVLHNLIPSLKASILAEDFANFGEIDSLYKEGLLLKLGFQDDMFKKFPLPKIVTTLQKSSEGLLRYDTPKIVSKDKYAWLRDDEFARQAIAGINPVNIERVTSYPPVSNLDPEIYGPGLHSALTEDHIIGQLDGLTVQQALETNRLFMVDYHDIYLPFLDRINALDGRKAYATRTILFLTRLGTLKPIAIELSLPSQSSSNQKSKRVVTPPVDATSNWMWQLAKAHVGSNDAGVHQLVNHWLRTHACLEPFILAAHRQLSAMHPIFKLLDPHMRYTLEINAVARQTLISADGVIESCFTAGQYGLEISSAAYKNKWRFDMEGLPADLIRRGMAVPDPTQPHGLKLLVEDYPYANDGLLLWSAIQTWVRTYVERYYANSNLIQTDTELQAWYSESINVGHADHRDAEWWPKLSTVEDLVSVITTIIWLASAQHAALNFGQYPYGGYVPNRPPLMRRLIPDESDPEFTSFIEDPQKYFFSSMPSLLQTTKFMAVVDTLSTHSPDEEYIGERQQPSIWTGDAEIVDAFYGFSAEIGRIEKEIDKRNRDPSRRNRCGAGVLPYELMAPSSEPGVTCRGVPNSVSI
Protein: Ephrin type-A receptor 1 (mEpha1) (EC 2.7.10.1) (Embryonic stem cell kinase) (Tyrosine-protein kinase receptor ESK) (Q60750)
Organism: Mus musculus (Mouse)
Function: Receptor tyrosine kinase which binds promiscuously membrane-bound ephrin-A family ligands residing on adjacent cells, leading to contact-dependent bidirectional signaling into neighboring cells. The signaling pathway downstream of the receptor is referred to as forward signaling while the signaling pathway downstream of the ephrin ligand is referred to as reverse signaling. Binds with a low affinity EFNA3 and EFNA4 and with a high affinity to EFNA1 which most probably constitutes its cognate/functional ligand. Upon activation by EFNA1 induces cell attachment to the extracellular matrix inhibiting cell spreading and motility through regulation of ILK and downstream RHOA and RAC. Also plays a role in angiogenesis and regulates cell proliferation. May play a role in apoptosis.
Subcellular location: Cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.
Interaction partners:
- Ephrin-A1
- Ephrin-A4
- Ephrin-A2
- Ephrin-A5
- Ephrin-A3
- Ephrin-B2
- Ephrin-B1
- Ephrin-B3
- Ephexin-1
- Tyrosine-protein kinase ABL1
Sequence:
MERRWPLGLALLLLLLCAPLPPGARAEEVTLMDTSTAQGELGWLLDPPETGWSEVQQMLNGTPLYMYQDCPIQEGGDTDHWLRSNWIYRGEEASRIYVELQFTVRDCKSFPGGAGPLGCKETFNLFYMESDQDVGIQLRRPLFQKVTTVAADQSFTIRDLASGSVKLNVERCSLGHLTRRGLYLAFHNPGSCVALVSVRVFYQRCAETVHGLAHFPDTLPGPGGLVEVAGTCLSHAQISLGSSGTPRMHCSPDGEWLVPVGQCQCEPGYEESSGNVGCTACPTGFYRVDMNTLRCLKCPQHSIAESEGSTICTCENGHYRAPGEGPQVACTRPPSAPQNLSFSTSGTQLSLRWEPPRDTGGRHDIRYSVECLQCRGIAQDGGPCQPCGKGVHFSPAASGLTTSTVQVQGLEPYANYTFTVKSQNRVSGLDSSSPSSASLSINMGHAESLSGLSLKLVKKEPRQLELTWAGSRPRNPGGNLSYELHVLNQDEEWHQMVLEPRVLLTKLQPDTTYIVRVRTLTPLGPGPFSPDHEFRTSPPVSRSLTGGEIVAVIFGLLLGIALLIGIYVFRSRRGQRQRQQRQRERTTNVDREDKLWLKPYVDLQAYEDPAQGALDFAQELDPAWLIVDTVIGEGEFGEVYRGALRLPSQDCKTVAIKTLKDTSPDGYWWNFLREATIMGQFNHPHILRLEGVITKRKPIMIITEFMENGALDAFLKEREDQLAPGQLVAMLLGIASGMNCLSGHNYVHRDLAARNILVNQNLCCKVSDFGLTRLLDDFDGTYETQGGKIPIRWTAPEAIAHRIFTTASDVWSFGIVMWEVLSFGDKPYGEMSNQEVMKSIEDGYRLPPPVDCPAPLYELMKNCWAYDRARRPHFLQLQAHLEQLLTDPHSLRTIANFDPRVTLRLPSLSGSDGIPYRSVSEWLESIRMKRYILHFRSAGLDTMECVLELTAEDLTQMGITLPGHQKRILCSIQGFKD
Protein: Origin recognition complex subunit 4 (O43929)
Organism: Homo sapiens (Human)
Function: Component of the origin recognition complex (ORC) that binds origins of replication. DNA-binding is ATP-dependent. The specific DNA sequences that define origins of replication have not been identified yet. ORC is required to assemble the pre-replication complex necessary to initiate DNA replication. Binds histone H3 and H4 trimethylation marks H3K9me3, H3K27me3 and H4K20me3.
Subcellular location: Nucleus.
Interaction partners:
- Origin recognition complex subunit 3
- Origin recognition complex subunit 5
- Origin recognition complex subunit 1
- DNA replication factor Cdt1
- Origin recognition complex subunit 2
- Cell division control protein 6 homolog
- Origin recognition complex subunit 6
- Protein DBF4 homolog A
- DNA replication licensing factor MCM6
- DNA replication licensing factor MCM2
Sequence:
MSSRKSKSNSLIHTECLSQVQRILRERFCRQSPHSNLFGVQVQYKHLSELLKRTALHGESNSVLIIGPRGSGKTMLINHALKELMEIEEVSENVLQVHLNGLLQINDKIALKEITRQLNLENVVGDKVFGSFAENLSFLLEALKKGDRTSSCPVIFILDEFDLFAHHKNQTLLYNLFDISQSAQTPIAVIGLTCRLDILELLEKRVKSRFSHRQIHLMNSFGFPQYVKIFKEQLSLPAEFPDKVFAEKWNENVQYLSEDRSVQEVLQKHFNISKNLRSLHMLLMLALNRVTASHPFMTAVDLMEASQLCSMDSKANIVHGLSVLEICLIIAMKHLNDIYEEEPFNFQMVYNEFQKFVQRKAHSVYNFEKPVVMKAFEHLQQLELIKPMERTSGNSQREYQLMKLLLDNTQIMNALQKYPNCPTDVRQWATSSLSWL
Protein: Collagen alpha-5(VI) chain (Collagen alpha-1(XXIX) chain) (A6H584)
Organism: Mus musculus (Mouse)
Function: Collagen VI acts as a cell-binding protein.
Subcellular location: Secreted, extracellular space, extracellular matrix {ECO:0000269|PubMed:18276594}. Note=Deposed in the extracellular matrix of skeletal muscle.
Interaction partners:
- Platelet glycoprotein VI
- CD44 antigen
- Integrin alpha-6
- Integrin beta-3
- Collagen alpha-2
- Integrin alpha-V
- Integrin beta-6
- Integrin alpha-7
- Integrin alpha-5
- Integrin beta-8
Sequence:
MKLRLIAFVLILWTETLADQSPGPGPEYADVVFLVDSSNYLGIKSFPFVRTFLNRMISSLPIEANKYRVALAQYSDALHNEFQLGTFKNRNPMLNHLKKNFGFIGGSLKIGNALQEAHRTYFSAPTNGRDKKQFPPILVVLASAESEDDVEEAAKALREDGVKIISVGVQKASEENLKAMATSQFHFNLRTARDLGMFAPNMTRIIKDVTQYREGTTVDLITAVAPTTPAAPATPAAPTIPAALTTAANHVDKTVPFPTSCQKDSLADLIFLVDESVGTTQNLRDLQNFLENVTSSVDVKDNCMRLGLMSFSDRAQTISSLRSSANQSEFQQQIQKLSLQTGASNVGAAIEQMRKEGFSESSGSRKAQGVPQIAVLVTHRASDDMVREAALDLRLEGVTMFAMGIEGANNTQLEDIVSYPSRQSISTHSSYSHLESYSGNFLKKIRNEIWTQVSTRAEQMELDKTGCVDTKEADIYFLIDGSSSIRKKEFEQIQIFMSSVIDMFPIGPNKVRVGVVQYSHKNEVEFPVSRYTDGIDLKKAVFNIKQLKGLTFTGKALDFILPLIKKGKTERTDRAPCYLIVLTDGKSNDSVLEPANRLRAEQITIHAIGIGEANKTQLRQIAGKDERVNFGQNFDSLKSIKNEIVHRICSEKGCEDMKADIMFLVDSSGSIGPTNFETMKTFMKNLVGKIQIGADRSQVGVVQFSDYNREEFQLNKYSTHEEIYAAIDRMSPINRNTLTGGALTFVNEYFDLSKGGRPQVRKFLILLTDGKAQDEVGGPATALRSKSVTIFSVGVYGANRAQLEEISGDGSLVFHVENFDHLKAIESKLIFRVCALHDCKRIELLDIVFVLDHSGSIGPREQESMMNLTIHLVKKADVGRDRVQIGALTYSNHPEILFYLNTYSSGSAIAEHLRRPRDTGGETYTAKALQHSNVLFTEEHGSRLTQNVRQLMIVITDGVSHDRDKLDEAARELRDKGITIFAVGVGNANQDELETMAGKKENTVHVDNFDKLRDIYLPLQETLCNNSQETCNLPEADVIFLCDGSDMVSDSEFVTMTTFLSDLIDNFDIESQRMKIGMAQYGSRYQEIIELESSLNKTQWKSQVHSVAQSKGLPRLDFALKHVSDMFDPSVGGRRNAGVPQTLVVITSSSPRYDVTDAVKVLKDLGICVLALGIGDVYKEQLLPITGNSEKIITFRDFNKLKNVDVKKRMVREICQSCGKANCFVDVVVGFDISTHRQGQPLFQGHPRLESYLPGILEDITSIRGVSCGAGAEAQVSLAFKVNSDQEFPAKFQIYQKAAFDSLLHVTVRGPTHLDAPFLQSLWDMFEERSASRGQVLLIFSDGLQGESITLLERQSDRLREAGLDALLVVSLNTFGHDEFSSFEFGKGFDYRTQLTIGMLDLGKTLSQYLGNIAERACCCTFCKCPGIPGPHGTRGLQASKGSSGPKGSRGHRGEDGDPGRRGEIGLQGDRGVVGCPGTRGQKGVKGFSGAQGEHGEDGLDGLDGEEGFYGFRGGKGQKGDPGNQGYPGIRGAAGEDGEKGFPGDPGDPGKDSNIKGQKGEKGERGRQGITGQKGTHGRPSSKGSRGMEGQRGPQGPSGQAGNPGPQGTQGPEGLQGSQGSSGNRGGKGDKGSQGYQGPQGSPGPAGPRGDIGRPGFGGRKGEPGVPGGPGPVGPPGQRGKQGDYGIPGYGQTGRKGVKGPTGFPGDPGQKGDAGNPGIPGGPGPKGFKGLTLSQGLKGRSGLQGSQGPPGRRGPKGTAGQPIYSPCELIQFLRDHSLIFTDKCPVYPTELVFALDQSSGITERRFNETRDTITSIVSDLNIRENNCPVGARVAVVSYDSDTSYLIRGSDYHNKKHLLQLLSQIKYQVPRKARDIGNAMRFVARNVFKRMSAGTNTRRVAVFFSNGQAASRASILTATMELSALDISLAVFAYNERVFLDEAFGFDDTGTFQVIPVPPVGDYEPLEKLRRCTLCYDKCFPNTCAEEPFFPENSYMDVAFLLDNSKNIASDDFQAVKALVSSVIDSFHITSNPSASESGDRVALLSYSPSESSRRKGRVKTEFAFTTYDNQSIMKNYIYTSLQQLNGDATIGLALQWAMEGLFLGTPNPRKHKVIIVISAGENHEEKEFVKTVALRAKCQGYVVFVISLGSTQRDEMEELASYPLDHHLIQLGRMYKPDLNYIVKFLKPFIYSVRRGFNQYPPPTLKDDCRLVELERGDTLPHGLRLTAKLREVPESTISLADQELNAGKDSSFVLEDHRGDHLVYVPSQMLEPHKLVSHYGNDRESVAMASLTSEHESHGREELGLAHEPGDASLQEYYMDVAFLIDASQRVGGRNEFKEVRTLITSVLDYFHIAPAPLTSVLGDRVAVLTYSPPGYLPNTEECPVYLEFDLVTYNTVHQMKHHLQESLQQLNGDVFIGHALQWTVDNVFVGTPNLRKNKVIFIVTAGETNPLDKEVLRNASLRAKCQGYSIFVFSFGPIHNDMELEELASHPLDHHLVRLGRVHRPDLDYVIKFIKPFVHSIRRAINKYPGRDLQAKCDNLTFPGPENAGTEDSALLIPEVYRIEAGENELSGDSGSQEQHFFLLGNSHGNHSESTADLMRQLYLLLSSGELMVNDKEEPCSAETPAPVNSKQDGEDAR
Protein: GTP cyclohydrolase II (EC 3.5.4.25) (F4KJA1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MMDSALYHPRIFFAHSFINGLYSSPRFANTCWRLVSRSSWEIKASENSDRNVFDENPVRKTDGSLFDSASFETVDAEITPETDDFFVSDAEGDPDCPTQGYSSIELALQALRKGKVCSLTIFLKTSDYDDLFLQLYRFGLTKKLSLMFQFVIVVDDETGDVEGNLIMAATLTSPKDIAFLIKNGSGIVSVGMKKENLERLSLTLMSPEMEDEDSSAPTFTITVDAKSGTSTGVSASDRAMTVLALSSLDAKPDDFRRPGHVFPLKYRDGGVLRRAGHTEASVDLMILAGLRPLSVLSAILDQEDGSMASLPYMKKLATEHDIPIVSLTDLIRYRRKRDKLVERITVSRLPTKWGLFQAYCYRSKLDGTENIALVKGNVGNGEDILVRVHSECLTGDIFGSARCDCGNQLDLAMELIEKEGRGVVVYLRGHEGRGIGLGHKLRAYNLQDEGHDTVQANVELGLSIDSREYGIGAQMLRDIGVRTMRLMTNNPAKFTGLKGYGLAVVGRVPVVTPITKENRRYMETKRKKMGHIYISDNNDQPLA
Protein: Proteoglycan 3 (Eosinophil major basic protein homolog) (Prepro-major basic protein homolog) (Prepro-MBPH) (Q9Y2Y8)
Organism: Homo sapiens (Human)
Function: Possesses similar cytotoxic and cytostimulatory activities to PRG2/MBP. In vitro, stimulates neutrophil superoxide production and IL8 release, and histamine and leukotriene C4 release from basophils.
Subcellular location: Cytoplasmic granule {ECO:0000269|PubMed:10318872}. Note=Localized to the eosinophil secondary granule.
Interaction partners:
- Eosinophil peroxidase
Sequence:
MQCLLLLPFLLLGTVSALHLENDAPHLESLETQADLGQDLDSSKEQERDLALTEEVIQAEGEEVKASACQDNFEDEEAMESDPAALDKDFQCPREEDIVEVQGSPRCKICRYLLVRTPKTFAEAQNVCSRCYGGNLVSIHDFNFNYRIQCCTSTVNQAQVWIGGNLRGWFLWKRFCWTDGSHWNFAYWSPGQPGNGQGSCVALCTKGGYWRRAQCDKQLPFVCSF
Protein: Erythromycin 3''-O-methyltransferase (EC 2.1.1.254) (Erythromycin biosynthesis protein G) (A4F7P5)
Organism: Saccharopolyspora erythraea (strain ATCC 11635 / DSM 40517 / JCM 4748 / NBRC 13426 / NCIMB 8594 / NRRL 2338)
Function: S-adenosyl-L-methionine-dependent O-methyltransferase that catalyzes the last step in the erythromycin biosynthesis pathway. Methylates the position 3 of the mycarosyl moiety of erythromycin C, forming the most active form of the antibiotic, erythromycin A. Can also methylate the precursor erythromycin D, forming erythromycin B.
Interaction partners:
- 3-alpha-mycarosylerythronolide B desosaminyl transferase
- Cytochrome P450 family protein EryCII
- Erythromycin C-12 hydroxylase
- 6-deoxyerythronolide-B synthase
- 6-deoxyerythronolide-B synthase
- TDP-4-keto-6-deoxyhexose 2,3-reductase
- 6-deoxyerythronolide-B synthase
Sequence:
MSVKQKSALQDLVDFAKWHVWTRVRPSSRARLAYELFADDHEATTEGAYINLGYWKPGCAGLEEANQELANQLAEAAGISEGDEVLDVGFGLGAQDFFWLETRKPARIVGVDLTPSHVRIASERAERENVQDRLQFKEGSATDLPFGAETFDRVTSLESALHYEPRTDFFKGAFEVLKPGGVLAIGDIIPLDLREPGSDGPPKLAPQRSGSLSGGIPVENWVPRETYAKQLREAGFVDVEVKSVRDNVMEPWLDYWLRKLQDESFKKSVSRLFYSQVKRSLTSDSGMKGELPALDFVIASARKPGA
Protein: Kinesin heavy chain (P17210)
Organism: Drosophila melanogaster (Fruit fly)
Function: Kinesin is a microtubule-associated force-producing protein that may play a role in organelle transport. Milt and Miro form an essential protein complex that links Khc to mitochondria for light chain-independent, anterograde transport of mitochondria.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000305}.
Interaction partners:
- Kinesin light chain
- Tropomyosin-1, isoforms 9A/A/B
- Trafficking kinesin-binding protein milt
- LD08195p
- Tubulin beta chain
- Kinesin-like protein Klp61F
- Kinesin-like protein at 67A, isoform A
- Mitochondrial Rho GTPase
- Kinesin-like protein Nod
- GH10889p
Sequence:
MSAEREIPAEDSIKVVCRFRPLNDSEEKAGSKFVVKFPNNVEENCISIAGKVYLFDKVFKPNASQEKVYNEAAKSIVTDVLAGYNGTIFAYGQTSSGKTHTMEGVIGDSVKQGIIPRIVNDIFNHIYAMEVNLEFHIKVSYYEIYMDKIRDLLDVSKVNLSVHEDKNRVPYVKGATERFVSSPEDVFEVIEEGKSNRHIAVTNMNEHSSRSHSVFLINVKQENLENQKKLSGKLYLVDLAGSEKVSKTGAEGTVLDEAKNINKSLSALGNVISALADGNKTHIPYRDSKLTRILQESLGGNARTTIVICCSPASFNESETKSTLDFGRRAKTVKNVVCVNEELTAEEWKRRYEKEKEKNARLKGKVEKLEIELARWRAGETVKAEEQINMEDLMEASTPNLEVEAAQTAAAEAALAAQRTALANMSASVAVNEQARLATECERLYQQLDDKDEEINQQSQYAEQLKEQVMEQEELIANARREYETLQSEMARIQQENESAKEEVKEVLQALEELAVNYDQKSQEIDNKNKDIDALNEELQQKQSVFNAASTELQQLKDMSSHQKKRITEMLTNLLRDLGEVGQAIAPGESSIDLKMSALAGTDASKVEEDFTMARLFISKMKTEAKNIAQRCSNMETQQADSNKKISEYEKDLGEYRLLISQHEARMKSLQESMREAENKKRTLEEQIDSLREECAKLKAAEHVSAVNAEEKQRAEELRSMFDSQMDELREAHTRQVSELRDEIAAKQHEMDEMKDVHQKLLLAHQQMTADYEKVRQEDAEKSSELQNIILTNERREQARKDLKGLEDTVAKELQTLHNLRKLFVQDLQQRIRKNVVNEESEEDGGSLAQKQKISFLENNLDQLTKVHKQLVRDNADLRCELPKLEKRLRCTMERVKALETALKEAKEGAMRDRKRYQYEVDRIKEAVRQKHLGRRGPQAQIAKPIRSGQGAIAIRGGGAVGGPSPLAQVNPVNS
Protein: nebramycin 5' synthase (EC 6.1.2.2) (Kanamycin A carbamoyltransferase) (Tobramycin carbamoyltransferase) (Q70IY1)
Organism: Streptoalloteichus tenebrarius (strain ATCC 17920 / DSM 40477 / JCM 4838 / CBS 697.72 / NBRC 16177 / NCIMB 11028 / NRRL B-12390 / A12253. 1 / ISP 5477) (Streptomyces tenebrarius)
Function: TobZ is involved in the biosynthesis of the 2-deoxystreptamine-containing aminoglycoside antibiotics such as nebramycin 5 and 6-O-carbamoylkanamycin. Catalyzes the hydrolysis of carbamoyl phosphate and its subsequent adenylation by ATP to yield O-carbamoyladenylate. Then it catalyzes the transfer of the carbamoyl moiety from O-carbamoyladenylate to the tobramycin 6-hydroxy group to yield nebramycin 5'. It catalyzes the same reaction with kanamycin A. These reactions are considerably slower in the presence of deoxy-ATP.
Interaction partners:
Sequence:
MRVLGLNGWPRDFHDASAALLVDGRIAAFAEEERFTRKKHGYNTAPVQAAAFCLAQAGLTVDDLDAVAFGWDLPAMYRERLGGWPHSDSEALDILLPRDVFPRRTDPPLHFVQHHLAHAASAYYFSGEDRGAVLIVDGQGEEECVTLAHAEGGKITVLDTVPGAWSLGFFYEHVSEYTGLGGDNPGKLMGLAAHGTTVDETLSAFAFDSDGYRLNLIDPQARDPEDWDEYSVTERAWFAHLERIYRLPPNEFVRRYDPAKGRVVRDTRRDPYEYRDLAATAQAALERAVFGLADSVLARTGERTLFVAGGVGLNATMNGKLLTRSTVDKMFVPPVASDIGVSLGAAAAVAVELGDRIAPMGDTAAWGPEFSPDQVRAALDRTGLAYREPANLEREVAALIASGKVVGWAQGRGEVGPRALGQRSLLGSAHSPTMRDHINLRVKDREWWRPFAPSMLRSVSDQVLEVDADFPYMIMTTKVRAAYAERLPSVVHEDWSTRPQTVTEASNPRYHRMLTELGDLVGDPVCLNTSFNDRGEPIVSSPADALLTFSRLPIDALAVGPYLVTKDLRH
Protein: Delta(3,5)-Delta(2,4)-dienoyl-CoA isomerase, mitochondrial (EC 5.3.3.-) (Q62651)
Organism: Rattus norvegicus (Rat)
Function: Isomerization of 3-trans,5-cis-dienoyl-CoA to 2-trans,4-trans-dienoyl-CoA.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:11278886, ECO:0000269|PubMed:9417087}. Peroxisome {ECO:0000269|PubMed:11278886, ECO:0000269|PubMed:9417087}.
Interaction partners:
- Enoyl-CoA delta isomerase 2
- Enoyl-CoA delta isomerase 1, mitochondrial
- 3-ketoacyl-CoA thiolase, mitochondrial
- Acyl-coenzyme A thioesterase 2, mitochondrial
- 2,4-dienoyl-CoA reductase [
- Medium-chain specific acyl-CoA dehydrogenase, mitochondrial
- Very long-chain specific acyl-CoA dehydrogenase, mitochondrial
- Peroxisomal acyl-coenzyme A oxidase 1
- Peroxisomal targeting signal 1 receptor
- Hydroxyacyl-coenzyme A dehydrogenase, mitochondrial
Sequence:
MATAMTVSSKLLGLLMQQLRGTRQLYFNVSLRSLSSSAQEASKRIPEEVSDHNYESIQVTSAQKHVLHVQLNRPEKRNAMNRAFWRELVECFQKISKDSDCRAVVVSGAGKMFTSGIDLMDMASDILQPPGDDVARIAWYLRDLISRYQKTFTVIEKCPKPVIAAIHGGCIGGGVDLISACDIRYCTQDAFFQVKEVDVGLAADVGTLQRLPKVIGNRSLVNELTFTARKMMADEALDSGLVSRVFPDKDVMLNAAFALAADISSKSPVAVQGSKINLIYSRDHSVDESLDYMATWNMSMLQTQDIIKSVQAAMEKKDSKSITFSKL
Protein: Adaptor related protein complex 3 subunit sigma 2 (Adaptor-related protein complex 3, sigma 2 subunit, isoform CRA_d) (H0YLI7)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasmic vesicle membrane {ECO:0000256|ARBA:ARBA00004180}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004180}; Cytoplasmic side {ECO:0000256|ARBA:ARBA00004180}. Golgi apparatus {ECO:0000256|ARBA:ARBA00004555}.
Interaction partners:
Sequence:
MIQAILVFNNHGKPRLVRFYQRFPEEIQQQIVRETFHLVLKRDDNICNFLEGGSLIGGSDYKLIYRHYATLYFVFCVDSSESELGILDLIQVHLEVVFFIAPKVFVETLDKCFENVCELDLIFHMDKVHYILQEVVMGGMVLETNMNEIVAQIEAQNRLEKSEGGLSAAPARAVSAVKNINLPEIPRNINIGDLNIKVPNLSQFV
Protein: Centrosomal protein of 83 kDa (Cep83) (Coiled-coil domain-containing protein 41) (Renal carcinoma antigen NY-REN-58) (Q9Y592)
Organism: Homo sapiens (Human)
Function: Component of the distal appendage region of the centriole involved in the initiation of primary cilium assembly. May collaborate with IFT20 in the trafficking of ciliary membrane proteins from the Golgi complex to the cilium during the initiation of primary cilium assembly.
Subcellular location: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000269|PubMed:23348840, ECO:0000269|PubMed:23530209}. Note=Localizes specifically to the distal appendage region of the centriole, which anchors the mother centriole to the plasma membrane. Localizes to centrioles at all stages of the cell cycle, including mitosis.
Interaction partners:
- Sodium channel and clathrin linker 1
- Centrosomal protein of 164 kDa
- Fas-binding factor 1
- Centrosomal protein of 89 kDa
- Outer dense fiber protein 2
- Ninein
- Intraflagellar transport protein 20 homolog
- Rab-3A-interacting protein
- Tau-tubulin kinase 2
- POTE ankyrin domain family member C
Sequence:
MVVSTFTDMDTFPNNFPPGGDSGLTGSQSEFQKMLIDERLRCEHHKANYQTLKAEHTRLQNEHVKLQNELKHLFNEKQTQQEKLQLLLEELRGELVEKTKDLEEMKLQILTPQKLELLRAQIQQELETPMRERFRNLDEEVEKYRAVYNKLRYEHTFLKSEFEHQKEEYARILDEGKIKYESEIARLEEDKEELRNQLLNVDLTKDSKRVEQLAREKVYLCQKLKGLEAEVAELKAEKENSEAQVENAQRIQVRQLAEMQATVRSLEAEKQSANLRAERLEKELQSSSEQNTFLINKLHKAEREINTLSSKVKELKHSNKLEITDIKLETARAKSELERERNKIQSELDGLQSDNEILKAAVEHHKVLLVEKDRELIRKVQAAKEEGYQKLVVLQDEKLELENRLADLEKMKVEHDVWRQSEKDQYEEKLRASQMAEEITRKELQSVRLKLQQQIVTIENAEKEKNENSDLKQQISSLQIQVTSLAQSENDLLNSNQMLKEMVERLKQECRNFRSQAEKAQLEAEKTLEEKQIQWLEEKHKLHERITDREEKYNQAKEKLQRAAIAQKKRKSLHENKLKRLQEKVEVLEAKKEELETENQVLNRQNVPFEDYTRLQKRLKDIQRRHNEFRSLILVPNMPPTASINPVSFQSSAMVPSMELPFPPHMQEEQHQRELSLLRKRLEELETTQRKQLEELGSSGE
Protein: Transcription factor MYB17 (Myb-related protein 17) (AtMYB17) (Protein LATE MERISTEM IDENTITY 2) (Q9M2D9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Transcription factor that may play a role in flower development by repressing ANT. Regulates the transition of meristem identity from vegetative growth to flowering. Acts downstream of LFY and upstream of AP1. Directly activates AP1 to promote floral fate. Together with LFY and AP1 may constitute a regulatory network that contributes to an abrupt and robust meristem identity transition.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00625, ECO:0000269|PubMed:19232308, ECO:0000269|PubMed:21750030}.
Interaction partners:
- Protein LEAFY
Sequence:
MGRTPCCDKIGLKKGPWTPEEDEVLVAHIKKNGHGSWRTLPKLAGLLRCGKSCRLRWTNYLRPDIKRGPFTADEEKLVIQLHAILGNRWAAIAAQLPGRTDNEIKNLWNTHLKKRLLSMGLDPRTHEPLPSYGLAKQAPSSPTTRHMAQWESARVEAEARLSRESMLFSPSFYSGVVKTECDHFLRIWNSEIGEAFRNLAPLDESTITSQSPCSRATSTSSALLKSSTNSWGGKEVTVAIHGSDYSPYSNDLEDDSTDSALQLLLDFPISDDDMSFLEENIDSYSQAPPIGLVSMVSKF
Protein: Transcription factor YY2 (Yin and yang 2) (YY-2) (Q3TTC2)
Organism: Mus musculus (Mouse)
Function: Functions as a multifunctional transcription factor that may exhibit positive and negative control on a large number of genes. May antagonize YY1 and function in development and differentiation.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Membrane-bound transcription factor site-2 protease
Sequence:
MASETEKLLCLNTESAEIPADFVELLPPDNIGDIEAVSLETSVGQTIEVYGDVGVDWAHGSQYHSPVIALQPLVGSSLSSRDHDKEMFVVQTREEEVVGYQDSDNLLFSPEFGSQMVLPVNEDDYLQPTTASFTGFLAAENGQGELSPYEGNLCGLTTFIEAGAEESVNADLGDKQWEQKQIDGLDGEFPFTMWDDVNEKEDPIAEEQAGESPPDYSEYMTGKKFPPEGIPGIDLSDPKQLAEFTSMRPKKPKGDFPRPIACSHKGCEKMFKDNSAMRKHLHIHGPRVHVCAECGKAFVESSKLKRHQLVHTGEKPYQCTFEGCGRRFSLDFNLRTHVRIHTGDKPFVCPFDACNKKFAQSTNLKSHILTHVKNKNDQ
Protein: Phosphatidylinositol:ceramide inositolphosphotransferase (LmjIPCS) (EC 2.7.8.-) (Inositol-phosphorylceramide synthase) (IPC synthase) (Sphingolipid synthase) (E9AFX2)
Organism: Leishmania major
Function: Bidirectional lipid inositolphosphotransferase capable of converting phosphatidylinositol (PI) and ceramide to inositol-phosphorylceramide (IPC) and diacylglycerol (DAG) and vice versa. Direction is dependent on the relative concentrations of DAG and ceramide as phosphoinositol acceptors. Essential for viability of the pathogenic bloodstream stage of this human protozoan parasite and, consequently, can be considered as potential drug target.
Subcellular location: Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Putative fatty acid desaturase
- Putative fatty acid desaturase
- Putative phosphatidic acid phosphatase
- serine C-palmitoyltransferase
- Serine palmitoyltransferase 1
- Inositol phosphosphingolipid phospholipase C-Like
- 3-dehydrosphinganine reductase
Sequence:
MTSHVTAHDVGGNEDIGTDHVPWYKQPLPLCTQVMRFILLLLLTVMFLGVAILVANARMPDPEKVRPLPDLLLESIPKVALLENGTNVIIFLLNATTVVVGFKVFLLERHMNGLPRVTFLVGVPKIGSFLNRMAFGVLDSGRRPFPLKNVFPIMAIRFLTSYAVVMVFRAFVIMGTSYPATDNHCQNPQVIEHPVLNVILTLVTLGSGAIHCGDLMFSGHTMILSLAFILAWDYSPFLHPWAVRVWVSVLLPISYYCILASRSHYTDDILVAMYVMIATYKVIDHAETGAPWQMQLLIRWMPWPGANTIEKWTADEVVVVVQTPAEDSTDASAALPEH