wanglab/gogpt-training-data huggingface dataset:
Protein: Voltage-gated potassium channel KCNC1 (NGK2) (Potassium voltage-gated channel subfamily C member 1) (RAW2) (Voltage-gated potassium channel subunit Kv3.1) (Voltage-gated potassium channel subunit Kv4) (P25122)
Organism: Rattus norvegicus (Rat)
Function: Voltage-gated potassium channel that plays an important role in the rapid repolarization of fast-firing brain neurons. The channel opens in response to the voltage difference across the membrane, forming a potassium-selective channel through which potassium ions pass in accordance with their electrochemical gradient. Can form functional homotetrameric channels and heterotetrameric channels that contain variable proportions of KCNC2, and possibly other family members as well. Contributes to fire sustained trains of very brief action potentials at high frequency in pallidal neurons.
Subcellular location: Cell membrane {ECO:0000269|PubMed:10482766, ECO:0000269|PubMed:14679187, ECO:0000269|PubMed:24161696}; Multi-pass membrane protein {ECO:0000255}. Cell projection, axon {ECO:0000269|PubMed:20857303}. Presynaptic cell membrane {ECO:0000269|PubMed:20857303}. Note=Localizes in parallel fiber membranes, distributed on the perisynaptic and extrasynaptic membranes away from the active zones. {ECO:0000269|PubMed:20857303}.
Interaction partners:
- A-type potassium channel modulatory protein KCNIP1
- A-type potassium channel modulatory protein KCNIP2
- Calsenilin
- A-type potassium channel modulatory protein DPP6
- Voltage-gated potassium channel subunit beta-1
- Kv channel-interacting protein 2x
- Kv channel-interacting protein 4
- Voltage-gated potassium channel subunit beta-2
- Inactive dipeptidyl peptidase 10
- Caveolin-3
Sequence:
MGQGDESERIVINVGGTRHQTYRSTLRTLPGTRLAWLAEPDAHSHFDYDPRADEFFFDRHPGVFAHILNYYRTGKLHCPADVCGPLYEEELAFWGIDETDVEPCCWMTYRQHRDAEEALDSFGGAPLDNSADDADADGPGDSGDGEDELEMTKRLALSDSPDGRPGGFWRRWQPRIWALFEDPYSSRYARYVAFASLFFILVSITTFCLETHERFNPIVNKTEIENVRNGTQVRYYREAETEAFLTYIEGVCVVWFTFEFLMRVVFCPNKVEFIKNSLNIIDFVAILPFYLEVGLSGLSSKAAKDVLGFLRVVRFVRILRIFKLTRHFVGLRVLGHTLRASTNEFLLLIIFLALGVLIFATMIYYAERIGAQPNDPSASEHTHFKNIPIGFWWAVVTMTTLGYGDMYPQTWSGMLVGALCALAGVLTIAMPVPVIVNNFGMYYSLAMAKQKLPKKKKKHIPRPPQLGSPNYCKSVVNSPHHSTQSDTCPLAQEEILEINRADSKLNGEVAKAALANEDCPHIDQALTPDEGLPFTRSGTRERYGPCFLLSTGEYACPPGGGMRKDLCKESPVIAKYMPTEAVRVT
Protein: Na(+)/H(+) antiporter subunit F (Mrp complex subunit F) (Multiple resistance and pH homeostasis protein F) (Sodium-cholate efflux protein MrpF) (O05228)
Organism: Bacillus subtilis (strain 168)
Function: Mrp complex is a Na(+)/H(+) antiporter that is considered to be the major Na(+) excretion system in B.subtilis. Has a major role in Na(+) resistance and a minor role in Na(+)- and K(+)-dependent pH homeostasis as compared to TetB. MrpA may be the actual Na(+)/H(+) antiporter, although the six other Mrp proteins are all required for Na(+)/H(+) antiport activity and Na(+) resistance. MrpA is required for initiation of sporulation when external Na(+) concentration increases. Also transports Li(+) but not K(+), Ca(2+) or Mg(2+).
Subcellular location: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Na
- Na
- Na
- Na
- Na
- Na
- Probable inorganic carbon transporter subunit DabB
Sequence:
MFTLILQIALGIMAVSTFLYVIRVIKGPTVPDRVVALDAIGINLIAITALVSILLKTSAFLDIILLLGILSFIGTIAFSKFLEKGEIIENDRNR
Protein: Exocyst complex component EXO70A1 (AtExo70a1) (Exocyst subunit Exo70 family protein A1) (Q9LZD3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Component of the exocyst complex involved in the docking of exocytic vesicles with fusion sites on the plasma membrane during regulated or polarized secretion. Involved in polarized cell growth and organ morphogenesis. Involved in polarized cell growth and organ morphogenesis. During cytokinesis, involved in cell plate initiation, cell plate maturation and formation of new primary cell wall. Participates in polarized pectin delivery required for the polarized development of the mucilage-producing volcano cells of the seed coat. Involved in the recycling and localization of auxin efflux carriers PIN1 and PIN2, and thus in polar auxin transport regulation. Functions in vesicle trafficking in tracheary elements to regulate patterned secondary cell wall (SCW) thickening.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:19895414}. Cytoplasm, cytoskeleton, phragmoplast {ECO:0000269|PubMed:20870962}. Cell membrane {ECO:0000269|PubMed:23163883}. Secreted, cell wall {ECO:0000269|PubMed:20870962}. Note=During cytokinesis, localizes to the nascent cell plate and later to the cell plate insertion site and along the post-cytokinetic wall (PubMed:20870962). Localized at vesicle-like small compartments at cortical microtubules, especially in the presence of FPP3/VETH1, FPP2/VETH2 and COG2 (PubMed:25541219). Confined to helical/annular plasma membrane (PM) domains in protoxylem of roots before the secondary cell wall (SCW) is deposited. After the induction of xylem differentiation, first associated with plasma membrane (PM) foci and later co-localizes with microtubules (MT) organized into regular bundles, especially at the cell cortex (PubMed:27801942). {ECO:0000269|PubMed:20870962, ECO:0000269|PubMed:25541219, ECO:0000269|PubMed:27801942}.
Interaction partners:
- Exocyst complex component SEC8
- Exocyst complex component SEC6
- Exocyst complex component SEC3A
- Exocyst complex component EXO84B
- Exocyst complex component SEC10a
- Exocyst complex component SEC15B
- Exocyst complex component SEC5A
- Exocyst complex component SEC5B
- Protein ROH1A
- Exocyst complex component EXO84C
Sequence:
MAVDSRMDLLSERAVLMRASLQKSQTITDNVVSILGSFDSRLSALETAMRPTQIRTHAIRKAHENIDRTLKAAEVILSQFDLLRQAETKVLKGPHEDLESYLDAIAQLRKIIRYFMSNKSFKSSDGVLNHANSLLAKAQSKLEEEFKQLLASYSKAVEPDRLFDGLPNSLRPSSDGDGGGKPHGGHHNDDAETAAYTLPILIPSRVLPLLHDLAQQMVQAGHQQQLLQIYRDTRSFVLEESLKKLGVEKLSKEDVQRMQWEVLEAKIGNWIHFMRIAVKLLFAGERQVCDQIFRGFDSLSDQCFAEVTVSSVSMLLSFGDAIARSKRSPEKLFVLLDMYEIMRELHTEIETIFKGKACLEIRDSATGLTKRLAQTAQETFGDFEEAVEKDATKTAVLDGTVHPLTSYVINYVKFLFDYQTTLKQLFLEFGNGDDSNSQLASVTMRIMQALQNNLDGKSKQYKDPALTHLFLMNNIHYMVRSVRRSEAKDLLGDDWVQRHRRIVQQHANQYKRVAWTKILQSSSAQGLTSSGGGSLEGGNSSGVSRGLLKERFKMFNMQFDELHQRQSQWTVPDTELRESLRLAVAEVLLPAYRSFLKRFGPLVESGKNPQKYIKYTAEDLERLLGELFEGKSMNEPRR
Protein: DDB1 and CUL4 associated factor 17 (H0Y2X0)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
XRHSTTCFAVPCSVPSSTFFTCRDSRDQQKDMPPLLFEVSSLENAFQIGGHPWHYIVTPNKKKQKGVFHICALKDNSLAKNGIQEMDCCSLESDWIYFHPDASGRIIHVGPNQVKVLKLTEIENNSSQHQISEDFVILANRENHKNENVLTVTASGRVVKKSFNLLDDDPEQETFKIVDYEDELDLLSVVAVTQIDAEGKAHLDFHCNEYGTLLKSIPLVESWDVTYSHEVYFDRDLVLHIEQKPNRVFSCYVYQMICDTGEEEETINRSC
Protein: Translational repressor ifet-1 (Spindle orientation defective protein 2) (Q20898)
Organism: Caenorhabditis elegans
Function: Involved in translational repression of multiple mRNAs in the distal gonad. Recruited to the 3' untranslated region (UTR) of zif-1 by oma-1 and is required for translational repression of zif-1. May also be involved in translational repression of mei-1 through recruitment to the mei-1 3' UTR by oma-1. Required for oogenesis but not spermatogenesis, for P granule formation and for the localization of car-1 and cgh-1 to P granules. Required for normal spindle orientation in early embryos.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:19786575, ECO:0000269|PubMed:23264733}. Note=In one-cell embryos, expressed highly and diffusely throughout the cytoplasm and is associated with P granules. {ECO:0000269|PubMed:19786575, ECO:0000269|PubMed:23264733}.
Interaction partners:
- ATP-dependent RNA helicase cgh-1
- Protein LSM14 homolog car-1
- Eukaryotic translation initiation factor 4E-3
- CCCH-type zinc finger protein oma-1
- Protein lin-41
- Eukaryotic translation initiation factor 4E-2
- CCR4-NOT transcription complex subunit let-711
- Cytoplasmic polyadenylation element-binding protein 3
- Eukaryotic translation initiation factor 4E-4
- Dual specificity tyrosine-phosphorylation-regulated kinase mbk-2
Sequence:
MTSHLDDEGLHPMVSTLLGGGTLPTVPFKAYTRERMMELRTTKASMTRPENLSEDFNGEDGKFSPLKWLEHRWEIEGIKNRPMSKKIDSLCAGADENTGLSPQRRAFSSGCKAPTDDKGRDGEYERLGGHGKNWRNGSTGGADKFASRGNDFKPSFQKGNQLERGTRGAEWKKDTTRGAKFAPRREERLTSLSGSEKLPEWADGPTTMDDMIELRGFDEPKKVKNKKNPKEKKEKEAVKAPEPVECVGSRPSSTGLKTSEPIDDPAIAYSSSGGGALPATDQELAALLGCLDIQKTSRKIDGDDMAWAHKSEETAGGTSRLSRFFAKKNKSPELDAMLSSVGGGNDENVANPMLARLFGHSGGDNNASSSGAGDIKGGMRLEDLEKGMESKEPSKVSPLQDPSQQAQLLQHLQKFAKQQAESGQHIHHHRQPTPPNGGPQHQQHLHHPMVHPGMQIIADPSLLASFAQNPVILNAYVENQLQEAVNAAIRANNGQQLPPQLHEQLRMASMRNKAFLQSQTLTFVSLQQQHQNIQQHQQQQQHHQHKGRTPAMIPASVQRQLQKSSSNADQKKEKTSQSPPESNQETSDAHNQSDAMNQLKKLHMQQNYANMVQAMNSGVGWARGNGVVNGQQQHPQQQLPPNVQMLMAQHQQAQMQHLKMMMSRAQQQHMLMAKIAQMQQQQAQMANMQERQGPSHNQQQHQPVVPSELSQVGPIQTPLEKLLASVGVQGSQFTGSGDRIPSSVRPMSLEDLEKQLTAVPK
Protein: Collagen alpha-1(XVI) chain (Q8BLX7)
Organism: Mus musculus (Mouse)
Function: Involved in mediating cell attachment and inducing integrin-mediated cellular reactions, such as cell spreading and alterations in cell morphology.
Subcellular location: Secreted, extracellular space, extracellular matrix {ECO:0000250}.
Interaction partners:
- Collagen alpha-1
- Collagen alpha-2
- Collagen alpha-1
- Collagen type V alpha 3 chain
- Collagen alpha-1
- Collagen alpha-2
- Collagen alpha-2
- Collagen alpha-1
- Collagen alpha-1
- Collagen alpha-1
Sequence:
MLTSWAPGLWVLGLWATFSHGTNIGERCPTSQQEGLKLEHSSDPSTNVTGFNLIRRLNLMKTSAIKKIRNPKGPLILRLGAAPVTQPTRRVFPRGLPEEFALVLTVLLKKHTFRNTWYLFQVTDANGYPQISLEVNSQERSLELRAQGQDGDFVSCIFPVPQLFDLRWHKLMLSVAGRVASVHVDCVSASSQPLGPRQSIRPGGHVFLGLDAEQGKPVSFDLQQAHIYCDPELVLEEGCCEILPGGCPPETSKSRRDTQSNELIEINPQTEGKVYTRCFCLEEPQNSKVDAQLMGRNIQKAERGTKVHQGTGVNECPPCAHSARESNVTLGPSGLKGGKGERGLTGPSGPKGEKGARGNDCVRVSPDAPLQCVEGPKGEKGESGDLGPPGLPGPTGQKGQKGEKGDGGLKGLPGKPGRDGRPGEICVIGPKGQKGDPGFVGPEGLAGEPGPPGLPGPPGIGLPGTPGDPGGPPGPKGEKGSSGIPGKEGPGGKPGKPGVPGTKGEKGDPCEVCPTLPEGSQNFVGLPGKPGPKGEPGDPAPAWEGLGTVGLKGDRGDPGIQGMKGEKGEPCSSCSSGVGAQHLGPSPGHGLPGLPGTSGIPGPRGLKGEKGSFGDTGPAGVPGSPGPVGPAGIKGAKGEPCEPCTALSELQDGDMRVVHLPGPAGEKGEPGSPGFGLPGKQGKAGERGLKGQKGDAGNPGDPGTPGITGQPGISGEPGIRGPAGPKGEKGDGCTACPSLQGALTDVSGLPGKPGPKGEPGPEGVGHPGKPGQPGLPGVQGPPGPKGTQGEPGPPGTGAEGPQGEPGTQGLPGTQGLPGPRGPPGSAGEKGAQGSPGPKGAIGPMGPPGAGVSGPPGQKGSRGEKGEPGECSCPSRGEPIFSGMPGAPGLWMGSSSQPGPQGPPGVPGPPGPPGMPGLQGVPGHNGLPGQPGLTAELGSLPIEKHLLKSICGDCAQGQTAHPAFLLEKGEKGDQGIPGVPGFDNCARCFIERERPRAEEARGDNSEGEPGCSGSPGLPGPPGMPGQRGEEGPPGMRGSPGPPGPIGLQGERGLTGLTGDKGEPGPPGQPGYPGAMGPPGLPGIKGERGYTGPSGEKGESGPPGSEGLPGPQGPAGPRGERGPQGSSGEKGDQGFQGQPGFPGPPGPPGFPGKAGAPGPPGPQAEKGSEGIRGPSGLPGSPGPPGPPGIQGPAGLDGLDGKDGKPGLRGDPGPAGPPGLMGPPGFKGKTGHPGLPGPKGDCGKPGPPGSSGRPGAEGEPGAMGPQGRPGPPGHLGPPGQPGPPGLSTVGLKGDRGVPGERGLAGLPGQPGTPGHPGPPGEPGSDGAAGKEGPPGKQGLYGPPGPKGDPGPAGQKGQAGEKGRSGMPGGPGKSGSMGPIGPPGPAGERGHPGSPGPAGNPGLPGLPGSMGDMVNYDDIKRFIRQEIIKLFDERMAYYTSRMQFPMEVAAAPGRPGPPGKDGAPGRPGAPGSPGLPGQIGREGRQGLPGMRGLPGTKGEKGDIGVGIAGENGLPGPPGPQGPPGYGKMGATGPMGQQGIPGIPGPPGPMGQPGKAGHCNPSDCFGAMPMEQQYPPMKSMKGPFG
Protein: Vacuolar protein sorting-associated protein 33 (Q9P7V6)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Essential for vacuolar biogenesis, maturation and function. Involved in the sorting of vacuolar proteins from the Golgi apparatus and their targeting to the vacuole.
Interaction partners:
- Vacuolar membrane protein pep3
- Probable vacuolar protein sorting-associated protein 16 homolog
- Vacuolar morphogenesis protein 6
- E3 ubiquitin-protein ligase pep5
- Vacuolar protein sorting-associated protein 41
- Vacuolar protein sorting-associated protein 3
- Vacuolar protein sorting-associated protein 8
- Syntaxin pep12
- Vesicle transport v-SNARE protein vti1
- GTP-binding protein ryh1
Sequence:
MTTDVKEKATFKLLDLIDSVTGKKSLLLERDLSGILGQIVTTNTLQEHGIPQVYWFNENIPNDIEKKTIYLCRPTYENAKLVATHVRQFQRDMLRIESTVIVLPTSNILFETVLQEEGVFGELLVTEWPLHAVPLDKDLLSLELGPEKLEESLLQRSTDALIDFERTHGRFPRVSGRGPYAAKMLELLEKTYQEEATINFGKVEGEISALYDSVLLVDRSLDRITPFLTQLTYFGFLDEILGIQQMNVKLPSSLVNRNEASNTGPMKKFSLSSSSSQITKEIRDINFNCIGPYLSKIARKLSSDFEGRRQAKTVNQIRDFVSKLGSLQSEHTSLNIHTGLAETLVQHTKNNYFQKLLQLQHLLVSHADSFTQFNLLDEIIYAEAPVEEVFRVLCLASITTNGLRRKDIDHYRREITQTYGYYHLLTFQALIDAGLLRLRQSTNISLQKSLSYSTWLNTYPLVKDEVDEQNPEDIAYTYSGYGPLSVHIAYDILKGRDNEEKILKLQNMPGTYVDKWTLDQEKVMPKNLKTNVPGKRRVLVFFIGGCTYTELAAFRLLQEKEDLYEFTFMTTGMVTGSSLIRAFIPNIESLNE
Protein: Light-mediated development protein DET1 (Protein DEETIOLATED 1) (P48732)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Component of light signal transduction machinery. Involved in repression of photomorphogenesis in darkness by participating in the CDD complex, a complex probably required to regulate the activity of ubiquitin conjugating enzymes (E2s). Involved in repression of deetiolation in the developing seedling. Repression of photomorphogenesis is probably mediated by ubiquitination and subsequent degradation of photomorphogenesis-promoting factors such as HY5, HYH and LAF1. Involved in the repression of blue light responsive promoter in chloroplasts. May be required to stabilize the CDD complex. Its association with histone tail suggests a role in remodeling of chromatin. Required for the regulation of histone H2B monoubiquitination (H2Bub) over most genes by controlling the stability of the deubiquitination module (DUB module).
Subcellular location: Nucleus, nucleoplasm {ECO:0000269|PubMed:30192741}. Note=Displays a rather patchy distribution forming a punctuated pattern in the euchromatin (PubMed:30192741). Does not localize in the heterochromatic chromocenters or nucleolus (PubMed:30192741). {ECO:0000269|PubMed:30192741}.
Interaction partners:
- Cullin-4
- Constitutive photomorphogenesis protein 10
- DNA damage-binding protein 1a
- E3 ubiquitin-protein ligase COP1
- Cullin-like protein 5
- Putative cullin-like protein 4
- Protein DAMAGED DNA-BINDING 2
- DET1- and DDB1-associated protein 1
- DNA damage-binding protein 1b
- RING-box protein 1a
Sequence:
MFTSGNVTARVFERQIRTPPPGASVNRARHFYENLVPSYTLYDVESPDHCFRKFTEDGLFLISFSRNHQELIVYRPSWLTYSTTDDSTTTLPPLPRRASKFDSFFTQLYSVNLASSNELICKDFFLYHQTRRFGLFATSTAQIHDSSSPSNDAVPGVPSIDKITFVLLRLDDGVVLDERVFLHDFVNLAHNMGVFLYDDLLAILSLRYQRIHLLQIRDSGHLVDARAIGYFCREDDELFLNSSSQAMMSQDKSKQQSLSGSKEDDTGENGLRHSLSQPSGSNSFLSGVKQRLLSFIFREIWNEESDNVMRVQSLKKKFYFHFQDYVDLIIWKVQFLDRQHLLIKFGSVDGGVTRSADHHPAFFAVYNMETTDIVAFYQNSAEDLYQLFEQFSDHFTVSSSTPFMNFVTSHSNNVYALEQLKYTKNKSNSFSQFVKKMLLSLPFSCQSQSPSPYFDQSLFRFDEKLISAADRHRQSSDNPIKFISRRQPQTLKFKIKPGPECGTADGRSKKICSFLFHPHLPLAISIQQTLFMPPSVVNIHFRR
Protein: Adenylate cyclase (ATP pyrophosphate-lyase) (Adenylyl cyclase) (P94982)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- Probable transmembrane protein
- PE family protein PE17
- Phenylalanine--tRNA ligase alpha subunit
- Phenylalanine--tRNA ligase beta subunit
- Probable conserved transmembrane protein
Sequence:
MAGSARTTYPCHVEVGPQDSESGAPDETATAMASPVPRQRSALRWLRTVNRSPGLVSFIHRARRLLPGDPEFGDPLSTAGEGGPRAAARAADRLLRDRDAASREVGLSVLQVWQALTEAVSRRPANPEVTLVFTDLVGFSTWSLHAGDDATLTLLRQVARAVESPLLDAGGHIVKRLGDGIMAVFRNPTVALRAVLVAQDAVKSLEVQGYTPRMRIGIHTGRPQRLAADWLGVDVNIAARVMERATKGGIMISQPTLDLIPQSELDALGVVARRVRKPVFASKPTGIPPDLAIYRIKTVSESTAADNFDEMSPDAQ
Protein: Putative nucleoside transporter YegT (P76417)
Organism: Escherichia coli (strain K12)
Function: Could be involved in nucleoside transport.
Subcellular location: Cell inner membrane; Multi-pass membrane protein.
Interaction partners:
- Uncharacterized protein YegU
- Uncharacterized sugar kinase YegV
Sequence:
MKTTAKLSFMMFVEWFIWGAWFVPLWLWLSKSGFSAGEIGWSYACTAIAAILSPILVGSITDRFFSAQKVLAVLMFAGALLMYFAAQQTTFAGFFPLLLAYSLTYMPTIALTNSIAFANVPDVERDFPRIRVMGTIGWIASGLACGFLPQILGYADISPTNIPLLITAGSSALLGVFAFFLPDTPPKSTGKMDIKVMLGLDALILLRDKNFLVFFFCSFLFAMPLAFYYIFANGYLTEVGMKNATGWMTLGQFSEIFFMLALPFFTKRFGIKKVLLLGLVTAAIRYGFFIYGSADEYFTYALLFLGILLHGVSYDFYYVTAYIYVDKKAPVHMRTAAQGLITLCCQGFGSLLGYRLGGVMMEKMFAYQEPVNGLTFNWSGMWTFGAVMIAIIAVLFMIFFRESDNEITAIKVDDRDIALTQGEVK
Protein: Sulfhydryl oxidase (EC 1.8.3.2) (H3BQQ4)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MNSLSVGLLPQRDTKFREDCPPDREELGRHSWAVLHTLAAYYPDLPTPEQQQDMAQFIHLFSKFYPCEECAEDLRKRLCRNHPDTRTRACFTQWLCHLHNEVNRKLGKPDFDCSKVDERWRDGWKDGSCD
Protein: Thromboxane-A synthase (EC 4.2.1.152) (EC 5.3.99.5) (Cytochrome P450 5A1) (Hydroperoxy icosatetraenoate dehydratase) (Q53F23)
Organism: Homo sapiens (Human)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004477}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004477}.
Interaction partners:
Sequence:
MMEALGFLKLEVNGPMVTVALSVALLALLKWYSTSAFSRLEKLGLRHPKPSPFIGNLTFFRQGFWESQMELRKLYGPLCGYYLGRRMFIVISEPDMIKQVLVENFSNFTNRMASGLEFKSVADSVLFLRDKRWEEVRGALMSAFSPEKLNEMVPLISQACDLLLAHLKRYAESGDAFDIQRCYCNYTTDVVASVAFGTPVDSWQAPEDPFVKHCKRFFEFCIPRPILVLLLSFPSIMVPLARILPNKNRDELNGFFNKLIRNVIALRDQQAAEERRRDFLQMVLDARHSASPMGVQDFDIVRDVFSSTGCKPNPSRQHQPSPMARPLTVDEIVGQAFIFLIAGYEIITNTLSFATYLLATNPDCQEKLLREVDVFKEKHMAPEFCSLEEGLPYLDMVIAETLRMYPPAFRFTREAAQDCEVLGQRIPAGAVLEMAVGALHHDPEHWPSPETFNPERFTAEARQQHRPFTYLPFGAGPRSCLGVRLGLLEVKLTLLHVLHKFRFQACPETQVPLQLESKSALGPKNGVYIKIVSR
Protein: Alpha-ketoglutarate-dependent dioxygenase alkB homolog 7, mitochondrial (EC 1.14.11.-) (Alkylated DNA repair protein alkB homolog 7) (Q9D6Z0)
Organism: Mus musculus (Mouse)
Function: May function as protein hydroxylase; can catalyze auto-hydroxylation at Leu-110 (in vitro), but this activity may be due to the absence of the true substrate. Required to induce programmed necrosis in response to DNA damage caused by cytotoxic alkylating agents. Acts by triggering the collapse of mitochondrial membrane potential and loss of mitochondrial function that leads to energy depletion and cell death. ALKBH7-mediated necrosis is probably required to prevent the accumulation of cells with DNA damage. Does not display DNA demethylase activity (By similarity). Involved in fatty acid metabolism.
Subcellular location: Mitochondrion matrix {ECO:0000269|PubMed:23572141}.
Interaction partners:
- Probable RNA/DNA demethylase ALKBH6
- Alpha-ketoglutarate-dependent dioxygenase alkB homolog 4
- tRNA
- Nucleic acid dioxygenase ALKBH1
- DNA oxidative demethylase ALKBH2
Sequence:
MAGSRRLAMRLLSGCAWVRGSDSAVLGRLRDEAVVHPGFLSQEEEDTLTRELEPQLRRRRYEYDHWDAAIHGFRETEKSCWSDASQVILQRVRAAAFGPDQSLLSPVHVLDLEPRGYIKPHVDSVKFCGSTIAGLSLLSPSVMKLVHTQEPEQWLELLLEPGSLYILRGSARYDFSHEILRDEESFFGEHRVPRGRRISVICRSLPEGMGPGRPEEPPPAC
Protein: Matrilin 3 (F1MD94)
Organism: Bos taurus (Bovine)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
- Cartilage oligomeric matrix protein
- Aggrecan core protein
- Collagen type IX alpha 3 chain
- Protein disulfide isomerase CRELD2
- Collagen type IX alpha 1 chain
Sequence:
MPRHLPGLLLLLWPLLLLPPPPAAPSPMARPGLRRLGTRGPGGSPGRRGPAPAAPASVPYSGTGQPGGARGAGVCKSRPLDLVFIIDSSRSVRPLQFTKVKTFVSKIIDTLDIGPMDTRVAVVNYASTVKIEFHLQTHSDKQSLKRAVARITPLSTGTMSGLAIQTAMDEAFTVEAGARGPSSNIPKVAIIVTDGRPQDQVNEVAARARASGIELYAVGVDRADMESLKMMASEPLDEHVFYVETYGVIEKLSSRFQETFCALDPCALGTHQCQHVCISDGEGRHHCECSQGYSLNADKKTCSAIDKCALNTHGCEHICVNDRTGSYHCECYEGYTLNEDRKTCSAQDQCALGTHGCQHICVNDRAGSHHCECYEGYTLNEDKKTCSVLNQCALGSHGCQHICVYDGNASYHCDCDTGYTLNEDKKTCSAIEEARRLISTEDACACEATLAFQDKVNSYLQRLNSKLDDILEKLQANEYGQVHR
Protein: Hemocyanin subunit C (Q8T115)
Organism: Scutigera coleoptrata (House centipede)
Function: Hemocyanins are copper-containing oxygen carriers occurring freely dissolved in the hemolymph of many mollusks and arthropods.
Subcellular location: Secreted, extracellular space {ECO:0000269|PubMed:12823556}.
Interaction partners:
Sequence:
MGAWKVWTFFAIALVVAVKAYDEEAKCMSHDEDSQVKERQILHIVDSINKPISPDFRAPRGVIDEHKLRGLGTLKKREIFSLFDERNWDEASKVVRLLLDAKDFDDFIDVAEVIRLRVNEELFLYAFSVAVMHRGDTQGLQVPRIHDIFPDKFLKEDVIHRLLELSNRGEHYDRIPIIDATQISHNYLDPNSELEYFLEDLGLNSHHHHWHVIHPAIWVSELGNEKDRKGEFFYWMHHQMLARYEAERMSNGLARTRTFQNWNDPIDEGYAPHISIMKTGYTYAYRPPGYTLRDLPNLPKNKMVEWAKRVLYSIHSGIFHFSNGTDAHLDTEHGIDELGNIVESSLTSLNRDYYGNLHCYAHVIAGRIADPEGKYGEDNGVMYDVATSARDPLFYRWHKYIDNIFQEYKNTLPPYTTEELTPQNSEFRVQGISVVGETSARDTVHTYWQHSLLKVGQGFEFTKHTPAYVKVKHLQHESFTYVIDVENRGRTRTGFFRIFAAPKYNELGQKWHINDQRLIMVEMDKFIEKLYPGKNTIERHSEDSTVTMSSASIFSDISSEQSEDHCSCGWPDYLLVPKGNFEGFPMEVFVIVTDYEEDKVEGPDEGCACHDALTYCGGIDYHFPDKRAMGFPFDRPIKQRNFNAFKTKNMGKVTVDVKFTGETIAPEDFHNQH
Protein: Zinc transporter ZIP13 homolog (Zinc/iron regulated transporter-related protein 99C) (Q9VAF0)
Organism: Drosophila melanogaster (Fruit fly)
Function: Involved in zinc transport and homeostasis.
Subcellular location: Basolateral cell membrane {ECO:0000269|PubMed:23322169}; Multi-pass membrane protein {ECO:0000269|PubMed:23322169}. Golgi apparatus membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Note=Also detected on intracellular membranes.
Interaction partners:
- LD23375p
- Zinc/iron regulated transporter-related protein 102B, isoform E
- Protein Malvolio
- Zinc transporter ZIP11
- Zinc/iron regulated transporter-related protein 42C.2
- Uncharacterized protein, isoform A
- Zinc transporter 63C, isoform F
Sequence:
MTTNSSFFDEHIAMIYSNLMDQYMPEYFKSFEYTPWVFSLLGSVVIGLSGIFPLIIIPTEEKMAKEGYKDPADSKLLRVLLSFAVGGLLGDVFLHLLPEAWEGDNQDPSSHPSLRSGLWVLSGILIFTIVEKIFSGYASADEENPQPKCVEIANCLLRRHGGQLPEGETSESCGGACDIEDVGKVCFLREQEQKSKERKEQPKKVAGYLNLLANSIDNFTHGLAVAGSFLVSFRHGILATFAILLHEIPHEVGDFAILLRSGFSRWDAARAQLLTAGAGLLGALVAIGGSGVTSAMEARTSWIMPFTAGGFLHIALVTVLPDLLKEEERKESIKQLLALVFGIALMAVMTMLFEH
Protein: Endoribonuclease MazF6 (EC 3.1.27.-) (Toxin MazF6) (mRNA interferase MazF-mt3) (P9WII3)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Toxic component of a type II toxin-antitoxin (TA) system. Upon expression in E.coli and in M.smegmatis partially inhibits cell growth and colony formation; its toxic effect is neutralized by coexpression with cognate antitoxin MazE6. Acts as an mRNA interferase on ssRNA, cleaving between the second and third bases in the sequences CUCCU and UUCCU. Further experiments demonstrate that it digests between the first and second bases of UCCUU, yielding a 5'-hydroxyl end; digests M.tuberculosis mRNA (in coding as well as the 5'- and 3'-UTR regions) and 23S rRNA, digests E.coli 16S rRNA both alone and in the 70S ribosome but no data for M.tuberculosis 16S rRNA cleavage was presented. 23S and 16S rRNA digestion occurs in predicted single-stranded regions, the 16S rRNA UCCUU site is in the anti-Shine-Dalgarno site and would cleave off the last 7 nucleotides. Non-cognate antitoxins VapB27 and VapB40 partially neutralize toxicity in vivo.
Subcellular location: Secreted. Note=Following 6 weeks of nutrient starvation. {ECO:0000269|PubMed:23345537}.
Interaction partners:
- Antitoxin MazE6
- Endoribonuclease MazF3
- Endoribonuclease MazF4
- Antitoxin MazE9
- Antitoxin MazE3
- Antitoxin MazE7
Sequence:
MVISRAEIYWADLGPPSGSQPAKRRPVLVIQSDPYNASRLATVIAAVITSNTALAAMPGNVFLPATTTRLPRDSVVNVTAIVTLNKTDLTDRVGEVPASLMHEVDRGLRRVLDL
Protein: Flagellar secretion chaperone FliS (O25448)
Organism: Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori)
Subcellular location: Cytoplasm, cytosol {ECO:0000256|ARBA:ARBA00004514, ECO:0000256|PIRNR:PIRNR039090}.
Interaction partners:
- Flagellin B
- Flagellin B homolog
- Flagellin A
- Flagellar biosynthesis protein FlhA
- Uncharacterized protein
- Flagellar hook-associated protein 1
- Flagellar hook-associated protein 2
- Flagellar basal body rod protein FlgB
- Flagellar motor switch protein FliN
- Flagellar basal-body rod protein FlgC
Sequence:
MQYANAYQAYQHNRVSVESPAKLIEMLYEGILRFSSQAKRCIENEDIEKKIYYINRVTDIFTELLNILDYEKGGEVAVYLTGLYTHQIKVLTQANVENDASKIDLVLNVARGLLEAWREIHSDELA