wanglab/gogpt-training-data huggingface dataset:
Protein: Beta-1,3-xylanase (EC 3.2.1.32) (Q8RS40)
Organism: Alcaligenes sp
Function: Catalyzes the hydrolysis of beta-1,3-xylan into oligosaccharides, mainly xylotriose and xylobiose with smaller amounts of xylotetraose, xylose, xylopentaose and xylohexaose. Does not hydrolyze xylobiose, p-nitrophenyl-beta-xyloside, beta-1,4-xylan, carboxymethylcellulose, curdlan, glucomannan or beta-1,4-mannan.
Interaction partners:
Sequence:
MKKLAKMISIATLGACAFSAHALDGKLVPNEGVLVSVGQDVDSVNDYSSAMSTTPAGVTNYVGIVNLDGLASNADAGAGRNNVVELANLYPTSALIVGVSMNGQIQNVAQGQYNANIDTLIQTLGELDRPVYLRWAYEVDGPWNGHNTEDLKQSFRNVYQRIRELGYGDNISMIWQVASYCPTAPGQLSSWWPGDDVVDWVGLSYFAPQDCNWDRVNEAAQWARSHNKPLFINESSPQRYQLADRTYSSDPAKGTNRQSKTEQQIWSEWFAPYFQFMEDNKDILKGFTYINADWDSQWRWAAPYNEGYWGDSRVQVLPYIKQQWQDTLENPKFINHSSDLFAKLGYVADGGDNGGDNGGDNGGDNGGDNGGDNGGTEPPENCQDDFNFNYVSDQEIEVYHVDKGWSAGWNYVCLNDYCLPGNKSNGAFRKTFNAVLGQDYKLTFKVEDRYGQGQQILDRNITFTTQVCN
Protein: Phosphatidylinositol 4-kinase beta (EC 2.7.1.67) (A0A0B4J1S8)
Organism: Homo sapiens (Human)
Subcellular location: Mitochondrion outer membrane {ECO:0000256|ARBA:ARBA00004450}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004450}. Rough endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00037860}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00037860}.
Interaction partners:
Sequence:
MRFLEARSLAVAMGDTVVEPAPLKPTSEPTSGPPGNNGGSLLSVITEGVGELSVIDPEVAQKACQEVLEKVKLLHGGVAVSSRGTPLELVNGDGVDSEIRCLDDPPAQIREEEDEMGAAVASGTAKGARRRRQNNSAKQSWLLRLFESKLFDISMAISYLYNSKEPGVQAYIGNRLFCFRNEDVDFYLPQLLNMYIHMDEDVGDAIKPYIVHRCRQSINFSLQCALLLGAYSSDMHISTQRHSRGTKLRKLILSDELKPAHRKRELPSLSPAPDTGLSPSKRTHQRSKSDATASISLSSNLKRTASNPKVENEDEELSSSTESIDNSFSSPVRLAPEREFIKSLMAIGKRLATLPTKEQKTQRLISELSLLNHKLPARVWLPTAGFDHHVVRVPHTQAVVLNSKDKAPYLIYVEVLECENFDTTSVPARIPENRIRSTRSVENLPECGITHEQRAGSFSTVPNYDNDDEAWSVDDIGELQVELPEVHTNSCDNISQFSVDSITSQESKEPVFIAAGDIRRRLSEQLAHTPTAFKRDPEDPSAVALKEPWQEKVRRIREGSPYGHLPNWRLLSVIVKCGDDLRQELLAFQVLKQLQSIWEQERVPLWIKPYKILVISADSGMIEPVVNAVSIHQVKKQSQLSLLDYFLQEHGSYTTEAFLSAQRNFVQSCAGYCLVCYLLQVKDRHNGNILLDAEGHIIHIDFGFILSSSPRNLGFETSAFKLTTEFVDVMGGLDGDMFNYYKMLMLQGLIAARKHMDKVVQIVEIMQQGSQLPCFHGSSTIRNLKERFHMSMTEEQLQLLVEQMVDGSMRSITTKLYDGFQYLTNGIM
Protein: Protein odd-skipped-related 1 (E1BWE8)
Organism: Gallus gallus (Chicken)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MGSKTLPAPVPIHPSLQLTNYSFLQAFNGLPAVPSDHLSNLYGFSALHAVHLHQWTLGYPAMHLPRSSFSKVPSVSSLVDARFQLPTFPLFPHVIQPKQEAANMTLKAKPRFDFANLAVAATQEDHSKLGQVDSQGSPPGLGSLLEVTKLSPEKKPTRGRLPSKTKKEFVCKFCGRHFTKSYNLLIHERTHTDERPYTCDICHKAFRRQDHLRDHRYIHSKEKPFKCQECGKGFCQSRTLAVHKTLHTQEIQRIPEDG
Protein: Nucleoporin 98-96 (Q867M7)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
SKYGLGDSDEEDELPTDPKKAKIATLEAQQRANAEKMTLNSLRQAQKISEDAARNLDPKALVAGVASGFRPMDDTAEFLLMDKTQFFQAGGNSDFSMFDPPRQRPTITSPTAVLAQEMVGNEAHKMQLMKSSFFVEDNAPEDEPMETTGRLLRHRKFFNVEPLVWKDGASESSSQYDFEHPSPALPISSSVSEASLMCDAHYEETSSMATGSIVAAVKETKFEMPVTKAFKFVCKPKVAPIKLRATTVPLPRSIAYEMRDNWIADLGFYKGRSFKLSFGPQNSLVLPSTYNNMQNLKEFTGPSLPVSMVFAPRSATDLSPSVMQLVEFNMVKGNEGFRESIIPHLEVQLNDCLSVNVEGSECPCIHPDSGTKLISKHFSESLKQRNAGLKEDYSVSVWSLLFALWGDHDELVDLEKNSHYMVMCRRNLLSEWLENTLLGKDLLSKKVSTHSYLEHMLDLLSCHRVNEACELAFSYDDANLALVLSQLSSGAVFRLLMEEQLFAWQQSKSDKYIDLERLKMYMLAAGAPMMQSSHGAINLLENKNWLTALALQLWYFTAPTSSITDALNAYNDAFQAEECYAEPPKPSYRDAPTDTKKPVYDLRYHLLQLHSKRMHSLEETLNPITHTADAMDFRLSWLLLQTLRALGYRHCSPLTEARLSVDFASQLENEGLWQWGIFVLLHIKQQTQRERAVQQMLQRNVSVSAKVALYAEERFIVEELGIPMSWVDYAKAVKAGASGKHHLQAKYLLKAKHFATAHDVIFQHIAPDAIINGKMKYLHSLLIQFEDTEGSSIRVPNWANQGQIFLDFIDISAKFKQIRSVTNIADINARWENLKPQLSELCSRISLLPCPTSKHRLCQSEISQSLSCLVHGMCIVCPEMESSTVLKVALERLPLPQEFASKELRIWLEELLDKIQNEPPFSERQQPTMMEI
Protein: Methyl-accepting chemotaxis protein Amb2333 (Q2W4T8)
Organism: Paramagnetospirillum magneticum (strain ATCC 700264 / AMB-1) (Magnetospirillum magneticum)
Function: Chemotactic-signal transducers respond to changes in the concentration of attractants and repellents in the environment, transduce a signal from the outside to the inside of the cell, and facilitate sensory adaptation through variation of methylation levels. Attractants increase the level of methylation while repellents decrease the level of methylation.
Subcellular location: Cell inner membrane {ECO:0000305|PubMed:20471399}; Multi-pass membrane protein {ECO:0000255}. Note=Found predominantly at cell poles. {ECO:0000269|PubMed:20471399}.
Interaction partners:
- Chemotaxis protein CheA
- Chemotaxis signal transduction protein
- Protein-glutamate methylesterase/protein-glutamine glutaminase 1
- protein-glutamate O-methyltransferase
- protein-glutamate O-methyltransferase
- Protein-glutamate methylesterase/protein-glutamine glutaminase 3
- Chemotaxis signal transduction protein
- Chemotaxis protein CheA
- Protein-glutamate methylesterase/protein-glutamine glutaminase 2
- protein-glutamate O-methyltransferase
Sequence:
MEGPYQRLPWGIWRMSISNWRFRAKIFLIVVLSLLGMGAIVAVNLANLHNELMAARKIKTQHVVETAHSLIGHYVKLSQSGQMSTDAAQAAAIEAIKTMRYAGTEYFWINSLAGKMVVHPIRPDMLGKDLMGLKDPAGKLFFEAMIDVVKKDKAGFVDYLWPKPGLDQPVPKVSYVKGIEEWGWLVGSGIYVDDVDSAFRAEVMNLGGIVTGVVLLVLLVSWWIGKNVVDGMRNATGGIRKLAEGDTSVEIKGHERGDEIGELVQAAEIFREHSLTMKRMSEERAEQRRQAEAERRSTLAGLATELERGVKSTVVTVSESAGRMRSTATGMAGAIDNASQESQAVAAAAQQTSSNVEAVAAAAEELSSSIRGIGSQVAESTQIAKEAVDAANRTDGVVRGLSEAADRIGEVVRLINDIAGQTNLLALNATIEAARAGEAGKGFAVVANEVKHLASQTAKATEEIGQQIASIQSTTADAVGAIESIGKTIGRMDEIANAIAEAVEQQGAATQEIARNVHEAADGAQEVSHHISSISRTASEAGVAARELLGAAAELAGESETLRNGVDRFLGEVRAM
Protein: Fos-related antigen 2 (FRA-2) (P47930)
Organism: Mus musculus (Mouse)
Function: Controls osteoclast survival and size. As a dimer with JUN, activates LIF transcription. Activates CEBPB transcription in PGE2-activated osteoblasts (By similarity).
Subcellular location: Nucleus {ECO:0000250|UniProtKB:P51145}.
Interaction partners:
- Transcription factor JunD
- Transcription factor JunB
- Transcription factor Jun
- Protein FosB
- Fos-related antigen 1
- Protein c-Fos
- Stress-activated protein kinase JNK
- Mitogen-activated protein kinase 14
- Mitogen-activated protein kinase 9
- CCAAT/enhancer-binding protein beta
Sequence:
MYQDYPGNFDTSSRGSSGSPAHAESYSSGGGGQQKFRVDMPGSGSAFIPTINAITTSQDLQWMVQPTVITSMSNPYPRSHPYSPLPGLASVPGHMALPRPGVIKTIGTTVGRRRRDEQLSPEEEEKRRIRRERNKLAAAKCRNRRRELTEKLQAETEELEEEKSGLQKEIAELQKEKEKLEFMLVAHGPVCKISPEERRSPPTSGLQSLRGTGSAVGPVVVKQEPPEEDSPSSSAGMDKTQRSVIKPISIAGGGFYGEEPLHTPIVVTSTPAITPGTSNLVFTYPNVLEQESPSSPSESCSKAHRRSSSSGDQSSDSLNSPTLLAL
Protein: Schlafen AlbA-2 domain-containing protein (Q386U9)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MFQIDVTDVYSAQTETEIARLFALAANSDFPSETPTIEVRLLLQTEKDGSQPTGDVWTRQERDTLLLCLDRSVSRVYPPLDPLQYTQPPPELEVRNGKRVARIYVTPTVRLFSFHSTPHCVEGRMGTANGTPPSLLTPFAEGEGVKASGEFEDFAVSRSRWRVAAWLTARLFNESSWVSTCPCGGLNNGDGTVAVPAERCSDVIDAAECDGQKRLLHVDVAGMEFVGLITAVTSRYAYVAVPHEEEGQLATKWVLVSRVSVPPALERIVGRETVKRPREDSERSRREEFVYEREVISHDNTPFRVLRVEERLLVTLRAHKVYCTKQRPVLGLPRAVSVLFEDVAVVKKVADSLTDGGDSTKVIHKSCCNSFADVLEIVRGSCKRFLRGYTKYKLNTNGPAVERLFSALTDTVSVQSVCHGAGTRRRRQRPPVTVSSPRDISSLYEGTCVEFKAKANKWEANSIEDFVETDVFGDASASAGGNYRSTSRKTGCMNMERIRHTIAAMASTLGGVLLVGVSDDGKVLGHSPDALKELRLTGFCPAMPKGTVQCTTMRAVSEDAPVTLPKEWWKNKTQNIGQRVNQQTNLVVTVITVSRGPAPVYTVARHSVPYIRGFASTLPLHVISVTRRITPLLP
Protein: Serine/threonine-protein kinase BRSK1 (EC 2.7.11.1) (Brain-selective kinase 1) (EC 2.7.11.26) (Brain-specific serine/threonine-protein kinase 1) (BR serine/threonine-protein kinase 1) (Serine/threonine-protein kinase SAD-B) (Synapses of Amphids Defective homolog 1) (SAD1 homolog) (hSAD1) (Q8TDC3)
Organism: Homo sapiens (Human)
Function: Serine/threonine-protein kinase that plays a key role in polarization of neurons and centrosome duplication. Phosphorylates CDC25B, CDC25C, MAPT/TAU, RIMS1, TUBG1, TUBG2 and WEE1. Following phosphorylation and activation by STK11/LKB1, acts as a key regulator of polarization of cortical neurons, probably by mediating phosphorylation of microtubule-associated proteins such as MAPT/TAU at 'Thr-529' and 'Ser-579'. Also regulates neuron polarization by mediating phosphorylation of WEE1 at 'Ser-642' in postmitotic neurons, leading to down-regulate WEE1 activity in polarized neurons. In neurons, localizes to synaptic vesicles and plays a role in neurotransmitter release, possibly by phosphorylating RIMS1. Also acts as a positive regulator of centrosome duplication by mediating phosphorylation of gamma-tubulin (TUBG1 and TUBG2) at 'Ser-131', leading to translocation of gamma-tubulin and its associated proteins to the centrosome. Involved in the UV-induced DNA damage checkpoint response, probably by inhibiting CDK1 activity through phosphorylation and activation of WEE1, and inhibition of CDC25B and CDC25C.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:15150265}. Nucleus {ECO:0000269|PubMed:15150265}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. Synapse {ECO:0000250|UniProtKB:B2DD29}. Presynaptic active zone {ECO:0000250|UniProtKB:B2DD29}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle {ECO:0000250|UniProtKB:B2DD29}. Note=Nuclear in the absence of DNA damage. Translocated to the nucleus in response to UV- or MMS-induced DNA damage (By similarity). {ECO:0000250}.
Interaction partners:
- Cerebellar degeneration-related protein 2
- Histone-lysine N-methyltransferase KMT5C
- Hsp70-binding protein 1
- M-phase inducer phosphatase 2
Sequence:
MSSGAKEGGGGSPAYHLPHPHPHPPQHAQYVGPYRLEKTLGKGQTGLVKLGVHCITGQKVAIKIVNREKLSESVLMKVEREIAILKLIEHPHVLKLHDVYENKKYLYLVLEHVSGGELFDYLVKKGRLTPKEARKFFRQIVSALDFCHSYSICHRDLKPENLLLDEKNNIRIADFGMASLQVGDSLLETSCGSPHYACPEVIKGEKYDGRRADMWSCGVILFALLVGALPFDDDNLRQLLEKVKRGVFHMPHFIPPDCQSLLRGMIEVEPEKRLSLEQIQKHPWYLGGKHEPDPCLEPAPGRRVAMRSLPSNGELDPDVLESMASLGCFRDRERLHRELRSEEENQEKMIYYLLLDRKERYPSCEDQDLPPRNDVDPPRKRVDSPMLSRHGKRRPERKSMEVLSITDAGGGGSPVPTRRALEMAQHSQRSRSVSGASTGLSSSPLSSPRSPVFSFSPEPGAGDEARGGGSPTSKTQTLPSRGPRGGGAGEQPPPPSARSTPLPGPPGSPRSSGGTPLHSPLHTPRASPTGTPGTTPPPSPGGGVGGAAWRSRLNSIRNSFLGSPRFHRRKMQVPTAEEMSSLTPESSPELAKRSWFGNFISLDKEEQIFLVLKDKPLSSIKADIVHAFLSIPSLSHSVLSQTSFRAEYKASGGPSVFQKPVRFQVDISSSEGPEPSPRRDGSGGGGIYSVTFTLISGPSRRFKRVVETIQAQLLSTHDQPSVQALADEKNGAQTRPAGAPPRSLQPPPGRPDPELSSSPRRGPPKDKKLLATNGTPLP
Protein: Nucleoside diphosphate kinase 3 (EC 2.7.4.6) (NM23 nucleoside diphosphate kinase 3) (Q9PTF3)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Mitochondrion outer membrane {ECO:0000250|UniProtKB:Q13232}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q13232}. Cytoplasm {ECO:0000250|UniProtKB:Q13232}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000250|UniProtKB:Q9WV85}.
Interaction partners:
- Inosine triphosphate pyrophosphatase
- Guanosine-3',5'-bis
- Thymidylate kinase
- Nucleoside-triphosphatase, cancer-related.
- Ribonucleoside-diphosphate reductase large subunit
- Adenylate kinase 9
- Cytidine monophosphate
- CTP synthase
- CTP synthase 1
- Deoxyuridine triphosphatase.
Sequence:
MIILCLTIFANIFKPGWTGANERTFLAVKPDGVQRRLVGEIIRRFERKGFKLVGMKLLQASEAQLRQHYWELREKPFYNGLVKYMSSGPIVAMVWQGLDVVKTARKMLGETNPADSLPGTIRGDYCVEVGRNVIHGSDSVESAAREISLWFEDHELFCYEECGQHWIYA
Protein: Succinate-semialdehyde dehydrogenase (EC 1.2.1.24) (X5DQN2)
Organism: Homo sapiens (Human)
Subcellular location: Mitochondrion {ECO:0000256|RuleBase:RU365091}.
Interaction partners:
Sequence:
MATCIWLRSCGARRLGSTFPGCRLRPRAGGLVPASGPAPGPAQLRCYAGRLAGLSAALLRTDSFVGGRWLPAAATFPVQDPASGAALGMVADCGVREARAAVRAAYEAFCRWREVSAKERSSLLRKWYNLMIQNKDDLARIITAESGKPLKEAHGEILYSAFFLEWFSEEARRVYGDIIHTPAKDRRALVLKQPIGVAAVITPWNFPSAMITRKVGAALAAGCTVVVKPAEDTPFSALALAELASQAGIPSGVYNVIPCSRKNAKEVGEAICTDPLVSKISFTGSTTTGKILLHHAANSVKRVSMELGGLAPFIVFDSANVDQAVAGAMASKFRNTGQTCVCSNQFLVQRGIHDAFVKAFAEAMKKNLRVGNGFEEGTTQGPLINEKAVEKVEKQVNDAVSKGATVVTGGKRHQLGKNFFEPTLLCNVTQDMLCTHEETFGPLAPVIKFDTEEEAIAIANAADVGLAGYFYSQDPAQIWRVAEQLEVGMVGVNEGLISSVECPFGGVKQSGLGREGSKYGIDEYLELKYVCYGGL
Protein: SMG6 protein (Q86BS8)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MSRKGTREQNDISLIIGTLPKRLQNKIAASCSHAAAAATTTKALETENAENAEPVATTANASRPVEILSNASTGGGKPDAQSKQPVLDTSGKMAWEGGIPGILRVTTSVAGDVNRNGQGQGKNKSGNSARRRGRKDKEHATQSPVTRTRLTTEHPDWFEPLLGLPHAKNIVHLYDQLMVLNQRNLILINWKNFCYIHDQLQDAFKQLLLEQLKFVCEHKVDVFFWKLLFYNVRNYLKRQQTDQAHTHTLLLIEQAIKFYRMLYDKLMAKCVASSRCDSALKVVAQRLLICLGDLTRYRVNHVKATDYMEAARYYQRAQELVPGNGAPFNQLAVISIYHHKRFDAVYYYVRSLLTSNSIQSAKESLLDLFDEIRRKYEETEMKQSPMHYAAGSKNQKSKQMRKEVWIYPDGIRRLHRTDDKGNKAKGNKATMAEVNRYEEMPPEEILPRIVSLYLYLLGKLYTGTDVDSLYPLLRKLQIQIGVALRHENLLSRSKLLKIVALNLFVVEHNKPKTSRREMRYHSFNFANSFFGLMMKKTNQLLAGFVEDSTNVQCLPEEDFATVNTYLQFVNVYVRWLSISLDVWEPVRSEEHSFIDCWAELTILFEYIECLMGKHKLEKNEILLDEDVALRGFTPLGRETLSMDYLKRGSERLQFFERVRRIGQFQEYYVQHQEALQQPLESSFTVEHLNAAMKNALENYDAESCGLAANVSKIQCKAVEELLCRSTDSDVSELCKLKKELEAKARVKQICTSKLEDILKFVDTKIYIEVRPRYLLPDTNCFIDCLEDFEKLSTEFKRYTLIIPLTVVKELDGLSKGVKLDSYRSSKQTQRIHHFDEVSSRAKKSLEFIKSAKGNVKCATTKGSFVNASVFALVEEEYLSNDDKILATAMAVSKTAKTEQCTADGKCFIQTELVLITTDRNLRVKALSRNLAVSALDEFLQWAKDCREST
Protein: Protein HIRA (cHIRA) (TUP1-like enhancer of split protein 1) (P79987)
Organism: Gallus gallus (Chicken)
Function: Cooperates with ASF1A to promote replication-independent chromatin assembly (By similarity). May regulate the transcription of a variety of genes controlling cell growth.
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- Histone chaperone ASF1
- Uncharacterized protein.
- Calcineurin binding protein 1.
- Histone-binding protein RBBP4
Sequence:
MKLLKPTWVNHNGKPIFSVDIHPDGTKFATGGQGQDSGKVVIWNMAPVLKEEDEKNENIPKMLCQMDNHLACVNCVRWSNNGVYLASGGDDKLIMVWKRAAYIGPSTVFGSSSKLTNVEQWRCVSILRSHSGDVMDVAWSPHDAWLASCSVDNTVVIWNAVKFPEILATLKGHSGLVKGLTWDPVGKYIASQADDRSLKVWRTMDWQLETSITKPFDECGGTTHVLRLSWSPDGHYLVSAHAMNNSGPTAQIIERDGWKTNMDFVGHRKAVTVVKFNPKIFKKKQKNGSSTKSSCPYCCCAVGSKDRSLSVWLTCLKRPLVVIHELFDKSIMDISWTLNGLGILVCSMDGSVAFLDFSQDELGDPLSEEEKSNIHQSTYGKSLAIMTEAQLSTTIIENPEMLKYQQRQQQQQAEQKNASIREASGAATTAPKVASMVNGESLEDIRKNLLKKQVETRTADGRRRITPLCIAQLDTGDFSTAFFNSIPISGTLAGSIMSSQNNQQLMSLDSNAANSLNTSKPSAEPTAASIKPTDDAASKDGVNATSVSTAPPASSSSVLTTPSKIEPMKAFDSRFTERSKATSGTAVVTNTNQTVVDRLKDQNLIKDNKPKDILESSSDSEEKIPAAKPLSAPKRKLELEGETVEKKKKGRPRKDSRLVPVTLTVQSPAALASEKDAACISAPALALKLPTPIPQKSFTLQVSSDPSMYLEVENEMTTVGGSKLSRLKCNREGKEWETVLTSRILTAAGSCEIVCVACEKRMLSVFSACGRRLLPPIILNTPISTLHCTGSYIMTLTTAATLSVWDVHKQTVIVRDESLQTILSGSDTTVSQILLTQHGIPVMSMSDGKAYCFNPSLSTWNLVSDKQDSLAQCADFRSSLPSQEAMLCSGPLAVIQGRTSNSGRQAARLFSMPHLVQQETTLAYLENQIAAALMLQSSHEYRHWLLIYARYLVNEGFEYRLRELCKDLLGPVHYSRGSQWESTVMGLRKRELLKELLPVIGQNLFQRLFTEYQEQLDIL
Protein: Solute carrier family 9 member C1 (Na(+)/H(+) exchanger 10) (NHE-10) (Sodium/hydrogen exchanger 10) (Solute carrier family 10 member 10) (Sperm-specific Na(+)/H(+) exchanger) (sNHE) (Q6UJY2)
Organism: Mus musculus (Mouse)
Function: Sperm-specific sodium/hydrogen exchanger involved in intracellular pH regulation of spermatozoa. Required for sperm motility and fertility. Involved in sperm cell hyperactivation, a step needed for sperm motility which is essential late in the preparation of sperm for fertilization. Required for the expression and bicarbonate regulation of the soluble adenylyl cyclase (sAC).
Subcellular location: Cell projection, cilium, flagellum membrane {ECO:0000269|PubMed:14634667}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Adenylate cyclase type 10
- Sodium/hydrogen exchanger 9B1
- Potassium channel subfamily U member 1 current)
Sequence:
MEMEEISENLTASHSIKLTNMWLELLKSVFLSTPQDLPEIILILSLICTVGAFLNMHLKDFPIPLPVILFLIGCCFEILSFASTQIQIYADAIQWMDPDIFFGIFTPVIIFNVAFDMDIYMLQKLFWQILVITIPGFLINYTLILWYLQSVNKLSLKTVPWLLFSAVLISSDPMLTSASIRDLGLSRSLTNLINGESLLTSVLSLVIYSGVVHIRFKSKSVNHTLAHKVMSTAWSYIVESFITGIVFTKVIQLWMATIFGDDVNHITLIFSVLYLIFYVCELVGMSGIFTLATIGLFLNSTSFKPGVEAFLLEFWNCLSFIGFLMVFTFIGLLIPAHTYLHISFSDVYYSLNIYFTLIVLRLLVFLLMSPILSRLGHGFSWRWAFIMVWSEMKGTPNINMALLLAYSDISLGSERERSQILFHGVSVCVITLIVNRFILPMAVTKLGLRDVTSTKYKSVYYTFQHFQELTKSTAMALKFDKDLANADWNMVDNAIILQNPYAMNQEEITEHQKVKCPDCNKEIDETLNIEAMELTNRRLLSAQIASYQRQYRNEVLSQSAVQVLVGAAGSFGEKKGEYMSPENIKNFSESKKLLSFLRKLLLNWVYNTKKDKGVPSRYMFLHACHRIVFTNEFEYTGYLVVLMSTYPMIICWISRLKDIYDNEIKCANYYFLAFYILEALLKVAAMRKEFFSHTWLLFELGITLVGVLDIILIETDSISYNFDLTETVVFMNVIRLLRILRILKLVTPKLLQIIDKRMSQQISFRYSILKGYVQGEMDVLNIIDQIASSKQTKQILLKRVMRNMEHAMKELGYLEYDHPEIAVTMKTKEEINVMLNMAREIVKAFRSKGIIHKVEGTEINKLIMAKKIQVLDLQSVIQPFNVEEAPCNIPWLSEDPEAITFIQEKAKVVTFDCGNNIFEEGDEPEGIYVIISGMVKLKRSKPHLEMERVSAESEIKIHPLPHTEYLLSGEIIGELNCLTKERMQYSATCKTVVETYFIPISHLYEGFEKRCPNMKHKMWQKIGLAITAQKIREHLSFEDWNYKLQLKLCNAFIRDIPKSMKTDIYDETVTHVVLIHGSAEDCQLRKIYKAPFLIPVTCHQIQGMEDFTKVMIIQTSIAVRKFRWNVRKYIPPRRISMKPDSERESFETLDETSEEDNGKKENQENEELIEENINI
Protein: Endo-1,4-beta-xylanase (EC 3.2.1.8) (F8WSY7)
Organism: Streptomyces sp. SWU10
Interaction partners:
Sequence:
MQQDGTQQDWTKQKRAPLDGVSRRGFLGGAGTLALATASGLLLPGTAHAATTITTNQTGTDGMYYSFWTDGGGSVSMTLNGGGSYSTQWTNCGNFVAGKGWSTGGRRTVRYNGYFNPSGNGYGCLYGWTSNPLVEYYIVDNWGSYRPTGTYKGTVSSDGGTYDIYQTTRYNAPSVEGTKTFQQYWSVRQSKVTSGSGTITTGNHFDAWARAGMNMGQFKYYMIMATEGYQSSGSSNITVSG
Protein: Protein tincar (Q86B91)
Organism: Drosophila melanogaster (Fruit fly)
Function: Involved in eye morphogenesis. May be essential for the normal differentiation of ommatidial cells.
Subcellular location: Membrane {ECO:0000269|PubMed:14516698, ECO:0000305}; Multi-pass membrane protein {ECO:0000269|PubMed:14516698, ECO:0000305}.
Interaction partners:
Sequence:
MGGKHQGSGAGASSGGGSLNSSLCNSVMTNATTASSSLTQQQQQLQAKYIKSKRHQSRYTSLQHSGHDSGSYLHLNSLWSIWYGVMLTLFQGYLAMHGAYRFLGCSLIPWKIEPVAELNLQIVLSGVVFILLPVFFTSAVFKVGNLANDGIKLATGARERRCTLSPHDGLEEESRGGTLRALWTHGGPTAAFVHIVIALCLLLPRLLLEARIIENGLLPKEQIWATELDFVVINRRNLMAMSVVGATPFPRHHQPSNQQQSHHQHGRLNLTANSLEQDEEDYFNDTMFTAIRGVPAGGNNNLFDLRPDRMANGRKAAKTTATTRTTTTANKLDAGKGQYFEVPDLINQDIDEEERQELEEAIRGEEDDGDEGVGVGEEGTVIMPDFDELAPRTAVGTSTTTAKASSDADKLNVENWQQLGTLGKADASSSSSSTTSTTTTTTTSTTTTAATTTSTRGTSTTTTTTTIKPMEITTSRQSAHHHHGKSRKHHKHHNKQRQQQPPRRHHVASHEQAILESFPEEETTTRDSSIHRVRPEVLPELPIPSTPVSASNSKIIAIKAKNQKRRISKRAAGVEIEPEYLLGDANINSSEFVAKSNEEEPEESEDFELEDGDFQAVPALTPAPPAEPNGPKSGQDYVRLDGFAGMLQLFFGIDKPIDVAIFSQPPSAEFVNLLCALLVWSVRYPAVFWNTSKAFACVFSLQMVVAALDIILGYVGISNLYKLQIYAEAMPVHQPGLILNAVVTLALYLLSTALVLASSMVMYLYGHGRLATRMRDRSIITLKTHQTWIYFAHCASLCFVLALAVVKAPLLNDLSATYKNNLHCPTFLAALVGVTHLLLWIVIWLCLTIKRRWHFKLPPLDSTYGGLLGKSSAQPLLMSSGQRTGSNSSSSGCNSTSTTVNGGDSKPDMMSTATSTELGMGMGMGIGGGINGGMGGTGMGLAAQEDIYWPKLTPSSPKLKVTFNEVTSTSDDVLLIGDQEQTDGKRHTSRGASVCFASATGEVDDGEYATLRAATAGAVVGITMGSMKRGLSNTSVGVSLLHLSEYDELPPPPPANLHHQQQQQQQQQQRQAHSFAHGHPHDYANLSGLGGISDDNISEEGKLLACVRDDSITYASTSDLEPPQPSAQAPPPPPPLPIKGAPVPQPPAVMPHSAGIYGRAPQAMPEMMQLSPEHHHNPLQHSLQHPQHHPLQQQQQKQQTPQHPLQQQGNPHQHLVSPLAPVTVAVHTNEAHIASSSTPRCLRRADSGVPNEALTPRSDTTSTTESTNTTSPPERAPSESSSGVHSGEERELEVIIRPRANSKPPPRPPQPPIQEEPYGRCTNMRMSSFNADPAATSSAVINSATLPPQRSVPEQKFDYTAHCSTMPLPVGCHSQQLAGSGNGYASTSAMTSSMGGGGMPPLPPSQVSSFMTPNSMHYANASVALGNVSGQQQPHTTLPNGVRYSNPHFLRRLPHVTKAAESPYGHLGYGAGHHAFAKLPHETHPTIPEDRDSANYSMASDQDCGLYVTAQLH
Protein: Immunoglobulin-binding protein EibC (Trimeric autotransporter adhesin EibC) (TAA EibC) (Type 5 secretion system autotransporter EibC) (Q9LA56)
Organism: Escherichia coli
Function: Binds (in a non-immune fashion) to the Fc portion of human IgG and less well to IgA; binding occurs on the cell surface. Confers the ability to survive exposure to human serum exposure. Binds to the Fc portion of human IgG and IgA and to whole mouse antibodies also via Fc.
Subcellular location: Cell surface {ECO:0000269|PubMed:22155776, ECO:0000305|PubMed:10722621, ECO:0000305|PubMed:19303642}. Cell outer membrane {ECO:0000269|PubMed:22155776, ECO:0000305|PubMed:10722621, ECO:0000305|PubMed:19303642}; Multi-pass membrane protein {ECO:0000305|PubMed:22155776}. Note=The C-terminal translocator domain is localized in the outer membrane and the passenger domain is at the cell surface. {ECO:0000269|PubMed:22155776, ECO:0000305|PubMed:10722621, ECO:0000305|PubMed:19303642}.
Interaction partners:
Sequence:
MSKKFTMTLLSSSLAGLLVMSGGVSAQEEKYTVPYAIGEGKWGNTYEVVKTGGNGNFRYEVKEKNGKKRSLFTFDSKGDVIINGSGITYTIHDGALNDFAQTAEKKKNGQSQSHRMTDSVVRDVYNKVYSLQRTKITGFSVEDGENGKVSLGSDAKASGEFSVAVGTGARADKKFATAVGSWAAADGKQSTALGVGAYAYANASTAAGTAAYVDGSAIYGTAIGNYAKVDENATEGTALGAKATVTNKNSVALGANSVTTRDNEVYIGYKTGTESDKTYGTRVLGGLSDGTRNSDAATVGQLNRKVGGVYDDVKARITVESEKQKKYTDQKTSEVNEKVEARTTVGVDSDGKLTRAEGATKTIAVNDGLVALSGRTDRIDYAVGAIDGRVTRNTQSIEKNSKAIAANTRTLQQHSARLDSQQRQINENHKEMKRAAAQSAALTGLFQPYSVGKFNATAAVGGYSDQQALAVGVGYRFNEQTAAKAGVAFSDGDASWNVGVNFEF
Protein: Delta 8-(E)-sphingolipid desaturase (EC 1.14.19.18) (Q5AEK8)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Function: Delta(8)-fatty-acid desaturase which introduces a double bond at the 8-position in the long-chain base (LCB) of ceramides. Required for the formation of the di-unsaturated sphingoid base (E,E)-sphinga-4,8-dienine during glucosylceramide (GluCer) biosynthesis.
Subcellular location: Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Ceramide glucosyltransferase
- Sphingolipid delta
- Ceramide very long chain fatty acid hydroxylase
Sequence:
MDVKRPKKIFTRSQIIDLIADGKVIVIYKNNVLNLTSWIKKHPGGDKAAYHMVGKDATDEMHAYHCDETVDTFTRFKIGEIEGPRWENLLPPIQGGIYAKGGHYGSLNNKNTSNKKTLDSKLDNDSSNSTSDLECLTTTNSCDSDISETEIANYKGIGFVPSVKPVVPQNQLVSKSNMDIVFPIIDEETKKKVIRNPKTLLNNYDNKLSQEDVMSLPALDYDSQQVLRDKYNELHQTIIDYGLYECDLWDYVREVTKIGSLFLYSLSFLKINQLFLSAVFMGMAWHQGTFIAHDAGHIGITHNYQIDNIFGMLIADWFGGLSLGWWKRNHNVHHLITNDPVHDPDIQHLPFFAVSVRLFQNVYSTYYDKILPFDKFSQFLIPLQKYLYYPILCFGRFNLYRLSWTHVLCGQGPRQGKAAWFRYFEFFGLSFFFYWFFYLLVFKTIEGGWNRFNYVMVSHITTMLVHVQITLSHFAMSTADLGVSESFPSRQVRTTMDVDCPEWLDFLHGGLQFQAIHHLFPRLPRHNLRKAQPFVIKFCEEVGLSYSIYGFGEGNEIVISRLADIGKQCSIFLDATKHYEGDLY
Protein: Stearoyl-[acyl-carrier-protein] 9-desaturase 2, chloroplastic (Stearoyl-ACP desaturase 2) (EC 1.14.19.2) (Acyl-[acyl-carrier-protein] desaturase 2) (Q9M881)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Converts stearoyl-ACP to oleoyl-ACP by introduction of a cis double bond between carbons 9 and 10 of the acyl chain (By similarity). Exhibits delta-9 palmitoyl-[acyl-carrier-protein] desaturase (PAD) activity. Involved in omega-7 monounsaturated fatty acid biosynthesis, especially in the endosperm oil.
Subcellular location: Plastid, chloroplast {ECO:0000305}.
Interaction partners:
- Oleoyl-acyl carrier protein thioesterase 2, chloroplastic
- Oleoyl-acyl carrier protein thioesterase 1, chloroplastic
- Enoyl-[acyl-carrier-protein] reductase, chloroplastic
- Palmitoyl-acyl carrier protein thioesterase, chloroplastic
- Enoyl-[acyl-carrier-protein] reductase, mitochondrial
- Transcription factor MYB115
- Transcription factor MYB118
Sequence:
MALLLNSTITVAMKQNPLVAVSFPRTTCLGSSFSPPRLLRVSCVATNPSKTSEETDKKKFRPIKEVPNQVTHTITQEKLEIFKSMENWAQENLLSYLKPVEASWQPQDFLPETNDEDRFYEQVKELRDRTKEIPDDYFVVLVGDMITEEALPTYQTTLNTLDGVKDETGGSLTPWAVWVRAWTAEENRHGDLLNKYLYLSGRVDMRHVEKTIQYLIGSGMDSKFENNPYNGFIYTSFQERATFISHGNTAKLATTYGDTTLAKICGTIAADEKRHETAYTRIVEKLFEIDPDGTVQALASMMRKRITMPAHLMHDGRDDDLFDHYAAVAQRIGVYTATDYAGILEFLLRRWEVEKLGMGLSGEGRRAQDYLCTLPQRIRRLEERANDRVKLASKSKPSVSFSWIYGREVEL
Protein: GPI-anchored wall transfer protein 1 (EC 2.3.-.-) (P47026)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Probable acetyltransferase, which acetylates the inositol ring of phosphatidylinositol during biosynthesis of GPI-anchor. Acetylation during GPI-anchor biosynthesis is not essential for the subsequent mannosylation and is usually removed soon after the attachment of GPIs to proteins.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:12714589, ECO:0000269|PubMed:14562095}; Multi-pass membrane protein {ECO:0000269|PubMed:12714589, ECO:0000269|PubMed:14562095}.
Interaction partners:
- N-acetylglucosaminyl-phosphatidylinositol de-N-acetylase
- GPI mannosyltransferase 1
- Protein PBN1
- Uncharacterized protein YJL132W
- GPI ethanolamine phosphate transferase 1
Sequence:
MSTLKQRKEDFVTGLNGGSITEINAVTSIALVTYISWNLLKNSNLMPPGISSVQYIIDFALNWVALLLSITIYASEPYLLNTLILLPCLLAFIYGKFTSSSKPSNPIYNKKKMITQRFQLEKKPYITAYRGGMLILTAIAILAVDFPIFPRRFAKVETWGTSLMDLGVGSFVFSNGIVSSRALLKNLSLKSKPSFLKNAFNALKSGGTLLFLGLLRLFFVKNLEYQEHVTEYGVHWNFFITLSLLPLVLTFIDPVTRMVPRCSIAIFISCIYEWLLLKDDRTLNFLILADRNCFFSANREGIFSFLGYCSIFLWGQNTGFYLLGNKPTLNNLYKPSTQDVVAASKKSSTWDYWTSVTPLSGLCIWSTIFLVISQLVFQYHPYSVSRRFANLPYTLWVITYNLLFLTGYCLTDKIFGNSSEYYKVAECLESINSNGLFLFLLANVSTGLVNMSMVTIDSSPLKSFLVLLAYCSFIAVISVFLYRKRIFIKL