wanglab/gogpt-training-data huggingface dataset:
Protein: PDZK1-interacting protein 1 (17 kDa membrane-associated protein) (Protein DD96) (Q13113)
Organism: Homo sapiens (Human)
Function: May play an important role in tumor biology.
Subcellular location: Apical cell membrane {ECO:0000305|PubMed:34880493, ECO:0000305|PubMed:37217492, ECO:0000305|PubMed:38057552, ECO:0000305|PubMed:8701988}; Single-pass membrane protein {ECO:0000269|PubMed:34880493, ECO:0000269|PubMed:37217492, ECO:0000269|PubMed:38057552}.
Interaction partners:
- Na
- Sodium/glucose cotransporter 1
- Sodium/glucose cotransporter 2
- Deleted in malignant brain tumors 1 protein
Sequence:
MSALSLLILGLLTAVPPASCQQGLGNLQPWMQGLIAVAVFLVLVAIAFAVNHFWCQEEPEPAHMILTVGNKADGVLVGTDGRYSSMAASFRSSEHENAYENVPEEEGKVRSTPM
Protein: SLIT and NTRK-like protein 1 (Q810C1)
Organism: Mus musculus (Mouse)
Function: It is involved in synaptogenesis and promotes excitatory synapse differentiation (By similarity). Enhances neuronal dendrite outgrowth.
Subcellular location: Membrane {ECO:0000250|UniProtKB:Q96PX8}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q96PX8}. Secreted {ECO:0000250|UniProtKB:Q96PX8}. Synapse {ECO:0000269|PubMed:27273464}.
Interaction partners:
- Receptor-type tyrosine-protein phosphatase S
- Receptor-type tyrosine-protein phosphatase delta
- Receptor-type tyrosine-protein phosphatase F
- Interleukin-1 receptor accessory protein-like 1
Sequence:
MLLWILLLETSLCFAAGNVTGDVCKEKICSCNEIEGDLHVDCEKKGFTSLQRFTAPTSQFYHLFLHGNSLTRLFPNEFANFYNAVSLHMENNGLHEIVPGAFLGLQLVKRLHINNNKIKSFRKQTFLGLDDLEYLQADFNLLRDIDPGAFQDLNKLEVLILNDNLISTLPANVFQYVPITHLDLRGNRLKTLPYEEVLEQIPGIAEILLEDNPWDCTCDLLSLKEWLENIPKNALIGRVVCEAPTRLQGKDLNETTEQDLCPLKNRVDSSLPAPPAQEETFAPGPLPTPFKTNGQDEHATPGAVPNGGTKIPGNWQLKIKPTPPIATGSARNKPPVHGLPCPGGCSCDHIPGSGLKMNCNNRNVSSLADLKPKLSNVQELFLRDNKIHSIRKSHFVDYKNLILLDLGNNNIANIENNTFKNLLDLRWLYMDSNYLDTLSREKFAGLQNLEYLNVEYNAIQLILPGTFNAMPKLRILILNNNLLRSLPVDVFAGVSLSKLSLHNNYFMYLPVAGVLDQLTSIIQIDLHGNPWECSCTIVPFKQWAERLGSEVLMSDLKCETPVNFFRKDFMLLSNEEICPQLYARISPTLTSHSKNSTGLAETGTHSNSYLDTSRVSISVLVPGLLLVFVTSAFTVVGMLVFILRNRKRSKRRDANSSASEINSLQTVCDSSYWHNGPYNADGSHRVYDCGSHSLSD
Protein: Glyceraldehyde-3-phosphate dehydrogenase (EC 1.2.1.-) (A0A348AAL1)
Organism: Bacillus anthracis
Interaction partners:
Sequence:
MTRVAINGFGRIGRMVFRQAIKESAFEIVAINASYPSETLAHLIKYDTVHGKFDGTVEAFEDHLLVDGKMIRLLNNRDPKELPWTDLGVEVVIEATGKFNSKEKAILHVEAGAKKVILTAPGKNEDVTIVVGVNEDQLDITKHTVISNASCTTNCLAPVVKVLDEQFGIENGLMTTVHAYTNDQKNIDNPHKDLRRARACGQSIIPTTTGAAKALAKVLPHLNGKLHGMALRVPTPNVSLVDLVVDVKRDVTVEAINDAFKTVANGALKGIVEFSEEPLVSIDFNTNTHSAIIDGLSTMVMGDRKVKVLAWYDNEWGYSRRVVDLVTLVVDELAKQENVQHI
Protein: CCAAT/enhancer-binding protein delta (C/EBP delta) (Transcription factor CELF) (Q03484)
Organism: Rattus norvegicus (Rat)
Function: Transcription activator that recognizes two different DNA motifs: the CCAAT homology common to many promoters and the enhanced core homology common to many enhancers. Important transcription factor regulating the expression of genes involved in immune and inflammatory responses. Transcriptional activator that enhances IL6 transcription alone and as heterodimer with CEBPB (By similarity).
Subcellular location: Nucleus {ECO:0000305|PubMed:1714459}.
Interaction partners:
- CCAAT/enhancer-binding protein beta
- KLF transcription factor 5
- Mothers against decapentaplegic homolog 4
- Cyclic AMP-responsive element-binding protein 1
- CUGBP Elav-like family member 2
- CUGBP Elav-like family member 1
- CUGBP Elav-like family member 3
- Mothers against decapentaplegic homolog 3
- Peroxisome proliferator-activated receptor gamma
Sequence:
MSAALFSLDSPARGAPWPTEPAAFYEPGRVGKPGRGPEPGDLGEPGSTTPAMYDDESAIDFSAYIDSMAAVPTLELCHDEIFADLFNSNHKAAGAGSLELLQGGPTRPPGVGSIARGPLKREPDWGDGDAPGSLLPAQVAVCAQTVVSLAAAAQPTPPTSPEPPRGSPGPSLAPGPVREKGAGKRGPDRGSPEYRQRRERNNIAVRKSRDKAKRRNQEMQQKLVELSAENEKLHQRVEQLTRDLASLRQFFKELPSPPFLPPTGTDCR
Protein: Potassium-transporting ATPase alpha chain 1 (EC 7.2.2.19) (Gastric H(+)/K(+) ATPase subunit alpha) (Proton pump) (P27112)
Organism: Oryctolagus cuniculus (Rabbit)
Function: The catalytic subunit of the gastric H(+)/K(+) ATPase pump which transports H(+) ions in exchange for K(+) ions across the apical membrane of parietal cells. Uses ATP as an energy source to pump H(+) ions to the gastric lumen while transporting K(+) ion from the lumen into the cell. Remarkably generates a million-fold proton gradient across the gastric parietal cell membrane, acidifying the gastric juice down to pH 1 (By similarity). Within a transport cycle, the transfer of a H(+) ion across the membrane is coupled to ATP hydrolysis and is associated with a transient phosphorylation that shifts the pump conformation from inward-facing (E1) to outward-facing state (E2). The release of the H(+) ion in the stomach lumen is followed by binding of K(+) ion converting the pump conformation back to the E1 state (By similarity).
Subcellular location: Apical cell membrane; Multi-pass membrane protein {ECO:0000250|UniProtKB:P20648}. Cell membrane {ECO:0000269|PubMed:10722662}; Multi-pass membrane protein {ECO:0000255}. Note=Localized in the apical canalicular membrane of parietal cells. {ECO:0000250|UniProtKB:P20648}.
Interaction partners:
- Potassium-transporting ATPase subunit beta
- inorganic diphosphatase
- Phospholysine phosphohistidine inorganic pyrophosphate phosphatase
- inorganic diphosphatase
- Potassium-transporting ATPase alpha chain 2
- Sodium/potassium-transporting ATPase subunit beta-1
- Gastrin
- Vacuolar proton pump subunit B
- V-type proton ATPase subunit a
- V-type proton ATPase proteolipid subunit
Sequence:
MGKADNYELYSVELGPGPGGDMAAKMSKKKKAGGGGGKRKEKLENMKKEMEINDHQLSVAELEQKYQTSATKGLSARLAAELLLRDGPNALRPPRGTPEYVKFARQLAGGLQCLMWVAAAICLIAFAIQASEGDLTTDDNLYLALALIAVVVVTGCFGYYQEFKSTNIIASFKNLVPQQATVIRDGDKFQINADQLVVGDLVEMKGGDRVPADIRILAAQGCKVDNSSLTGESEPQTRSPECTHESPLETRNIAFFSTMCLEGTAQGLVVNTGDRTIIGRIASLASGVENEKTPIAIEIEHFVDIIAGLAILFGATFFVVAMCIGYTFLRAMVFFMAIVVAYVPEGLLATVTVCLSLTAKRLASKNCVVKNLEAVETLGSTSVICSDKTGTLTQNRMTVSHLWFDNHIHTADTTEDQSGQTFDQSSETWRALCRVLTLCNRAAFKSGQDAVPVPKRIVIGDASETALLKFSELTLGNAMGYRDRFPKVCEIPFNSTNKFQLSIHTLEDPRDPRHLLVMKGAPERVLERCSSILIKGQELPLDEQWREAFQTAYLSLGGLGERVLGFCHLYLSEKDYPPGYAFDVEAMNFPSSGLCFAGLVSMIDPPRATVPDAVLKCRTAGIRVIMVTGDHPITAKAIAASVGIISEGSETVEDIAARLRVPVDQVNRKDARACVINGMQLKDMDPSELVEALRTHPEMVFARTSPQQKLVIVESCQRLGAIVAVTGDGVNDSPALKKADIGVAMGIAGSDAAKNAADMILLDDNFASIVTGVEQGRLIFDNLKKSIAYTLTKNIPELTPYLIYITVSVPLPLGCITILFIELCTDIFPSVSLAYEKAESDIMHLRPRNPKRDRLVNEPLAAYSYFQIGAIQSFAGFTDYFTAMAQEGWFPLLCVGLRPQWEDHHLQDLQDSYGQEWTFGQRLYQQYTCYTVFFISIEMCQIADVLIRKTRRLSAFQQGFFRNRILVIAIVFQVCIGCFLCYCPGMPNIFNFMPIRFQWWLVPMPFGLLIFVYDEIRKLGVRCCPGSWWDQELYY
Protein: 2-oxoisovalerate dehydrogenase subunit beta 2, mitochondrial (EC 1.2.4.4) (Branched-chain alpha-keto acid dehydrogenase E1 component beta chain) (BCKDE1B) (BCKDH E1-beta) (Protein DARK INDUCIBLE 4) (Q9LDY2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: The branched-chain alpha-keto dehydrogenase complex catalyzes the overall conversion of alpha-keto acids to acyl-CoA and CO(2). It contains multiple copies of three enzymatic components: branched-chain alpha-keto acid decarboxylase (E1), lipoamide acyltransferase (E2) and lipoamide dehydrogenase (E3) (By similarity). Required during sugar starvation and acts under the control of a sugar-sensing mechanism involving Ser/Thr kinases and phosphatases.
Subcellular location: Mitochondrion matrix {ECO:0000250|UniProtKB:P21953}.
Interaction partners:
- 2-oxoisovalerate dehydrogenase subunit alpha 1, mitochondrial
- Lipoamide acyltransferase component of branched-chain alpha-keto acid dehydrogenase complex, mitochondrial
- 2-oxoisovalerate dehydrogenase subunit alpha 2, mitochondrial
- Putative 2-dehydropantoate 2-reductase
- Dihydrolipoyl dehydrogenase 2, mitochondrial
- Dihydrolipoyl dehydrogenase 1, chloroplastic
- Dihydrolipoyl dehydrogenase 2, chloroplastic
- Dihydrolipoyl dehydrogenase 1, mitochondrial
- Pyruvate dehydrogenase E1 component subunit alpha-3, chloroplastic
- Pyruvate dehydrogenase E1 component subunit alpha-1, mitochondrial
Sequence:
MAAALVRRFCRGSSFPVSGHGYRMLSTVENVSESGKSMNLYSAINQALHIALETDPRSYVFGEDVGFGGVFRCTTGLAERFGKSRVFNTPLCEQGIVGFGIGLAAMGNRVIAEIQFADYIFPAFDQIVNEAAKFRYRSGNQFNCGGLTIRAPYGAVGHGGHYHSQSPEAFFCHVPGIKVVIPRSPREAKGLLLSSIRDPNPVVFFEPKWLYRQAVEDVPEDDYMIPLSEAEVMREGSDITLVGWGAQLTIMEQACLDAENEGISCELIDLKTLIPWDKEIVETSVRKTGRLLISHEAPVTGGFGAEIAATIVERCFLRLEAPVSRVCGLDTPFPLVFEPFYMPTKNKILDAIRSTVNY
Protein: Phospholipid-transporting ATPase 11C (EC 7.6.2.1) (ATPase class VI type 11C) (P4-ATPase flippase complex alpha subunit ATP11C) (Q9QZW0)
Organism: Mus musculus (Mouse)
Function: Catalytic component of a P4-ATPase flippase complex which catalyzes the hydrolysis of ATP coupled to the transport of aminophospholipids, phosphatidylserines (PS) and phosphatidylethanolamines (PE), from the outer to the inner leaflet of the plasma membrane. Major PS-flippase in immune cell subsets. In erythrocyte plasma membrane, it is required to maintain PS in the inner leaflet preventing its exposure on the surface. This asymmetric distribution is critical for the survival of erythrocytes in circulation since externalized PS is a phagocytic signal for erythrocyte clearance by splenic macrophages. Required for B cell differentiation past the pro-B cell stage. Seems to mediate PS flipping in pro-B cells. May be involved in the transport of cholestatic bile acids.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q8NB49}; Multi-pass membrane protein {ECO:0000255}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q8NB49}; Multi-pass membrane protein {ECO:0000255}. Early endosome membrane {ECO:0000250|UniProtKB:Q8NB49}; Multi-pass membrane protein {ECO:0000255}. Recycling endosome membrane {ECO:0000250|UniProtKB:Q8NB49}; Multi-pass membrane protein {ECO:0000255}. Note=Efficient exit from the endoplasmic reticulum requires the presence of TMEM30A. Internalized via clathrin-dependent endocytosis in response to ca(2+) signaling induced by G-protein coupled serotonin and histamine receptors, HTR2A and HRH1 respectively. {ECO:0000250|UniProtKB:Q8NB49}.
Interaction partners:
- Cell cycle control protein 50A
- Cell cycle control protein 50B
- Cell cycle control protein 50C
- XK-related protein 8
- Phospholipid-transporting ATPase IA
- Phospholipid-transporting ATPase IB
- Phospholipid-transporting ATPase IC
- Phospholipid-transporting ATPase
- Phospholipid-transporting ATPase VB
- Phospholipid-transporting ATPase VA
Sequence:
MFRRTLNRLCAGEEKRVGTRTVFVGNHPISGTEPYIAQRFCDNRIVSSKYTLWNFLPKNLFEQFRRIANFYFLIIFLVQVTVDTPTSPVTSGLPLFFVITVTAIKQGYEDWLRHRADNEVNKSAVYIIENAKRVRKESEKIKVGDVVEVQANETFPCDLILLSSCTTDGTCYVTTASLDGESNCKTHYAVRDTIALCTAESIDNLRATIECEQPQPDLYRFVGRISIYSNSIEAVARSLGPENLLLKGATLKNTKKIYGVAVYTGMETKMALNYQGKSQKCSAVEKSINAFLIVYLFILLTKAAVCTTLKYVWQSSPYNDEPWYNQKTQKERETFQVLKMFTDFLSFMVLFNFIIPVSMYVTVEMQKFLGSFFISWDKDFFDEEINEGALVNTSDLNEELGQVDYVFTDKTGTLTENSMEFIECCIDGHKYKGTTQEVDGLSQTDGPLAYFDKADKNREALFLRALCLCHTVEMKTNDDVDGPVEGAGFTYISSSPDEIALVKGAKRFGFTFLGNQNGYIRVENQRKEIEEYELLHTLNFDSVRRRMSVIVRTQKGDILLFCKGADSSIFPRVHSHQIELTKDHVERNAMDGYRTLCVAFKEIPPDDFERINAQLVEAKMALQDREEKLEKVFDEIETNMNLIGATAVEDKLQDQAAETIEALHAAGLKVWVLTGDKMETAKSTCYACRLFQTNTELLELTTKTIEESERKEDRLHELLIEYRKKLLHEFPKSTRSLKKAWTEHQEYGLIIDGSTLSLILNSSQDCSSNNYKSIFLQICMKCTAVLCCRMAPLQKAQIVRMVKNLKGSPITLSIGDGANDVSMILESHVGIGIKGKEGRQAARNSDYSVPKFKHLKKLLLVHGHLYYVRIAHLVQYFFYKNLCFILPQFLYQFFCGFSQQPLYDAAYLTMYNICFTSLPILAYSLLEQHINIDTLTADPRLYMKITGNAMLQLGPFLHWTFLAAFEGTVFFFGTYFLFQTSSLEDNGKIYGNWTFGTIVFTVLVFTVTLKLALDTRFWTWINHFVIWGSLAFYVFFSFFWGGIIWPFLKQQRMYFVFAQMLCSVSTWLAIILLIFISLFPEILLIVVKNVRRRSARRNLSCRRASDSLSARPSVRPLLLRTFSDESNIL
Protein: F19P19.27 protein (Thioesterase superfamily protein) (P93828)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Zinc finger CCCH domain-containing protein 33
- Malonyl-CoA decarboxylase family protein
- GPI mannosyltransferase 1
- At2g44010
- AT4g26130/F20B18_240
- At5g11810
- ARM repeat superfamily protein
- At5g26800
- 2-carboxy-1,4-naphthoquinone phytyltransferase, chloroplastic
Sequence:
MDLESVKKYLEGDEDEKAKEPMVAKLPHRFLERFVTNGLKVDLIEPGRIVCSMKIPPHLLNAGKFLHGGATATLVDLIGSAVIYTAGASHSGVSVEINVSYLDAAFLDEEIEIESKALRVGKAVAVVSVELRKKTTGKIIAQGRHTKYFAPRSNL
Protein: Anti-sigma-F factor RsbW (Anti-sigma-F factor UsfX) (Regulator of SigF) (Sigma-F anti-sigma factor RsbW) (P9WGX7)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: A cognate anti-sigma factor for alternative sigma factor SigF. Alternative sigma factors are held in an inactive form by an anti-sigma factor. Binds ATP and GTP, may hydrolyze both.
Interaction partners:
- RNA polymerase sigma factor SigF
- Multidomain regulatory protein Rv1364c
- Anti-sigma-F factor antagonist RsfB
- Anti-sigma-F factor antagonist RsfA
- Anti-sigma factor antagonist
- Putative anti-anti-sigma factor Rv2638
- Protein USFY
- Uncharacterized protein Rv1354c
- Osmosensory protein A
- FO synthase
Sequence:
MTDQLEDQTQGGSTVDRSLPGGCMADSDLPTKGRQRGVRAVELNVAARLENLALLRTLVGAIGTFEDLDFDAVADLRLAVDEVCTRLIRSALPDATLRLVVDPRKDEVVVEASAACDTHDVVAPGSFSWHVLTALADDVQTFHDGRQPDVAGSVFGITLTARRAASSR
Protein: Zinc finger protein 169 (Q14929)
Organism: Homo sapiens (Human)
Function: May be involved in transcriptional regulation.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Argininosuccinate synthase
Sequence:
MSPGLLTTRKEALMAFRDVAVAFTQKEWKLLSSAQRTLYREVMLENYSHLVSLGIAFSKPKLIEQLEQGDEPWREENEHLLDLCPEPRTEFQPSFPHLVAFSSSQLLRQYALSGHPTQIFPSSSAGGDFQLEAPRCSSEKGESGETEGPDSSLRKRPSRISRTFFSPHQGDPVEWVEGNREGGTDLRLAQRMSLGGSDTMLKGADTSESGAVIRGNYRLGLSKKSSLFSHQKHHVCPECGRGFCQRSDLIKHQRTHTGEKPYLCPECGRRFSQKASLSIHQRKHSGEKPYVCRECGRHFRYTSSLTNHKRIHSGERPFVCQECGRGFRQKIALLLHQRTHLEEKPFVCPECGRGFCQKASLLQHQSSHTGERPFLCLECGRSFRQQSLLLSHQVTHSGEKPYVCAECGHSFRQKVTLIRHQRTHTGEKPYLCPQCGRGFSQKVTLIGHQRTHTGEKPYLCPDCGRGFGQKVTLIRHQRTHTGEKPYLCPKCGRAFGFKSLLTRHQRTHSEEELYVDRVCGQGLGQKSHLISDQRTHSGEKPCICDECGRGFGFKSALIRHQRTHSGEKPYVCRECGRGFSQKSHLHRHRRTKSGHQLLPQEVF
Protein: RNA helicase (EC 3.6.4.13) (Q05BE5)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MPEEAGFPPAKRFRPGSGPPSRAGSFPPGRQVVMLLTAGSGGRGGGGGRRQQPPLAQPSASPYPEAVELQRRSLPIFQARGQLLAQLRNLDNAVLIGSPFFTGHPGVPHWAGGDRSHEQDVPRHCKAPPRRLPCDAGPSSVRLPALCTAAPSLPRGPKDSGLEVLAVQRVSKTQAWQRTGRAGREDSGICYRLYTEDEFEKFDKMTVPEIQRCNLASVMLQLLAMKVPNVLTFDFMSKPSPDHIQAAIAQLDLLGALEHKDDQLTLTPMGRKMAAFPLEPKFAKTILMSPKFHCTEEILTIVSLLSVDSVLHNPPSRREEVQGVRKKFISSEGDHMTLLNIYRTFKNLGGNKDWCKENFVNSKNMTLVAEVRAQLRDICLKMSMPIASSRGDVESVRRCLAHSLFMSTAELQPDGTYATTDTHQPVAIHPSSVLFHCKPACVVYTELLYTNKCYMRDLCVIDAQWLYEAAPEYFRRKLRTARN
Protein: UDP-glycosyltransferase 76B1 (EC 2.4.1.-) (Q9C768)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Glycosylates the amino acid-related molecules isoleucic acid (2-hydroxy-3-methylpentanoic acid) and valic acid (2-hydroxy-3-methylbutyric acid). Acts as a negative regulator of salicylic acid (SA)-dependent plant defense in the absence of pathogens and promotes the jasmonate (JA) response. Negatively influences the onset of senescence.
Interaction partners:
- Probable flavin-containing monooxygenase 1
- Aminotransferase ALD1, chloroplastic
- Protein SAR DEFICIENT 4
- Uncharacterized protein At1g15430
- Proline iminopeptidase
- At2g35730
- Cytochrome P450 71B19
- Immune-associated nucleotide-binding protein 4
- F-box protein At3g17710
- Plant intracellular Ras-group-related LRR protein 7
Sequence:
METRETKPVIFLFPFPLQGHLNPMFQLANIFFNRGFSITVIHTEFNSPNSSNFPHFTFVSIPDSLSEPESYPDVIEILHDLNSKCVAPFGDCLKKLISEEPTAACVIVDALWYFTHDLTEKFNFPRIVLRTVNLSAFVAFSKFHVLREKGYLSLQETKADSPVPELPYLRMKDLPWFQTEDPRSGDKLQIGVMKSLKSSSGIIFNAIEDLETDQLDEARIEFPVPLFCIGPFHRYVSASSSSLLAHDMTCLSWLDKQATNSVIYASLGSIASIDESEFLEIAWGLRNSNQPFLWVVRPGLIHGKEWIEILPKGFIENLEGRGKIVKWAPQPEVLAHRATGGFLTHCGWNSTLEGICEAIPMICRPSFGDQRVNARYINDVWKIGLHLENKVERLVIENAVRTLMTSSEGEEIRKRIMPMKETVEQCLKLGGSSFRNLENLIAYILSF
Protein: AT5g43680/MQO24_4 (Q94AZ7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MLGLSYGELLLIVGATAALVGPKDLPIIARAGGRLFGRAIGYINMARGHLDGVMKQPQMQEISKEVQDLRAQVDAISHGARFSLFDSSPLTRRVDNQKTQEPSPSTTNGIVTSVNVEEKQKPVDHYTKAQEFSGSSSASVNLHAQATSFARLSETVNGKTHSLNSDSPVLPVSAEMAKLLPQRKESARGSDLMLEAVLEAEVAHKAKSFFAQAEKETPALKGKFFSDRKGEN
Protein: Cytochrome P450 81F1 (EC 1.14.-.-) (O65790)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in indole glucosinolate biosynthesis. Catalyzes hydroxylation reactions of the glucosinolate indole ring. Converts indol-3-yl-methylglucosinolate (I3M) to 4-hydroxy-indol-3-yl-methylglucosinolate (4OH-I3M) and/or 1-hydroxy-indol-3-yl-methylglucosinolate (1OH-I3M) intermediates. These hydroxy intermediates are converted to 4-methoxy-indol-3-yl-methylglucosinolate (4MO-I3M) and 1-methoxy-indol-3-yl-methylglucosinolate (1MO-I3M) by indole glucosinolate methyltransferase 1 and 2 (IGMT1 and IGMT2).
Subcellular location: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
- Indole glucosinolate O-methyltransferase 1
- Probable 2-oxoacid dependent dioxygenase
- Probable inactive 2-oxoglutarate-dependent dioxygenase AOP2
- Indole glucosinolate O-methyltransferase 2
- Cytosolic sulfotransferase 16
- Transcription factor MYB28
- Flavin-containing monooxygenase FMO GS-OX2
- Flavin-containing monooxygenase FMO GS-OX5
- Cytosolic sulfotransferase 18
- Transcription factor MYB34
Sequence:
MLYFILLPLLFLVISYKFLYSKTQRFNLPPGPPSRPFVGHLHLMKPPIHRLLQRYSNQYGPIFSLRFGSRRVVVITSPSLAQESFTGQNDIVLSSRPLQLTAKYVAYNHTTVGTAPYGDHWRNLRRICSQEILSSHRLINFQHIRKDEILRMLTRLSRYTQTSNESNDFTHIELEPLLSDLTFNNIVRMVTGKRYYGDDVNNKEEAELFKKLVYDIAMYSGANHSADYLPILKLFGNKFEKEVKAIGKSMDDILQRLLDECRRDKEGNTMVNHLISLQQQQPEYYTDVIIKGLMMSMMLAGTETSAVTLEWAMANLLRNPEVLEKARSEIDEKIGKDRLIDESDIAVLPYLQNVVSETFRLFPVAPFLIPRSPTDDMKIGGYDVPRDTIVMVNAWAIHRDPEIWEEPEKFNPDRYNDGCGSDYYVYKLMPFGNGRRTCPGAGLGQRIVTLALGSLIQCFEWENVKGEEMDMSESTGLGMRKMDPLRAMCRPRPIMSKLLL
Protein: Uncharacterized protein (Q384I8)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MSTLASALPLLATKNVLCGVTGSTIQFFCDLTRDYGPTSTKKSVIIASSCGNRPIGTTGAHIVLNVFFAKETKPQLDEDTLAPLRTREVFGLYCYRSVVGEKILCIEVDFNDVGTKKVGKGRGTVLATSRGCRPLGNTGIYCSFNCLRSLGAPSNLSELSSVFQPSTHPVGEKVDLGNGFIMNVESSTQITIVYECGRDEMCDTVRLRPYLLNGVINLNMCIRCGVKRNAAYENESSKKRTLLLSNSSVFAKPSLTARNAKARYTVTPGVNTERIRLEVRFDPTYIHYNGGWNEPIIVSNTGGWVTLEDGVMFTFCAHRSPVSLASDTVVDAVREVLGGFSPEELAYLRFKEVYRKVFEKVGTANAEEDDMKEEVRLAIISHFHRRAF
Protein: Somatostatin receptor type 5 (SS-5-R) (SS5-R) (SS5R) (O08858)
Organism: Mus musculus (Mouse)
Function: Receptor for somatostatin-28. The activity of this receptor is mediated by G proteins which inhibit adenylyl cyclase. Increases cell growth inhibition activity of SSTR2 following heterodimerization.
Subcellular location: Cell membrane {ECO:0000269|PubMed:21820437}; Multi-pass membrane protein {ECO:0000269|PubMed:21820437}.
Interaction partners:
- Somatostatin
- Cortistatin
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Appetite-regulating hormone
- Pro-neuropeptide Y
- Pro-opiomelanocortin
- Neuropeptide Y receptor type 5
- Oxytocin-neurophysin 1
Sequence:
MEPLSLTSTPSWNASAASSSSHNWSLVDPVSPMGARAVLVPVLYLLVCTVGLGGNTLVIYVVLRYAKMKTVTNVYILNLAVADVLFMLGLPFLATQNAVSYWPFGSFLCRLVMTLDGINQFTSIFCLMVMSVDRYLAVVHPLRSARWRRPRVAKLASAAVWVFSLLMSLPLLVFADVQEGWGTCNLSWPEPVGLWGAAFITYTSVLGFFGPLLVICLCYLLIVVKVKAAGMRVGSSRRRRSERKVTRMVVVVVLVFVGCWLPFFIVNIVNLAFTLPEEPTSAGLYFFVVVLSYANSCANPLLYGFLSDNFRQSFRKALCLRRGYGVEDADAIEPRPDKSGRPQTTLPTRSCEANGLMQTSRL
Protein: UV excision repair protein RAD23 homolog B (HR23B) (hHR23B) (XP-C repair-complementing complex 58 kDa protein) (p58) (P54727)
Organism: Homo sapiens (Human)
Function: Multiubiquitin chain receptor involved in modulation of proteasomal degradation. Binds to polyubiquitin chains. Proposed to be capable to bind simultaneously to the 26S proteasome and to polyubiquitinated substrates and to deliver ubiquitinated proteins to the proteasome. May play a role in endoplasmic reticulum-associated degradation (ERAD) of misfolded glycoproteins by association with PNGase and delivering deglycosylated proteins to the proteasome.
Subcellular location: Nucleus. Cytoplasm. Note=The intracellular distribution is cell cycle dependent. Localized to the nucleus and the cytoplasm during G1 phase. Nuclear levels decrease during S-phase; upon entering mitosis, relocalizes in the cytoplasm without association with chromatin.
Interaction partners:
- DNA repair protein complementing XP-C cells
- 26S proteasome non-ATPase regulatory subunit 4
- Centrin-2
- DNA excision repair protein ERCC-1
- Peptide-N
- Ataxin-3
- DNA repair protein complementing XP-A cells
- DNA repair endonuclease XPF
- DNA excision repair protein ERCC-5
- General transcription and DNA repair factor IIH helicase subunit XPD
Sequence:
MQVTLKTLQQQTFKIDIDPEETVKALKEKIESEKGKDAFPVAGQKLIYAGKILNDDTALKEYKIDEKNFVVVMVTKPKAVSTPAPATTQQSAPASTTAVTSSTTTTVAQAPTPVPALAPTSTPASITPASATASSEPAPASAAKQEKPAEKPAETPVATSPTATDSTSGDSSRSNLFEDATSALVTGQSYENMVTEIMSMGYEREQVIAALRASFNNPDRAVEYLLMGIPGDRESQAVVDPPQAASTGAPQSSAVAAAAATTTATTTTTSSGGHPLEFLRNQPQFQQMRQIIQQNPSLLPALLQQIGRENPQLLQQISQHQEHFIQMLNEPVQEAGGQGGGGGGGSGGIAEAGSGHMNYIQVTPQEKEAIERLKALGFPEGLVIQAYFACEKNENLAANFLLQQNFDED
Protein: Coatomer subunit beta (Beta-coat protein) (Q5A6M6)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Subcellular location: Cytoplasm {ECO:0000256|PIRNR:PIRNR005727}. Golgi apparatus membrane {ECO:0000256|ARBA:ARBA00004255, ECO:0000256|PIRNR:PIRNR005727}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004255, ECO:0000256|PIRNR:PIRNR005727}; Cytoplasmic side {ECO:0000256|ARBA:ARBA00004255, ECO:0000256|PIRNR:PIRNR005727}. Cytoplasmic vesicle, COPI-coated vesicle membrane {ECO:0000256|PIRNR:PIRNR005727}; Peripheral membrane protein {ECO:0000256|PIRNR:PIRNR005727}; Cytoplasmic side {ECO:0000256|PIRNR:PIRNR005727}.
Interaction partners:
- Coatomer subunit zeta
- Coatomer subunit gamma
- Coatomer subunit beta'
- Coatomer subunit delta
- Coatomer subunit alpha
- Coatomer subunit epsilon
- ADP-ribosylation factor GTPase-activating protein
- ADP-ribosylation factor
- Uso1p
- ADP-ribosylation factor
Sequence:
MSDSGYTLIYEPNTATKVSVNEFKNLLEKGKDDVKVDTMKKILITILNGDPLPDLLMHIIRFVMPSRNKELKKLLYHYWEVCPKMDESGKMRHEMILVCNAIQRDLQHPNEYIRGNTLRYLTKLKEPELLETLVPNVRQCLEHRHAYVRKNAVFALWSIHKVSDHLAPDADELIYRFLYEENDSVCKRNAFVCLGDLNREAALQYIQDNISVIETLDPLIQLAFIEFIKKDSIQNPALKQQYAQLMTEIIESSSNVVMYEAANTLTVLTSNPQSILLAGNKFVELATRESDNNVKIITLERINQLHKQHPGVLQDLSLEILRVLSSQDLDVKKKALDVTLQFITTRNVEDVVKLLKKELQSTALSNDDKNADYRQLLINAIHQLAIKFVEVAANVIDLLLDSIADLNTTAAYEVITFVKEVVEKFPDLRDAILRRLILALPHVKSGKVFRGALWVIGEYALEESLIQESWKYIRGSIGEVPIIASELKSKKRDDTEESQEEETEYDGKPRRKGPVVLPDGTYATESALTSETTDSLESDSKTPIRKQILAGDFYLGAVLASTLVKLILRLQSLKQTQEKILNGLKAEALLIMVSILRVGESSLVSKKIDEDSADRILSYIKILNDEEDLQEIKTSFLEDTKDAFKAQINNAELKKAEALAKDLHDNAEQIDDAIVFRQLDKDNKKSKASVDDVAAASGSNELKKENLSSRLNKIIQLTGFSDPIYAEAFVKVHQYDVVLDVLLVNQTTTTLRNLSVEFATLGDLKVVDKPTTANIGPHGFYKVQTTIKVTSADTGVIFGNIVYDGQHSDDSRIVILNDVHVDIMDYIKPATCSESQFRKMWNEFEWENKITIKSPIETLKEYLDELMKGTNMQCLTPGAVIGEECQFLSANLYSRSSFGEDALANLCIEKQSDGPIIGHVRIRSKGQGLALSLGDRVASISRKGKKATIARV
Protein: LD02709p (Microtubule-associated protein 60) (Q7K180)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Centrosome-associated zinc finger protein Cp190
- Centrosomin
Sequence:
MAIQLDKILQDIAKEKVLHPNNGGASKQEQEEAWARIGRLNKLSVHESRSIFIVLQKKYEQEKLKGNSAWKLFSLMHQIHQEPKISIKEENDQVPMEEVEEYEMLEVQEPEDEDDAHQYGQHTNSTGSASSDGESPTKSHSTGSPEKDERLAYAKPNVDTPRPAIEEKKLLNTLANNTPRSSSLSAAAAVLQKKGITVKKTPSSAAAPKPAIGQQAPASGQRSSSSRTTIQLPDSLKRKLSEEYTSSSAQKKQTKTTSPKQAASSAAATSVHTSVPDQLPAGNNVVHTTTAQLMQVKKEREDNQTPPPGINIITIPSAQQINGGGGGANSSTAATIASTSVASTNGFSPHIDELDFKNDIIFGPKINAASSNTPEIINLGNFDNSLPPTFFKNLCNSSRHESLGLYVANVMNRLSSRASAKLELSILRAILDVQSDELEQ
Protein: Palustrin-1d (P84277)
Organism: Lithobates palustris (Pickerel frog) (Rana palustris)
Function: Antimicrobial activity against Gram-negative bacterium E.coli.
Subcellular location: Secreted {ECO:0000269|PubMed:11087945}.
Interaction partners:
Sequence:
ALSILKGLEKLAKMGIALTNCKATKKC