wanglab/gogpt-training-data huggingface dataset:
Protein: Rab GTPase-activating protein 1 (GAP and centrosome-associated protein) (Rab6 GTPase-activating protein GAPCenA) (Q9Y3P9)
Organism: Homo sapiens (Human)
Function: May act as a GTPase-activating protein of RAB6A. May play a role in microtubule nucleation by centrosome. May participate in a RAB6A-mediated pathway involved in the metaphase-anaphase transition.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:10202141}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:10202141}. Note=Predominantly cytosolic but also associated with the centrosome. {ECO:0000269|PubMed:10202141}.
Interaction partners:
- Ras-related protein Rab-6A
- Tuftelin
- Ras-related protein Rab-6B
Sequence:
MDDKASVGKISVSSDSVSTLNSEDFVLVSRQGDETPSTNNGSDDEKTGLKIVGNGSEQQLQKELADVLMDPPMDDQPGEKELVKRSQLDGEGDGPLSNQLSASSTINPVPLVGLQKPEMSLPVKPGQGDSEASSPFTPVADEDSVVFSKLTYLGCASVNAPRSEVEALRMMSILRSQCQISLDVTLSVPNVSEGIVRLLDPQTNTEIANYPIYKILFCVRGHDGTPESDCFAFTESHYNAELFRIHVFRCEIQEAVSRILYSFATAFRRSAKQTPLSATAAPQTPDSDIFTFSVSLEIKEDDGKGYFSAVPKDKDRQCFKLRQGIDKKIVIYVQQTTNKELAIERCFGLLLSPGKDVRNSDMHLLDLESMGKSSDGKSYVITGSWNPKSPHFQVVNEETPKDKVLFMTTAVDLVITEVQEPVRFLLETKVRVCSPNERLFWPFSKRSTTENFFLKLKQIKQRERKNNTDTLYEVVCLESESERERRKTTASPSVRLPQSGSQSSVIPSPPEDDEEEDNDEPLLSGSGDVSKECAEKILETWGELLSKWHLNLNVRPKQLSSLVRNGVPEALRGEVWQLLAGCHNNDHLVEKYRILITKESPQDSAITRDINRTFPAHDYFKDTGGDGQDSLYKICKAYSVYDEEIGYCQGQSFLAAVLLLHMPEEQAFSVLVKIMFDYGLRELFKQNFEDLHCKFYQLERLMQEYIPDLYNHFLDISLEAHMYASQWFLTLFTAKFPLYMVFHIIDLLLCEGISVIFNVALGLLKTSKDDLLLTDFEGALKFFRVQLPKRYRSEENAKKLMELACNMKISQKKLKKYEKEYHTMREQQAQQEDPIERFERENRRLQEANMRLEQENDDLAHELVTSKIALRKDLDNAEEKADALNKELLMTKQKLIDAEEEKRRLEEESAQLKEMCRRELDKAESEIKKNSSIIGDYKQICSQLSERLEKQQTANKVEIEKIRQKVDDCERCREFFNKEGRVKGISSTKEVLDEDTDEEKETLKNQLREMELELAQTKLQLVEAECKIQDLEHHLGLALNEVQAAKKTWFNRTLSSIKTATGVQGKETC
Protein: Mitochondrial glycine transporter (Heme biosynthesis protein of SLC25 family) (Solute carrier family 25 member 38 homolog) (Q07534)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Mitochondrial glycine transporter that imports glycine into the mitochondrial matrix. Plays an important role in providing glycine for the first enzymatic step in heme biosynthesis, the condensation of glycine with succinyl-CoA to produce 5-aminolevulinate (ALA) in the mitochondrial matrix.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:16823961, ECO:0000269|PubMed:27476175}. Mitochondrion inner membrane {ECO:0000255|HAMAP-Rule:MF_03064, ECO:0000305|PubMed:10930523, ECO:0000305|PubMed:27476175}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_03064, ECO:0000305|PubMed:10930523}.
Interaction partners:
- Uncharacterized mitochondrial carrier YFR045W
- Putative mitochondrial carrier protein PET8
- Protoporphyrinogen oxidase
- ATP-dependent clpX-like chaperone, mitochondrial
- 5-aminolevulinate synthase, mitochondrial
- Uroporphyrinogen-III synthase
Sequence:
MTEQATKPRNSSHLIGGFFGGLTSAVALQPLDLLKTRIQQDKKATLWKNLKEIDSPLQLWRGTLPSALRTSIGSALYLSCLNLMRSSLAKRRNAVPSLTNDSNIVYNKSSSLPRLTMYENLLTGAFARGLVGYITMPITVIKVRYESTLYNYSSLKEAITHIYTKEGLFGFFRGFGATCLRDAPYAGLYVLLYEKSKQLLPMVLPSRFIHYNPEGGFTTYTSTTVNTTSAVLSASLATTVTAPFDTIKTRMQLEPSKFTNSFNTFTSIVKNENVLKLFSGLSMRLARKAFSAGIAWGIYEELVKRFM
Protein: non-specific protein-tyrosine kinase (EC 2.7.10.2) (A0A5F9ZHJ2)
Organism: Homo sapiens (Human)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004236}. Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Endomembrane system {ECO:0000256|ARBA:ARBA00029433}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00029433}; Cytoplasmic side {ECO:0000256|ARBA:ARBA00029433}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MPAARRFPGLELSFPLLARLRRRLYTRLGGGRMQPEEGTGWLLELLSEVQLQQYFLRLRDDLNVTRLSHFEYVKNEDLEKIGMGRPGQRRLWEAVKRRKALCKRKSWMSKVFSGKRLEAEFPPHHSQSTFRKTSPAPGGPAGEGPLQSLTCLIGEKDLRLLEKLGDGSFGVVRRGEWDAPSGKTVSVAVKCLKPDVLSQPEAMDDFIREVNAMHSLDHRNLIRLYGVVLTPPMKMVTELAPLGSLLDRLRKHQGHFLLGTLSRYAVQVAEGMGYLESKRFIHRDLAARNLLLATRDLVKIGDFGLMRALPQNDDHYVMQEHRKVPFAWCAPESLKTRTFSHASDTWMFGVTLWEMFTYGQEPWIGLNGSQILHKIDKEGERLPRPEDCPQDIYNVMVQCWAHKPEDRPTFVALRDFLLEAQPTDMRALQDFEEPDKLHIQMNDVITVIEGRAENYWWRGQNTRTLCVGPFPRNVVTSVAGLSAQDISQPLQNSFIHTGHGDSDPRHCWGFPDRIDELYLGNPMDPPDLLSVELSTSRPPQHLGGVKKPTYDPVSEDQDPLSSDFKRLGLRKPGLPRGLWLAKPSARVPGTKASRGSGAEVTLIDFGEEPVVPALRPCAPSLAQLAMDACSLLDETPPQSPTRALPRPLHPTPVVDWDARPLPPPPAYDDVAQDEDDFEICSINSTLVGAGVPAGPSQGQTNYAFVPEQARPPPPLEDNLFLPPQGGGKPPSSAQTAEIFQALQQECMRQLQAPAGSPAPSPSPGGDDKPQVPPRVPIPPRPTRPHVQLSPAPPGEEETSQWPGPASPPRVPPREPLSPQGSRTPSPLVPPGSSPLPPRLSSSPGKTMPTTQSFASDPKYATPQVIQAPGPRAGPCILPIVRDGKKVSSTHYYLLPERPSYLERYQRFLREAQSPEEPTPLPVPLLLPPPSTPAPAAPTATVRPMPQAALDPKANFSTNNSNPGARPPPPRATARLPQRGCPGDGPEAGRPADKIQMLQAMVHGVTTEECQAALQCHGWSVQRAAQYLKVEQLFGLGLRPRGECHKVLEMFDWNLEQAGCHLLGSWGPAHHKR
Protein: Cell adhesion molecule CEACAM4 (Carcinoembryonic antigen CGM7) (Carcinoembryonic antigen-related cell adhesion molecule 4) (CEA cell adhesion molecule 4) (Non-specific cross-reacting antigen W236) (O75871)
Organism: Homo sapiens (Human)
Function: Granulocyte orphan receptor that acts as an trigger efficient phagocytosis of attached particles.
Subcellular location: Membrane; Single-pass type I membrane protein.
Interaction partners:
Sequence:
MGPPSAAPRGGHRPWQGLLITASLLTFWHPPTTVQFTIEALPSSAAEGKDVLLLACNISETIQAYYWHKGKTAEGSPLIAGYITDIQANIPGAAYSGRETVYPNGSLLFQNITLEDAGSYTLRTINASYDSDQATGQLHVHQNNVPGLPVGAVAGIVTGVLVGVALVAALVCFLLLSRTGRASIQRDLREQPPPASTPGHGPSHRSTFSAPLPSPRTATPIYEELLYSDANIYCQIDHKADVVS
Protein: Tripartite motif-containing protein 10 (B30-RING finger protein) (RING finger protein 9) (Q9UDY6)
Organism: Homo sapiens (Human)
Function: E3 ligase that plays an essential role in the differentiation and survival of terminal erythroid cells. May directly bind to PTEN and promote its ubiquitination, resulting in its proteasomal degradation and activation of hypertrophic signaling (By similarity). In addition, plays a role in immune response regulation by repressing the phosphorylation of STAT1 and STAT2 in the interferon/JAK/STAT signaling pathway independent of its E3 ligase activity. Mechanistically, interacts with the intracellular domain of IFNAR1 and thereby inhibits the association between TYK2 and IFNAR1.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:11331580, ECO:0000269|PubMed:33811647}.
Interaction partners:
- Glycophorin-B
- Glycophorin-A
Sequence:
MASAASVTSLADEVNCPICQGTLREPVTIDCGHNFCRACLTRYCEIPGPDLEESPTCPLCKEPFRPGSFRPNWQLANVVENIERLQLVSTLGLGEEDVCQEHGEKIYFFCEDDEMQLCVVCREAGEHATHTMRFLEDAAAPYREQIHKCLKCLRKEREEIQEIQSRENKRMQVLLTQVSTKRQQVISEFAHLRKFLEEQQSILLAQLESQDGDILRQRDEFDLLVAGEICRFSALIEELEEKNERPARELLTDIRSTLIRCETRKCRKPVAVSPELGQRIRDFPQQALPLQREMKMFLEKLCFELDYEPAHISLDPQTSHPKLLLSEDHQRAQFSYKWQNSPDNPQRFDRATCVLAHTGITGGRHTWVVSIDLAHGGSCTVGVVSEDVQRKGELRLRPEEGVWAVRLAWGFVSALGSFPTRLTLKEQPRQVRVSLDYEVGWVTFTNAVTREPIYTFTASFTRKVIPFFGLWGRGSSFSLSS
Protein: CD1c molecule (H0Y6Y6)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
XFLHNWSKGNFSNEELSDLELLFRFYLFGLTREIQDHASQDYSKYPFEVQVKAGCELHSGKSPEGFFQVAFNGLDLLSFQNTTWVPSPGCGSLAQSVCHLLNHQYEGVTETVYNLIRSTCPRFLLGLLDAGKMYVHRQVRPEAWLSSRPSLGSGQLLLVCHASGFYPKPVWVTWMRNEQEQLGTKHGDILPNADGTWYLQVILEVASEEPAGLSCRVRHSSLGGQDIILYWAHIRTSCETLPPDSPIVLRTQQPRSLVQYSDAIPSTLHLNCFSFCIINIC
Protein: Inositol polyphosphate 5-phosphatase K (EC 3.1.3.56) (Phosphatidylinositol-3,4,5-trisphosphate 5-phosphatase) (EC 3.1.3.86) (Phosphatidylinositol-4,5-bisphosphate 5-phosphatase) (EC 3.1.3.36) (Skeletal muscle and kidney-enriched inositol phosphatase) (Q9BT40)
Organism: Homo sapiens (Human)
Function: Inositol 5-phosphatase which acts on inositol 1,4,5-trisphosphate, inositol 1,3,4,5-tetrakisphosphate, phosphatidylinositol 4,5-bisphosphate and phosphatidylinositol 3,4,5-trisphosphate. Has 6-fold higher affinity for phosphatidylinositol 4,5-bisphosphate than for inositol 1,4,5-trisphosphate. Negatively regulates assembly of the actin cytoskeleton. Controls insulin-dependent glucose uptake among inositol 3,4,5-trisphosphate phosphatases; therefore, is the specific regulator for insulin signaling in skeletal muscle (By similarity).
Subcellular location: Endoplasmic reticulum {ECO:0000269|PubMed:12536145, ECO:0000269|PubMed:26940976, ECO:0000269|PubMed:28190456}. Cytoplasm {ECO:0000269|PubMed:10753883}. Note=Following stimulation with EGF, translocates to membrane ruffles (PubMed:12536145, PubMed:26940976). Concentrated at the periphery of the nucleus (PubMed:10753883). {ECO:0000269|PubMed:10753883, ECO:0000269|PubMed:12536145, ECO:0000269|PubMed:26940976}.
Interaction partners:
- Inositol polyphosphate-5-phosphatase A
- Inositol-trisphosphate 3-kinase C
- Inositol-trisphosphate 3-kinase B
- Multiple inositol polyphosphate phosphatase 1
- Inositol-trisphosphate 3-kinase A
- Inositol polyphosphate multikinase
- Inositol-tetrakisphosphate 1-kinase
- Inositol polyphosphate 1-phosphatase
- Phosphatidylinositol 4,5-bisphosphate 5-phosphatase A
- 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase epsilon-1
Sequence:
MSSRKLSGPKGRRLSIHVVTWNVASAAPPLDLSDLLQLNNRNLNLDIYVIGLQELNSGIISLLSDAAFNDSWSSFLMDVLSPLSFIKVSHVRMQGILLLVFAKYQHLPYIQILSTKSTPTGLFGYWGNKGGVNICLKLYGYYVSIINCHLPPHISNNYQRLEHFDRILEMQNCEGRDIPNILDHDLIIWFGDMNFRIEDFGLHFVRESIKNRCYGGLWEKDQLSIAKKHDPLLREFQEGRLLFPPTYKFDRNSNDYDTSEKKRKPAWTDRILWRLKRQPCAGPDTPIPPASHFSLSLRGYSSHMTYGISDHKPVSGTFDLELKPLVSAPLIVLMPEDLWTVENDMMVSYSSTSDFPSSPWDWIGLYKVGLRDVNDYVSYAWVGDSKVSCSDNLNQVYIDISNIPTTEDEFLLCYYSNSLRSVVGISRPFQIPPGSLREDPLGEAQPQI
Protein: Flagellar hook-associated protein 2 (HAP2) (Filament cap protein) (Flagellar cap protein) (P16328)
Organism: Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Function: Required for the morphogenesis and for the elongation of the flagellar filament by facilitating polymerization of the flagellin monomers at the tip of growing filament. Forms a capping structure, which prevents flagellin subunits (transported through the central channel of the flagellum) from leaking out without polymerization at the distal end.
Subcellular location: Secreted. Bacterial flagellum.
Interaction partners:
- Flagellar hook-associated protein 1
- Flagellar hook-associated protein 3
- Flagellar protein FliT
- Flagellar secretion chaperone FliS
- Flagellin
- Flagellar hook protein FlgE
- Flagellar M-ring protein
- Basal-body rod modification protein FlgD
- Flagellar hook-basal body complex protein FliE
- Flagellar basal body rod protein FlgB
Sequence:
MASISSLGVGSNLPLDQLLTDLTKNEKGRLTPITKQQSANSAKLTAYGTLKSALEKFQTANTALNKADLFKSTVASSTTEDLKVSTTAGAAAGTYKINVTQLAAAQSLATKTTFATTKEQLGDTSVTSRTIKIEQPGRKEPLEIKLDKGDTSMEAIRDAINDADSGIAASIVKVKENEFQLVLTANSGTDNTMKITVEGDTKLNDLLAYDSTTNTGNMQELVKAENAKLNVNGIDIERQSNTVTDAPQGITLTLTKKVTDATVTVTKDDTKAKEAIKSWVDAYNSLVDTFSSLTKYTAVEPGEEASDKNGALLGDSVVRTIQTGIRAQFANSGSNSAFKTMAEIGITQDGTSGKLKIDDDKLTKVLKDNTAAARELLVGDGKETGITTKIATEVKSYLADDGIIDNAQDNVNATLKSLTKQYLSVSNSIDETVARYKAQFTQLDTMMSKLNNTSSYLTQQFTAMNKS
Protein: Protein interacting with Ttk69 and Sin3A, isoform E (M9PHN7)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MSLQTKRQHCYLCDLPRMPWAMINDFSEAVCRGCVNYEGADRIEAVLDAARQMKRLHPASKQQRSHENGEVSAAAAAAVVLQQQQQLQVGPVPGQGPGSHRGGGGGGPPGAPPGSGGPGPSGAGSLSSLGNAVAAAAAAAAVHHHHQMPYQMPVPRIGPPLDYPVKLEDAPGGGVRPVRISHMTPHHLPPNATRGGGGAPGGGVPTAGSGGGSLPPALSVNLKRPPSEDVDVDVSQQQQQSGHGLAPDGSAGNSLSAGGGVSGGCPPGIKRSAMDDPSGVGGRPPLTRGESLPAAVSYVPERQLSGLRDKQQPVRAPSFDASTFKAGSSSGRRSSGSRHVSSTTVTSSEVGGSNPGQAVVAGGLGGGGGGGPGSNAASGQLGGPSGGSGQLSCTSGGPGGSASSGSGGNGAIGPASMAPNSVAGDGSPAGGNGPSGSNGSGGSVNPGPGSSGSQGGGGGGTPLASGGGSAGSGGLGGAPGSSAASNSAAAAAAAAAQNATLKCTLCQERLEDTHFVQCPSVNHHKFCFPCSRESIKRQNGLGNEVYCPSGDRCPLANSVIPWAFMQGEITTILGEEVKVKKERES
Protein: F-actin-capping protein subunit beta (CapZ beta) (Q5XI32)
Organism: Rattus norvegicus (Rat)
Function: F-actin-capping proteins bind in a Ca(2+)-independent manner to the fast growing ends of actin filaments (barbed end) thereby blocking the exchange of subunits at these ends. Unlike other capping proteins (such as gelsolin and severin), these proteins do not sever actin filaments. Plays a role in the regulation of cell morphology and cytoskeletal organization (By similarity). Forms, with CAPZB, the barbed end of the fast growing ends of actin filaments in the dynactin complex and stabilizes dynactin structure. The dynactin multiprotein complex activates the molecular motor dynein for ultra-processive transport along microtubules (By similarity).
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:19343716}. Cytoplasm, myofibril, sarcomere {ECO:0000305}.
Interaction partners:
- F-actin-capping protein subunit alpha-1
- F-actin-capping protein subunit alpha-3
- F-actin-capping protein subunit alpha-2
- Dynactin subunit 4
- F-actin-capping protein subunit alpha
- Myotrophin
- Dynactin subunit 2
- Dynactin subunit 6
- Alpha-centractin
- Dynactin subunit 1
Sequence:
MSDQQLDCALDLMRRLPPQQIEKNLSDLIDLVPSLCEDLLSSVDQPLKIARDKVVGKDYLLCDYNRDGDSYRSPWSNKYDPPLEDGAMPSARLRKLEVEANNAFDQYRDLYFEGGVSSVYLWDLDHGFAGVILIKKAGDGSKKIKGCWDSIHVVEVQEKSSGRTAHYKLTSTVMLWLQTNKSGSGTMNLGGSLTRQMEKDETVSDCSPHIANIGRLVEDMENKIRSTLNEIYFGKTKDIVNGLRSVQTFADKSKQEALKNDLVEALKRKQQC
Protein: ERC protein 2 (CAZ-associated structural protein 1) (CAST1) (Q6PH08)
Organism: Mus musculus (Mouse)
Function: Thought to be involved in the organization of the cytomatrix at the nerve terminals active zone (CAZ) which regulates neurotransmitter release. Seems to act together with BSN. May recruit liprin-alpha proteins to the CAZ.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:12163476}. Synapse {ECO:0000269|PubMed:12163476}. Presynaptic active zone {ECO:0000269|PubMed:12163476}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:12163476}. Note=Localized to the active zone of presynaptic density.
Interaction partners:
- Protein bassoon
- Regulating synaptic membrane exocytosis protein 2
- Protein unc-13 homolog B
- Regulating synaptic membrane exocytosis protein 1
- Protein piccolo
- Protein unc-13 homolog A
- Liprin-alpha-3
- Ras-related protein Rab-6A
Sequence:
MYGSARTISNLEGSPSRSPRLPRSPRLGHRRTSSGGGGGTGKTLSMENIQSLNAAYATSGPMYLSDHEGVASTTYPKGTMTLGRATNRAVYGGRVTAMGSSPNIASAGLSHTDVLSYTDQHGGLSGSSHHHHHQVPSMLRQVRDSTMLDLQAQLKELQRENDLLRKELDIKDSKLGSSMNSIKTFWSPELKKERVLRKEEAARMSVLKEQMRVSHEENQHLQLTIQALQDELRTQRDLNHLLQQESGNRGAEHFTIELTEENFRRLQAEHDRQAKELFLLRKTLEEMELRIETQKQTLNARDESIKKLLEMLQSKGLPSKSLEDDNERTRRMAEAESQVSHLEVILDQKEKENIHLREELHRRSQLQPEPAKTKALQTVIEMKDTKIASLERNIRDLEDEVQMLKANGVLNTEDREEEIKQIEVYKSHSKFMKTKIDQLKQELSKKESELLALQTKLETLSNQNSDCKQHIEVLKESLTAKEQRAAILQTEVDALRLRLEEKESFLNKKTKQLQDLTEEKGTLAGEIRDMKDMLEVKERKINVLQKKIENLQEQLRDKDKQLTNLKDRVKSLQTDSSNTDTALATLEEALSEKERIIERLKEQRERDDRERLEEIESFRKENKDLKEKVNALQAELTEKESSLIDLKEHASSLASAGLKRDSKLKSLEIAIEQKKEECNKLEAQLKKAHNIEDDSRMNPEFADRLKQLDKEASYYRDECGKAQAEVDRLLEILKEVENEKNDKDKKIAELESLTLRHMKDQNKKVANLKYNQQLEKKKNAQLLEEVRRREDSMVDNSQHLQIEELMNALEKTRQELDATKARLASTQQSLAEKEAHLANLRIERRKQLEEILEMKQEALLAAISEKDANIALLELSASKKKKTQEEVMALKREKDRLVHQLKQQTQNRMKLMADNYDEDHHHYHHHHHHHHHRSPGRSQHSNHRPSPDQDDEEGIWA
Protein: Cyclin Y, isoform A (Cyclin Y, isoform B) (LD31675p) (Q9VKF0)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- cyclin-dependent kinase
- PITH domain-containing protein CG6153
Sequence:
MGNKNSCCAYSSPQSDRKSKDMPPVFEERIIQLGHPPHTSQHQLDGHHGSASAVHLHHHHHGHNQQQNQQGGGGDNYENQQNLQHISEREALEGEEDPSVDPTAATMFLERSKVENGGMTRKRSQQQIAQQAGSGGGGGGGGGGGSTPGGNSCGGGGGMKKSSSCSTIYLDDSTVSQPNLKNTVKCVSLAIYYHIKNRQSDRRLDIFDEKLHPLTHDQVPDNYDTHNPEHRQIYKFVRTLFNAAQLTAECAIITLVYLERLLTYAELDVGPCNWKRMVLGAILLASKVWDDQAVWNVDYCQILKDITVEDMNELERQFLELLQFNINVPSSVYAKYYFDLRTLAEANELNFPTEPLSKERAQKLEAMSRVMQDKVTAEALKNGIKKWSSMDNISQGGPRRSVAILS
Protein: Tubulin-binding cofactor B (A1ZBM2)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
- Tubulin-specific chaperone D
- LD34582p
- Tubulin-specific chaperone E
- ADP-ribosylation factor-like protein 2
- Trafficking protein particle complex subunit
Sequence:
MSTIIETGKSDFIKVNVSNSHNDAVAFEVKLAKDLTVAQLKTKLEILTGGCAGTMKVQVFKGDTCVSTMDNNDAQLGYYANSDGLRLHVVDSFATFSFDSAPVEKFELSKDQYEQRTDSVRNYLKINRMGKYNDEEMQQAEEKKRLQAEEIQKRAELCVLGGRCEVTVPGNPTRRGTIRYNGPLEGKSGHFIGVEYDEPLGKNNGSFGGKAYFTCAPNYGGFVSPLSVTVGDFPPEDFNMDDEL
Protein: Zinc finger MIZ domain-containing protein 2 (PIAS-like protein Zimp7) (Q8NF64)
Organism: Homo sapiens (Human)
Function: Increases ligand-dependent transcriptional activity of AR and other nuclear hormone receptors.
Subcellular location: Nucleus {ECO:0000269|PubMed:16051670, ECO:0000269|PubMed:9853615}. Note=Detected at replication foci throughout S phase.
Interaction partners:
- SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily E member 1
- SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 4
Sequence:
MNSMNPMKPALPPAPHGDGSFAYESVPWQQSATQPAGSLSVVTTVWGVGNATQSQVLGNPMGPAGSPSGSSMMPGVAGGSSALTSPQCLGQQAFAEGGANKGYVQQGVYSRGGYPGAPGFTTGYAGGPGGLGLPSHAARPSTDFTQAAAAAAVAAAAATATATATATVAALQEKQSQELSQYGAMGAGQSFNSQFLQHGGPRGPSVPAGMNPTGIGGVMGPSGLSPLAMNPTRAAGMTPLYAGQRLPQHGYPGPPQAQPLPRQGVKRTYSEVYPGQQYLQGGQYAPSTAQFAPSPGQPPAPSPSYPGHRLPLQQGMTQSLSVPGPTGLHYKPTEQFNGQGASFNGGSVSYSQPGLSGPTRSIPGYPSSPLPGNPTPPMTPSSSVPYMSPNQEVKSPFLPDLKPNLNSLHSSPSGSGPCDELRLTFPVRDGVVLEPFRLQHNLAVSNHVFQLRDSVYKTLIMRPDLELQFKCYHHEDRQMNTNWPASVQVSVNATPLTIERGDNKTSHKPLYLKHVCQPGRNTIQITVTACCCSHLFVLQLVHRPSVRSVLQGLLKKRLLPAEHCITKIKRNFSSGTIPGTPGPNGEDGVEQTAIKVSLKCPITFRRIQLPARGHDCRHIQCFDLESYLQLNCERGTWRCPVCNKTALLEGLEVDQYMLGILIYIQNSDYEEITIDPTCSWKPVPVKPDMHIKEEPDGPALKRCRTVSPAHVLMPSVMEMIAALGPGAAPFAPLQPPSVPAPSDYPGQGSSFLGPGTFPESFPPTTPSTPTLAEFTPGPPPISYQSDIPSSLLTSEKSTACLPSQMAPAGHLDPTHNPGTPGLHTSNLGAPPGPQLHHSNPPPASRQSLGQASLGPTGELAFSPATGVMGPPSMSGAGEAPEPALDLLPELTNPDELLSYLGPPDLPTNNNDDLLSLFENN
Protein: Ovarian jelly-peptide 3 (OJP3) [Cleaved into: Ovarian jelly-peptide 2 (OJP2)] (P85069)
Organism: Sepia officinalis (Common cuttlefish)
Function: Has myotropic activity targeting the genital tract.
Subcellular location: Secreted {ECO:0000269|PubMed:16434122}.
Interaction partners:
Sequence:
DEVKIVLD
Protein: Large ribosomal subunit protein uL11x (60S ribosomal protein L12-3) (Q9FF52)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Binds directly to 26S ribosomal RNA.
Interaction partners:
- Large ribosomal subunit protein eL43y
- Large ribosomal subunit protein uL24z
- Large ribosomal subunit protein uL5y/uL5x/uL5w
- Large ribosomal subunit protein uL5z
- Small ribosomal subunit protein eS24z
- Large ribosomal subunit protein eL31y
- Large ribosomal subunit protein uL18y
- Large ribosomal subunit protein eL8y
- Large ribosomal subunit protein eL31x
- Large ribosomal subunit protein uL23y
Sequence:
MPPKLDPSQIVDVYVRVTGGEVGAASSLAPKIGPLGLAPKKIGEDIAKETAKEWKGLRVTVKLTVQNRQAKVTVVPSAAALVIKALKEPERDRKKVKNIKHNGNISFDDVIEIAKIMRPRSIAKELSGTVKEILGTCVSVGCTVDGKDPKDLQEEINSGDIDIPNE
Protein: Nopp140, isoform E (M9PFZ1)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Nucleolar protein 56
- rRNA 2'-O-methyltransferase fibrillarin
- Nucleolar protein 58
- H/ACA ribonucleoprotein complex subunit 4
- LD11307p
- Ribosomal L1 domain-containing protein CG13096
- Guanine nucleotide-binding protein-like 3 homolog
- DNA-directed RNA polymerase I subunit RPA2
- H/ACA ribonucleoprotein complex subunit 2
- Ribosome biogenesis protein BOP1 homolog
Sequence:
MTDLLKIADAIVLEYLQSKDKNLAKVFQQKTKAASVAKSSPKLSEILQFYQTKSPKKIPAIKATAGDSSEDSDSDSESDAAPKKPATAPALTNGKAVKKAASSTSEDSDSEEEKKPAAKATPAKAVGKKAKSSSEDSSSEEEAPKKAAPVKAPPAKAAPAKKVESSSEDSSSEEEPAKPAVKATTTKVAPAKKADSSSEESSSDEETKPAAKPVAKAAPAKKAASSSEESDSDDEPAAKKPAVQPAAKPAPKAAASSSEDSSSEEEVKPAAKSAAKLAPAKKGASSSDDSSSEDEAPKKAATLAKPISKAAPTKKADSSTEDSSSEDDAPKKVAPAKATPAKAIPAKKAASSDDSSSEEEAPKKAAPANATPARAPPAKKAASSDDSSSEEEAPKKAAPAKATPAKATPAKKAASSDDSSSEEEAPKKAAAPAKATPAKKAKSSSEDSDSDEEEAPKKPAAKAVAKAASSEDSDSSEDEKPAKAAPKALAKSAKAASSDSDDSSDEETPAVKPAVKKTAAPAKKADSSSDESDSGEESGEVKPNSATNGNEKTAQKRKFSGGDQDEATPNKKYNNFVKSGEQQKNDFTSTPNNTFSRNHNMNNSGGGSGRRSPFRRVRTEDVVVDSRVQDMSFEAKENDFKKHNNGRGGRGGSGFSGRPDRSTWETNKFNGEGGGDGGGFKKIGDRKSFGGFDNNQRGGRGGGGRGGGGGFGGRGGGGRGGGGGFGGRGGGGRGGGGFGGRGGRGGGGRGGGFGNKSFDSSAPKQNKKITFDN
Protein: Protein indeterminate-domain 13 (F4JYZ8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probable transcription factor.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00768}.
Interaction partners:
- Protein LOW PSII ACCUMULATION 1
- SH2 domain-containing protein B
- Receptor-like protein 9b
- Receptor-like protein 9a
- At5g55690
- Zinc finger protein AZF3
- Transcription factor bHLH162
Sequence:
MTASHSLALSMTKSTSPLILTLTLSLQPPLKHPRKRETFQEIQAYPNAEVISLSPKSLMATNRFFCEICNKGFQREQNLQLHKRGHNLPWKLKQKTNKNQVKKKVYICPEKSCVHHDPARALGDLTGIKKHFSRKHGEKKWKCDKCSKKYAVISDWKAHNKICGSREFRCDCGTLFSRKDSFISHRSFCDVLAEESSKFFSVPSPLAANSTIATVTDTNNPILIQSQLDQSSTGTADLNVNNNHTTLFGQKFTNSNPTQQQPNALALSSPPSPRSTSDSVHNLWKLQEEECAHQWLLNEYMNNNKNIFHKGIFKNQEDEIKKGNIYSGSNPTDGNIASLFSYNQEAVNMASFSATTLLQKVAQTGTPSSSETSTTMFGQMTSSIFNNTMLNSYCLTAKNNEEELTRDFLGVGSSEDQQRLHRHRFPSSVPLTANHDIPKLAATIVGRKQP
Protein: Flavin-containing monooxygenase 1 (EC 1.14.13.148) (EC 1.14.13.8) (Dimethylaniline monooxygenase [N-oxide-forming] 1) (Dimethylaniline oxidase 1) (Hepatic flavin-containing monooxygenase 1) (FMO 1) (Trimethylamine monooxygenase) (P16549)
Organism: Sus scrofa (Pig)
Function: Broad spectrum monooxygenase that catalyzes the oxygenation of a wide variety of nitrogen- and sulfur-containing compounds including xenobiotics. Catalyzes the S-oxygenation of hypotaurine to produce taurine, an organic osmolyte involved in cell volume regulation as well as a variety of cytoprotective and developmental processes (By similarity). In vitro, catalyzes the N-oxygenation of trimethylamine (TMA) to produce trimethylamine N-oxide (TMAO) and could therefore participate to the detoxification of this compound that is generated by the action of gut microbiota from dietary precursors such as choline, choline containing compounds, betaine or L-carnitine (By similarity).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:7758472}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MAKRVAIVGAGVSGLASIKCCLEEGLEPTCFERSDDLGGLWRFTEHVEEGRASLYKSVVSNSCKEMSCYPDFPFPEDYPNYVPNSHFLEYLRMYANQFNLLKCIQFKTKVCSVTKHEDFNTTGQWDVVTLCEGKQESAVFDAVMVCTGFLTNPYLPLDSFPGINTFKGQYFHSRQYKHPDIFKDKSVLVVGMGNSGTDIAVEASHLAKKVFLSTTGGAWVISRVFDSGYPWDMVFMTRFQNMFRNSLPTPIVNWLIAKKMNSWFNHANYGLIPEDRIQLREPVLNDELPGRIITGKVLIKPSIKEVKENSVVFNSSPEEEPIDIIVFATGYTFAFPFLDESVVKVEDGQASLYKYIFPAHLQKPTLAVIGLIKPLGSLLPTGDTQARWAVRVLKGVNKLPPSSVMIQEVNTRKENKPSGFGLCYCKALQSDYIAYIDELLTYIDAKPNMFSLLLTDPHLALTIFFGPCTPYQFRLTGPGKWEGARNAIMTQWDRTFKVTKTRIVKESPSPFASLLKLFSFLALLVAIFQIFL