wanglab/gogpt-training-data huggingface dataset:
Protein: Zinc transport protein ZntB (P64423)
Organism: Escherichia coli (strain K12)
Function: Zinc transporter. Acts as a Zn(2+):proton symporter, which likely mediates zinc ion uptake. Purified ZntB reconstituted in liposomes also binds and transports Cd(2+), Ni(2+) and Co(2+).
Subcellular location: Cell inner membrane {ECO:0000255|HAMAP-Rule:MF_01565, ECO:0000269|PubMed:15919996, ECO:0000269|PubMed:29101379}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_01565, ECO:0000269|PubMed:29101379}.
Interaction partners:
- Zinc transporter ZitB
- Cation-efflux pump FieF
Sequence:
MEAIKGSDVNVPDAVFAWMLDGRGGVKPLENTDVIDEAHPCWLHLNYVHHDSAQWLATTPLLPNNVRDALAGESTRPRVSRLGEGTLITLRCINGSTDERPDQLVAMRVYMDGRLIVSTRQRKVLALDDVVSDLEEGTGPTDCGGWLVDVCDALTDHSSEFIEQLHDKIIDLEDNLLDQQIPPRGFLALLRKQLIVMRRYMAPQRDVYARLASERLPWMSDDQRRRMQDIADRLGRGLDEIDACIARTGVMADEIAQVMQENLARRTYTMSLMAMVFLPSTFLTGLFGVNLGGIPGGGWQFGFSIFCILLVVLIGGVALWLHRSKWL
Protein: Alpha/beta-Hydrolases superfamily protein (F4KBJ3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Ankyrin repeat family protein
- Ankyrin repeat family protein
- RHOMBOID-like protein 9, chloroplastic
- NADH dehydrogenase 1 alpha subcomplex assembly factor 3
- Coatomer subunit epsilon-2
Sequence:
MRALTWTAMSPPVMSRTATSTVNLRRISLRRDRVCVRATASSSATVSGGGVVEAVELAEIGERSKKWKWKGEYSVNYFVKDSPEEVTPASQTVLLVHGFGASIPHWRRNINALSKNHTVYAIDLLGFGASDKPPGFSYTMESWAELILNFLEEVVQKPTILIGNSVGSLACVIAASGTKFLIYLEKKTESRGDLVKGLVLLNCAGGMNNKAVFDDWRIKLLMPLLLLIDFLLKQRGIASALFNRVKDRENLKNILTNVYGNKDNVDDTLVEIIAGPANTEGALDAFVSILTGPPGPNPIKLIPEITKPVLVLWGDQDGLTPLDGPVGKYFTSLPDQLPNFNLYVLQGVGHCPQDDRPDLVHERLLPWLAQLSST
Protein: Ubiquitin-protein ligase E3A (EC 2.3.2.26) (E6AP ubiquitin-protein ligase) (HECT-type ubiquitin transferase E3A) (Human papillomavirus E6-associated protein) (Oncogenic protein-associated protein E6-AP) (Renal carcinoma antigen NY-REN-54) (Q05086)
Organism: Homo sapiens (Human)
Function: E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and transfers it to its substrates. Several substrates have been identified including the BMAL1, ARC, RAD23A and RAD23B, MCM7 (which is involved in DNA replication), annexin A1, the PML tumor suppressor, and the cell cycle regulator CDKN1B. Additionally, may function as a cellular quality control ubiquitin ligase by helping the degradation of the cytoplasmic misfolded proteins. Finally, UBE3A also promotes its own degradation in vivo. Plays an important role in the regulation of the circadian clock: involved in the ubiquitination of the core clock component BMAL1, leading to its proteasomal degradation. Acts as transcriptional coactivator of progesterone receptor PGR upon progesterone hormone activation. Acts as a regulator of synaptic development by mediating ubiquitination and degradation of ARC (By similarity). Synergizes with WBP2 in enhancing PGR activity.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:O08759}. Nucleus {ECO:0000250|UniProtKB:O08759}.
Interaction partners:
- Cellular tumor antigen p53
- 26S proteasome non-ATPase regulatory subunit 4
- Ubiquitin-conjugating enzyme E2 D1
- Ubiquitin-conjugating enzyme E2 D2
- Tuberin
- Protein scribble homolog
- Disks large homolog 1
- UV excision repair protein RAD23 homolog A
- Catenin beta-1
- Transcriptional repressor NF-X1
Sequence:
MEKLHQCYWKSGEPQSDDIEASRMKRAAAKHLIERYYHQLTEGCGNEACTNEFCASCPTFLRMDNNAAAIKALELYKINAKLCDPHPSKKGASSAYLENSKGAPNNSCSEIKMNKKGARIDFKDVTYLTEEKVYEILELCREREDYSPLIRVIGRVFSSAEALVQSFRKVKQHTKEELKSLQAKDEDKDEDEKEKAACSAAAMEEDSEASSSRIGDSSQGDNNLQKLGPDDVSVDIDAIRRVYTRLLSNEKIETAFLNALVYLSPNVECDLTYHNVYSRDPNYLNLFIIVMENRNLHSPEYLEMALPLFCKAMSKLPLAAQGKLIRLWSKYNADQIRRMMETFQQLITYKVISNEFNSRNLVNDDDAIVAASKCLKMVYYANVVGGEVDTNHNEEDDEEPIPESSELTLQELLGEERRNKKGPRVDPLETELGVKTLDCRKPLIPFEEFINEPLNEVLEMDKDYTFFKVETENKFSFMTCPFILNAVTKNLGLYYDNRIRMYSERRITVLYSLVQGQQLNPYLRLKVRRDHIIDDALVRLEMIAMENPADLKKQLYVEFEGEQGVDEGGVSKEFFQLVVEEIFNPDIGMFTYDESTKLFWFNPSSFETEGQFTLIGIVLGLAIYNNCILDVHFPMVVYRKLMGKKGTFRDLGDSHPVLYQSLKDLLEYEGNVEDDMMITFQISQTDLFGNPMMYDLKENGDKIPITNENRKEFVNLYSDYILNKSVEKQFKAFRRGFHMVTNESPLKYLFRPEEIELLICGSRNLDFQALEETTEYDGGYTRDSVLIREFWEIVHSFTDEQKRLFLQFTTGTDRAPVGGLGKLKMIIAKNGPDTERLPTSHTCFNVLLLPEYSSKEKLKERLLKAITYAKGFGML
Protein: Serine/threonine-protein kinase MARK1 (EC 2.7.11.1) (EC 2.7.11.26) (MAP/microtubule affinity-regulating kinase 1) (O08678)
Organism: Rattus norvegicus (Rat)
Function: Serine/threonine-protein kinase (By similarity). Involved in cell polarity and microtubule dynamics regulation. Phosphorylates DCX, MAP2 and MAP4. Phosphorylates the microtubule-associated protein MAPT/TAU (By similarity). Involved in cell polarity by phosphorylating the microtubule-associated proteins MAP2, MAP4 and MAPT/TAU at KXGS motifs, causing detachment from microtubules, and their disassembly. Involved in the regulation of neuronal migration through its dual activities in regulating cellular polarity and microtubule dynamics, possibly by phosphorylating and regulating DCX. Also acts as a positive regulator of the Wnt signaling pathway, probably by mediating phosphorylation of dishevelled proteins (DVL1, DVL2 and/or DVL3).
Subcellular location: Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:9108484}. Cytoplasm {ECO:0000250|UniProtKB:Q9P0L2}. Cell projection, dendrite {ECO:0000250|UniProtKB:Q9P0L2}. Note=Appears to localize to an intracellular network.
Interaction partners:
Sequence:
MSARTPLPTVNERDTENHTSVDGYTETHIPPTKSSSRQNIPRCRNSITSATDEQPHIGNYRLQKTIGKGNFAKVKLARHVLTGREVAVKIIDKTQLNPTSLQKLFREVRIMKILNHPNIVKLFEVIETEKTLYLVMEYASGGEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKCIVHRDLKAENLLLDADMNIKIADFGFSNEFTVGNKLDTFCGSPPYAAPELFQGKKYDGPEVDVWSLGVILYTLVSGSLPFDGQNLKELRERVLRGKYRVPFYMSTDCENLLKKLLVLNPIKRGSLEQIMKDRWMNVGHEEEELKPYSEPELDLNDAKRIDIMVTMGFARDEINDALVSQKYDEVMATYILLGRKPPEFEGGESLSSGNLCQRSRPSSDLNNSTLQSPAHLKVQRSISANQKQRRFSDHAGPSIPPAVSYTKRPQANSVESEQKEEWDKDTARRLGSTTVGSKSEVTASPLVGPDRKKSSAGPSNNVYSGGSMTRRNTYVCERSTDRYAALQNGRDSSLTEMSASSMSSTGSTVASAGPSARPRHQKSMSTSGHPIKVTLPTIKDGSEAYRPGTAQRVPAASPSAHSISASTPDRTRFPRGSSSRSTFHGEQLRERRSAAYSGPPASPSHDTAALAHARRGTSTGIISKITSKFVRRDPSEGEASGRTDTARGSSGEPKDKEEGKEAKPRSLRFTWSMKTTSSMDPNDMVREIRKVLDANTCDYEQRERFLLFCVHGDARQDSLVQWEMEVCKLPRLSLNGVRFKRISGTSIAFKNIASKIANELKL
Protein: Complex I assembly factor TMEM126B, mitochondrial (Transmembrane protein 126B) (Q8IUX1)
Organism: Homo sapiens (Human)
Function: As part of the MCIA complex, involved in the assembly of the mitochondrial complex I. Participates in constructing the membrane arm of complex I.
Subcellular location: Mitochondrion membrane {ECO:0000269|PubMed:24191001}; Multi-pass membrane protein {ECO:0000269|PubMed:24191001}.
Interaction partners:
- Complex I intermediate-associated protein 30, mitochondrial
- Complex I assembly factor ACAD9, mitochondrial
- Evolutionarily conserved signaling intermediate in Toll pathway, mitochondrial
- Complex I assembly factor TIMMDC1, mitochondrial
- NADH dehydrogenase 1 alpha subcomplex subunit 13
- NADH dehydrogenase 1 subunit C2
- Transmembrane protein 186
- NADH dehydrogenase 1 alpha subcomplex assembly factor 4
- NADH dehydrogenase 1 alpha subcomplex assembly factor 3
- NADH dehydrogenase iron-sulfur protein 3, mitochondrial
Sequence:
MVVFGYEAGTKPRDSGVVPVGTEEAPKVFKMAASMHGQPSPSLEDAKLRRPMVIEIIEKNFDYLRKEMTQNIYQMATFGTTAGFSGIFSNFLFRRCFKVKHDALKTYASLATLPFLSTVVTDKLFVIDALYSDNISKENCVFRSSLIGIVCGVFYPSSLAFTKNGRLATKYHTVPLPPKGRVLIHWMTLCQTQMKLMAIPLVFQIMFGILNGLYHYAVFEETLEKTIHEE
Protein: Photosystem I iron-sulfur center (EC 1.97.1.12) (9 kDa polypeptide) (PSI-C) (Photosystem I subunit VII) (PsaC) (P62090)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Apoprotein for the two 4Fe-4S centers FA and FB of photosystem I (PSI); essential for photochemical activity. FB is the terminal electron acceptor of PSI, donating electrons to ferredoxin. The C-terminus interacts with PsaA/B/D and helps assemble the protein into the PSI complex. Required for binding of PsaD and PsaE to PSI. PSI is a plastocyanin-ferredoxin oxidoreductase, converting photonic excitation into a charge separation, which transfers an electron from the donor P700 chlorophyll pair to the spectroscopically characterized acceptors A0, A1, FX, FA and FB in turn.
Subcellular location: Plastid, chloroplast thylakoid membrane {ECO:0000255|HAMAP-Rule:MF_01303}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_01303}; Stromal side {ECO:0000255|HAMAP-Rule:MF_01303}.
Interaction partners:
- Photosystem I reaction center subunit VIII
- NAD
- Photosystem I P700 chlorophyll a apoprotein A2
- Photosystem I reaction center subunit II-2, chloroplastic
- Photosystem I reaction center subunit IX
- Photosystem I reaction center subunit III, chloroplastic
- Photosystem I reaction center subunit V, chloroplastic
- NAD
- Photosystem I reaction center subunit IV A, chloroplastic
- Photosystem I P700 chlorophyll a apoprotein A1
Sequence:
MSHSVKIYDTCIGCTQCVRACPTDVLEMIPWDGCKAKQIASAPRTEDCVGCKRCESACPTDFLSVRVYLWHETTRSMGLAY
Protein: Galectin (Q8I4A4)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MPSVWHCAKYINIPYRSKLTERIEPGQTLIIRGKTIDESKRFNINLHKDSPDFSGNDVPLHLSIRFDEGKIVYNAYTKGTWGKEERAKNPIKKGDDFDIRIRAHDSKFQVSINHKEVKNFEHRIPLNSVSHLSIDGDVVLNHVQWGGKYYPVPYESGIAADGLVPGKTLVVYGTPEKKAKKFNINLLKKNGDIALHFNPRFDEKANGFMCAKPTPGKDYDPFIETNESVVRNSLVNGEWGNEEREGKNPFERLTAFDLEIRNEEFAFQIFVNGERFASYAHRVDPHDIAGLQIQGDIELTGIQVVNNQPAQE
Protein: RIC3 acetylcholine receptor chaperone, isoform O (E1JGQ0)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004586}.
Interaction partners:
Sequence:
MPATATSKPRAPLVEEGMTPKKTALIIVTVIGCIAILWPKVFHPMMFGGVPPSQPNFKDPRAAPGGLRQERPAHLHPESIYQAMRERGRAIPATPTVPILERKTSPSNPPPRIVDGRPGPIPGMRPPMGAGALHQPQQRGSSMGFLMPLYTIGIVVFFGYTLMKIMFKKQVPNDPYGAAPPNPAFRQEVFGSQNHSQVEDLGGSKLVVTAIQGLIDAADEQLNGQDKQRATSDTETDSNKKNDNEKTREQPLDKQNLSNGHASSTDQNPEQETVAKGARKRRDLSAEQELTVLGMELTASCEGGHKWTGRPPTPVFRAPSEHSKLEDNLPEPQSIYLEGALAHESQILVADSQIKREEVYDSELNGSAEEPAIILSSRMTLSLINLDANQQNGNAGKSAVESPLADDIEIIGHDEQ
Protein: Large ribosomal subunit protein eL28 (60S ribosomal protein L28) (Q9VZS5)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Large ribosomal subunit protein uL30
- Small ribosomal subunit protein eS25
- Small ribosomal subunit protein eS6
- Small ribosomal subunit protein uS9
- Small ribosomal subunit protein eS8
- Large ribosomal subunit protein eL29
- Large ribosomal subunit protein eL31
- Small ribosomal subunit protein eS1
- Small ribosomal subunit protein eS12
- Large ribosomal subunit protein eL18
Sequence:
MATSSHLNWLIIRNNNAFLLKKRDVKKPFSTEPNNLASVSSYRYSGIVHKKTLGVVPAADKKGFTAVLKKGKYAQRPAKNTVRVDFKAGPRRSLKKLKNLLIGSKYRKDLTQAALRRASAVLRSQKPAPVKGKKAEFAKGKKPE
Protein: Cilia- and flagella-associated protein 410 (Q8C6G1)
Organism: Mus musculus (Mouse)
Function: Plays a role in cilia formation and/or maintenance. Plays a role in the regulation of cell morphology and cytoskeletal organization (By similarity). Involved in DNA damage repair (By similarity).
Subcellular location: Cell projection, cilium {ECO:0000269|PubMed:26294103, ECO:0000269|PubMed:26974433, ECO:0000269|PubMed:27548899}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000269|PubMed:26167768, ECO:0000269|PubMed:26294103}. Mitochondrion {ECO:0000250|UniProtKB:O43822}. Cell projection, cilium, photoreceptor outer segment {ECO:0000250|UniProtKB:O43822}. Cytoplasm {ECO:0000250|UniProtKB:O43822}. Note=Localized to the connecting cilium of the cone and rod photoreceptors (PubMed:26974433, PubMed:27548899). Colocalizes with NEK1 and SPATA7 at the basal body (By similarity). {ECO:0000250|UniProtKB:O43822, ECO:0000269|PubMed:26167768, ECO:0000269|PubMed:26974433, ECO:0000269|PubMed:27548899}.
Interaction partners:
Sequence:
MKLTRKMVLSRAKASELHNVRKLNCWGSQLTDISICREMPSLEVITLSVNSVSTLEPVRSCRRLSELYLRRNRIPSLNELFYLKDLPHLRVLWLAENPCCGTSPHLYRMTVLRNLPHLQKLDNQAVTEEELTRALMEGDEITAAPHREGAGNGCPKPPYALNSVSSATETSQHLLSYTEETEVQGQTTTDQSPSFSPRDTMRSHKNRNILTAILLLLRELDTEGLETVQQTVGSRLQALHRPEPQEDME
Protein: Mediator of RNA polymerase II transcription subunit 8 (Cell separation protein sep15) (Mediator complex subunit 8) (O94646)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Mediator of RNA polymerase II transcription subunit 22
- Mediator of RNA polymerase II transcription subunit 18
- Mediator of RNA polymerase II transcription subunit 6
- Mediator of RNA polymerase II transcription subunit 20
- Mediator of RNA polymerase II transcription subunit 31
- Mediator of RNA polymerase II transcription subunit 11
- Mediator of RNA polymerase II transcription subunit 17
- Mediator of RNA polymerase II transcription subunit 7
- Mediator of RNA polymerase II transcription subunit 10
- Mediator of RNA polymerase II transcription subunit 27
Sequence:
MEDISTEKTVESLEAIRHRIAQIVQSLTHFLAILHQSESLSPWPTIHKNFNILLSQIHSLSNNLAAHSHTLQTTSIYPSLEFPVKEQEPLLTTLLRTKALPEVEEWEANTLQEYEASISSQPKKKEANDAYQKDQLWDQARIIFMEERENYSWFDFVTRRQESEGEFVSQRQLEIDRATEEQNANQMLTDILSFMKSGKR
Protein: DNA gyrase subunit B (EC 5.6.2.2) (C5C7X8)
Organism: Micrococcus luteus (strain ATCC 4698 / DSM 20030 / JCM 1464 / CCM 169 / CCUG 5858 / IAM 1056 / NBRC 3333 / NCIMB 9278 / NCTC 2665 / VKM Ac-2230) (Micrococcus lysodeikticus)
Function: A type II topoisomerase that negatively supercoils DNA in an ATP-dependent manner. About 140 bp of DNA wraps around gyrase in the presence or absence of ATP, when ATP is added negative supercoils are made.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01898, ECO:0000269|PubMed:276855}.
Interaction partners:
- DNA gyrase subunit A
- DNA topoisomerase
- DNA replication and repair protein RecF
- DNA-directed RNA polymerase subunit beta
- Beta sliding clamp
- Protein RecA
- ATP synthase subunit beta
- DNA-directed RNA polymerase subunit beta'
- Tryptophan synthase beta chain
- Translation initiation factor IF-2
Sequence:
MVDAMPENPAEEPTAASAAPNPEAVPDAVGQPEAPVKDRKVPGEYGASAITVLEGLEAVRKRPGMYIGSTGPRGLHHLVYEVVDNSVDEALAGYATGIDVTLQADGGVRVADDGRGIPVDLHPTEGRPTVEVVMTILHAGGKFGGGGYAVSGGLHGVGISVVNALSRRVDTEVRRQGHVWRMSFADGGVPQGELVKGEATDATGTVQTFYPDAEIFDSIEFDYETLRARFQQMAFLNKGLRITLTDERVQESNEVVDDEIAGEGAAGEDVAENGLAEDAEQEPQRRSVTYLYENGLLDYVQHLNSAKKVEYVHDDVIAFEAEDFSDGRSMAVEVAMQWTSAYSESVHTYANTINTHEGGTHEEGFRAALTSLVNRYAREKEILKPKEDNLSGEDIREGLTAVISVKLSEPQFEGQTKTKLGNSEARGFVSKAVTDHLGDWFERNPGPAKEIIRKAIMASHARLAARKARDNARRKSPLESFGMPGKLADCSSKDPERCEVYIVEGDSAGGSAKQGRNPETQAILPLRGKILNVERARLDKALGNAEIQSMITAFGTNIGEEFDISKLRYHKIVLMADADVDGQHITTLLLTVLFRYMRPLIEAGHVFLAQPPLYRIKWSNAPHDYVFSDEERDAAVEAGLAKGWRYPKDNGVQRYKGLGEMNYQELWDTTMDPEHRTLLQVTMEDAAAADAVFSMLMGEDVESRRTFIQQNAKDIRFLDV
Protein: Calcium-transporting ATPase 8, plasma membrane-type (EC 7.2.2.10) (Ca(2+)-ATPase isoform 8) (Q9LF79)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: This magnesium-dependent enzyme catalyzes the hydrolysis of ATP coupled with the translocation of calcium from the cytosol out of the cell.
Subcellular location: Cell membrane; Multi-pass membrane protein.
Interaction partners:
- Calmodulin-7
- AAA-ATPase At3g28540
- AAA-ATPase At1g43910
Sequence:
MTSLLKSSPGRRRGGDVESGKSEHADSDSDTFYIPSKNASIERLQQWRKAALVLNASRRFRYTLDLKKEQETREMRQKIRSHAHALLAANRFMDMGRESGVEKTTGPATPAGDFGITPEQLVIMSKDHNSGALEQYGGTQGLANLLKTNPEKGISGDDDDLLKRKTIYGSNTYPRKKGKGFLRFLWDACHDLTLIILMVAAVASLALGIKTEGIKEGWYDGGSIAFAVILVIVVTAVSDYKQSLQFQNLNDEKRNIHLEVLRGGRRVEISIYDIVVGDVIPLNIGNQVPADGVLISGHSLALDESSMTGESKIVNKDANKDPFLMSGCKVADGNGSMLVTGVGVNTEWGLLMASISEDNGEETPLQVRLNGVATFIGSIGLAVAAAVLVILLTRYFTGHTKDNNGGPQFVKGKTKVGHVIDDVVKVLTVAVTIVVVAVPEGLPLAVTLTLAYSMRKMMADKALVRRLSACETMGSATTICSDKTGTLTLNQMTVVESYAGGKKTDTEQLPATITSLVVEGISQNTTGSIFVPEGGGDLEYSGSPTEKAILGWGVKLGMNFETARSQSSILHAFPFNSEKKRGGVAVKTADGEVHVHWKGASEIVLASCRSYIDEDGNVAPMTDDKASFFKNGINDMAGRTLRCVALAFRTYEAEKVPTGEELSKWVLPEDDLILLAIVGIKDPCRPGVKDSVVLCQNAGVKVRMVTGDNVQTARAIALECGILSSDADLSEPTLIEGKSFREMTDAERDKISDKISVMGRSSPNDKLLLVQSLRRQGHVVAVTGDGTNDAPALHEADIGLAMGIAGTEVAKESSDIIILDDNFASVVKVVRWGRSVYANIQKFIQFQLTVNVAALVINVVAAISSGDVPLTAVQLLWVNLIMDTLGALALATEPPTDHLMGRPPVGRKEPLITNIMWRNLLIQAIYQVSVLLTLNFRGISILGLEHEVHEHATRVKNTIIFNAFVLCQAFNEFNARKPDEKNIFKGVIKNRLFMGIIVITLVLQVIIVEFLGKFASTTKLNWKQWLICVGIGVISWPLALVGKFIPVPAAPISNKLKVLKFWGKKKNSSGEGSL
Protein: Charged multivesicular body protein 1b (Q9TXI3)
Organism: Caenorhabditis elegans
Interaction partners:
- Charged multivesicular body protein 2a
- Charged multivesicular body protein 5
- Charged multivesicular body protein 3
- IST1 homolog
- vesicle-fusing ATPase
- Charged multivesicular body protein 6
- Charged multivesicular body protein 7
- Charged multivesicular body protein 4b
- Vacuolar protein-sorting-associated protein 25
- Charged multivesicular body protein 2b
Sequence:
MGAGESSMALEKHLFDLKFAAKQLEKNAQRCEKDEKVEKDKLTAAIKKGNKEVAQVHAENAIRKKNEAVNYIKMAARIDAVAARVQTAATQKRVTASMSGVVKAMESAMKSMNLEKVQQLMDRFERDFEDLDVTTKTMEKTMDGTTVLNAPKSQVDALIAEAADKAGIELNQELPSNVPTALPTGTQAVSEDKDLTERLAALRNM
Protein: Cilia- and flagella-associated protein 58 (Flagellum-associated protein 58) (A8HUA1)
Organism: Chlamydomonas reinhardtii (Chlamydomonas smithii)
Subcellular location: Cell projection, cilium, flagellum {ECO:0000269|PubMed:15998802}.
Interaction partners:
Sequence:
MASDFSTGLHGGHHETLEQYNKVLEELAADAVMDPFRVEYEKLHRALRKTYESQARLAKKCQELNSDISLNASKVQSALKLNEEDRETAVALKREINKAWKMVDDSTVKETKAKETAQQLKVEIANLSRLVEEGAGLAIGEETALNELLKQKEELARERDAQVEQLMKYRSDLMETQEKLRAADAEKLQLDADIQHLRGTINDKKAEAEREIRKKERMEKEMKELRQQLEIRSSEIKSKQLQVTSTEEQVARLEQMLRDAKFATEKVQKEYNMLNERMQKLHHDLEEQIHTNTQLLTENSAKQVELRVKEEEISGIKQEASRVNKLREQTVKKTKQLEEQRVEVEKERDVLRAELAALERELEAKQKEVDVEKKKLEELTRERDAENATQKQIDLVKINENAKRNLEQEIQGYKMEAQKQSKLIYQLEKEREKYDLEAAEAANKYQQAQSEVKLRVDAIMDLQRRIAEGESKLKQQQNLYEAVRADRNLYSKNLIEAQDEIQEMKRKFKIMQHQIEQLKEEITGKDLYLLKEHFEHQKVINEKEQLRNELDRSKSNIKEADSAINAQKVEIDKLNHIINEADQERRRQKKEYDIVVNERDILGTQLVRRNDELAALYERIKIQQATLQMGQSQYRDRLAEIRQLKVRLADLKRQLHLLKSSVSNIDVLKREVHQLGRELLQERTKVKALSEELENPLNVHRWRKLEGSDPGTYEMIQKIQTLQKRLISKTEEVVEKDLLIQEKEKLYMELKNILARQPGPEVAEQLSIYQANLREKTKQMKAMASELNMYQAQVNEYKYEIERLVRELNEMKQVFFDRRKKEQADRARTMKASMYGPSLLDQLPGGSGTGSGGMATGGGVGMS
Protein: DNA polymerase eta (Q38C71)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- DNA damage repair protein, putative
- Proliferating cell nuclear antigen
- Sister chromatid cohesion protein
- Structural maintenance of chromosomes protein
- DNA polymerase
- Replication factor C, subunit 2, putative
- AAA+ ATPase domain-containing protein
- Replication factor C, subunit 1, putative
- Replication factor C, subunit 5, putative
- Replication factor C, subunit 4, putative
Sequence:
MRCIAHIDMDCFYAQVEAVRLGVDCRTEPYVLSQWGNLIAVNYPARKFGIGRFDTVTDALEKCPHVKISHVATYAAGEVEYRYHENPSKQTHKVALEPYREASRKIFRILDSFDGVEVEKGSVDEAFLDVTKAAHMKQGEMGLLSSQGELRLEDVADPTTIVIPSRQAEIAAWLKEHGREFSDVFDVTLHPQPTAENMSLLAAASRVVWTIRQKIYDELRYDCSAGIAHNKLLAKSISARHKPNQQTLLFPDCVASVMWDLPFKSIRGFGGKFGEVVRLACGGKETCREAWLHSLCAMSKFFESVGDAEYAYRRLRGYDEGKIRERSISKSLMASKAFSPPSSTANGVQKWVTVLSGELSARYEDFCNTYGVKGHSFNVKLGNRGLDQPSSVANKTFPLPELVTPQTLVSAAMQCVTAIMANRPGVVVNAVMLTIGSFKKQESDESGVRSQQTTLRDFFKLKNPGKRERNHTDEAMVITLSSCPSSPVSRESLKSTPGTRVVFDVEDDGDDEEGESGEKDVHIID
Protein: Protein TIFY 11b (OsTIFY11b) (Jasmonate ZIM domain-containing protein 10) (OsJAZ10) (OsJAZ4) (Q10QW3)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Repressor of jasmonate responses.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00768}.
Interaction partners:
- Coronatine-insensitive protein homolog 1b
- Coronatine-insensitive protein homolog 1a
- Transcription factor MYC2
- Os10g0506950 protein
- Coronatine-insensitive protein homolog 2
Sequence:
MAMEGKSRRFAVACGVLSQYVRAEQKMAAAAGAAPARAVTTLSLMPGAEVVVEEEERREVGEEEAGPATAPAAPLTIFYGGRMVVFEDFPADKAAEVMRMASSGMAAAPAQREGAALADMPIMRKASLQRFFAKRKDRLAATTPYARPSPAETKASEPEEKKTPTSWLDLAASASAAARRDSLTIAL
Protein: RE41891p (Q5BIE7)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
SQSCSSVVIGNMPRFQIKSLVFLAGLIVLVGEANSTLRRIPIQKSPNFKRSHKNIVAERDFVQQKYNRQYTANGYPMEHLSNYDNFQYYGNISIGTPGQDFLVQFDTGSSNLWVPGSSCISTACQDHQVFYKNKSSTYVANGTAFSITYGTGSVSGYLSVDCVGFAGLTIQSQTFGEVTTEQGTNFVDAYFDGILGMGFPSLAVDGVTPTFQNMMQQGLVQSPVFSFFLRDNGSVTFYGGELILGGSDPSLYSGSLTYVNVVQAAYWKFQTDYIKVGSTSISTFAQAIADTGTSLIIAPQAQYDQISQLFNANSEGLFECSSTSYPDLIININGVDFKIPAKYYVIEEEDFCSLAIQSINQDFWIMGDVFLGRIYTEFDVGNQRLGFAPVNSAVGLRKAVLWRIFTLLLACGMWKLKN
Protein: Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)] (P05877)
Organism: Human immunodeficiency virus type 1 group M subtype B (isolate MN) (HIV-1)
Function: Oligomerizes in the host endoplasmic reticulum into predominantly trimers. In a second time, gp160 transits in the host Golgi, where glycosylation is completed. The precursor is then proteolytically cleaved in the trans-Golgi and thereby activated by cellular furin or furin-like proteases to produce gp120 and gp41.
Subcellular location: [Surface protein gp120]: Virion membrane {ECO:0000255|HAMAP-Rule:MF_04083}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_04083}. Host cell membrane {ECO:0000255|HAMAP-Rule:MF_04083}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_04083}. Host endosome membrane {ECO:0000255|HAMAP-Rule:MF_04083}; Single-pass type I membrane protein {ECO:0000255|HAMAP-Rule:MF_04083}. Note=The surface protein is not anchored to the viral envelope, but associates with the extravirion surface through its binding to TM. It is probably concentrated at the site of budding and incorporated into the virions possibly by contacts between the cytoplasmic tail of Env and the N-terminus of Gag. {ECO:0000255|HAMAP-Rule:MF_04083}.; SUBCELLULAR LOCATION: [Transmembrane protein gp41]: Virion membrane {ECO:0000255|HAMAP-Rule:MF_04083}; Single-pass type I membrane protein {ECO:0000255|HAMAP-Rule:MF_04083}. Host cell membrane {ECO:0000255|HAMAP-Rule:MF_04083}; Single-pass type I membrane protein {ECO:0000255|HAMAP-Rule:MF_04083}. Host endosome membrane {ECO:0000255|HAMAP-Rule:MF_04083}; Single-pass type I membrane protein {ECO:0000255|HAMAP-Rule:MF_04083}. Note=It is probably concentrated at the site of budding and incorporated into the virions possibly by contacts between the cytoplasmic tail of Env and the N-terminus of Gag. {ECO:0000255|HAMAP-Rule:MF_04083}.
Interaction partners:
Sequence:
MRVKGIRRNYQHWWGWGTMLLGLLMICSATEKLWVTVYYGVPVWKEATTTLFCASDAKAYDTEVHNVWATQACVPTDPNPQEVELVNVTENFNMWKNNMVEQMHEDIISLWDQSLKPCVKLTPLCVTLNCTDLRNTTNTNNSTANNNSNSEGTIKGGEMKNCSFNITTSIRDKMQKEYALLYKLDIVSIDNDSTSYRLISCNTSVITQACPKISFEPIPIHYCAPAGFAILKCNDKKFSGKGSCKNVSTVQCTHGIRPVVSTQLLLNGSLAEEEVVIRSENFTDNAKTIIVHLNESVQINCTRPNYNKRKRIHIGPGRAFYTTKNIIGTIRQAHCNISRAKWNDTLRQIVSKLKEQFKNKTIVFNQSSGGDPEIVMHSFNCGGEFFYCNTSPLFNSTWNGNNTWNNTTGSNNNITLQCKIKQIINMWQEVGKAMYAPPIEGQIRCSSNITGLLLTRDGGKDTDTNDTEIFRPGGGDMRDNWRSELYKYKVVTIEPLGVAPTKAKRRVVQREKRAAIGALFLGFLGAAGSTMGAASVTLTVQARLLLSGIVQQQNNLLRAIEAQQHMLQLTVWGIKQLQARVLAVERYLKDQQLLGFWGCSGKLICTTTVPWNASWSNKSLDDIWNNMTWMQWEREIDNYTSLIYSLLEKSQTQQEKNEQELLELDKWASLWNWFDITNWLWYIKIFIMIVGGLVGLRIVFAVLSIVNRVRQGYSPLSLQTRPPVPRGPDRPEGIEEEGGERDRDTSGRLVHGFLAIIWVDLRSLFLFSYHHRDLLLIAARIVELLGRRGWEVLKYWWNLLQYWSQELKSSAVSLLNATAIAVAEGTDRVIEVLQRAGRAILHIPTRIRQGLERALL