wanglab/gogpt-training-data huggingface dataset:
Protein: Short neuropeptide F [Cleaved into: sNPF-associated peptide (sNPF-AP); sNPF peptide 2 (sNPF-2); sNPF peptide 3 (sNPF-3); sNPF peptide 4 (sNPF-4); RLRF peptide 1; RLRF peptide 2] (Q9VIQ0)
Organism: Drosophila melanogaster (Fruit fly)
Function: Plays a role in controlling food intake and regulating body size.
Subcellular location: Secreted.
Interaction partners:
- Neuropeptide F
- GH23382p
- FMRFamide-related peptides
- Tachykinins
- Allatostatin-A
- Neuropeptide F receptor
- Adipokinetic hormone
- Drosulfakinins
- Protein PDF
- Eclosion hormone
Sequence:
MFHLKRELSQGCALALICLVSLQMQQPAQAEVSSAQGTPLSNLYDNLLQREYAGPVVFPNHQVERKAQRSPSLRLRFGRSDPDMLNSIVEKRWFGDVNQKPIRSPSLRLRFGRRDPSLPQMRRTAYDDLLERELTLNSQQQQQQLGTEPDSDLGADYDGLYERVVRKPQRLRWGRSVPQFEANNADNEQIERSQWYNSLLNSDKMRRMLVALQQQYEIPENVASYANDEDTDTDLNNDTSEFQREVRKPMRLRWGRSTGKAPSEQKHTPEETSSIPPKTQN
Protein: Ribosome biogenesis protein WDR12 (WD repeat-containing protein 12) (Q9JJA4)
Organism: Mus musculus (Mouse)
Function: Component of the PeBoW complex, which is required for maturation of 28S and 5.8S ribosomal RNAs and formation of the 60S ribosome.
Subcellular location: Nucleus, nucleolus {ECO:0000255|HAMAP-Rule:MF_03029}. Nucleus, nucleoplasm {ECO:0000255|HAMAP-Rule:MF_03029}.
Interaction partners:
- Pescadillo homolog
- Ribosome biogenesis protein BOP1
- 60S ribosome subunit biogenesis protein NIP7 homolog
- Ribosomal L1 domain-containing protein 1
- GTP-binding protein 4
- MKI67 FHA domain-interacting nucleolar phosphoprotein
- ATP-dependent RNA helicase DDX18
- Nucleolar complex protein 2 homolog
- mRNA turnover protein 4 homolog
- WD repeat-containing protein 74
Sequence:
MAQLQARFYSENKKYAVDDVPFSIPAAAEVADLSNIINKLLETKNELHKHVEFDFLIKGQFLRVPLVKHMELENISSEEVVELEYVEKYTAPQPEQCMFHDDWISSIEGAEEWILSGSYDKTSRIWSLEGKSIMTIVGHTDVVKDVAWVKKDSLSCLLLTASMDQTVLLWEWNVEKNKVKALHCCRGHAGSVDAIAVDSSGAKFCSGSWDKMLKIWSTVPTDEEDEMEEATNRPRKKQKTEQLGLTRTPLVTLSGHTEAISSVLWSDAEEICSASWDHTIRVWDVESGGLKSTLTGNKVFNCISYSPLCKRLASGSTDRHIRLWDPRTKDGSLVSLSLTSHTGWVTSVKWSPTHEQQLISGSLDNIVKLWDTRSCKAPLYDLAAHEDKVLSVDWTDTGLLLSGGADNKLYSYSYSPTTSHVGA
Protein: Defective in cullin neddylation protein (Q57US7)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Ubiquitin-conjugating enzyme E2, putative
- Cullin, putative
- Cullin, putative
- Cullin, putative
- Ubiquitin, putative
- NEDD8-activating enzyme E1 catalytic subunit
- Cullin 1, putative
- COP9 signalosome complex subunit 5
- TATA-binding protein interacting
Sequence:
MVTGDMSTTVTGLDPHKMARRASRFVSSVKASTGTASSTGRTEMERYFENFASMDSAEGLETIGPKGIQHLCEDLAIKRDSFEMYTLIWKLGITRGGCIPRSDWLNMVYNYNIEVPVELKRRLREWVKDARGPSFVEFYSELYDYIRGDSARMMLPETAARAWDVLFRGDQQVAQWIRWYTGFYDCEVTRDIWRHVALFFNTGENATPYRKEDAWPTAFDLFAEWRETCETP
Protein: Armadillo repeat-containing protein 6 (Q6NXE6)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MSERCCSRYSSGASIGCTPTSTQAKMVSKRIAQETFDAAVRENIEEFAMGPEEAVKEAVEQFESQGVDLSNIVKTAPKVSADGSQEPTHDILQMLSDLQESVASSRPQEVSAYLTRFCDQCKQDKACRFLAAQKGAYPIIFTAWKLATAGDQGLLLQSLNALSVLTDGQPDLLDAQGLQLLVATLTQNADEADLTCSGIRCVRHACLKHEQNRQDLVKAGVLPLLTGAITHHGHHTDVVREACWALRVMTFDDDIRVPFGHAHNHAKMIVQENKGLKVLIEATKAFLDNPGILSELCGTLSRLAIRNEFCQEVVDLGGLSILVSLLADCNDHQMRDQSGVQELVKQVLSTLRAIAGNDDVKDAIVRAGGTESIVAAMTQHLTSPQVCEQSCAALCFLALRKPDNSRIIVEGGGAVAALQAMKAHPQKAGVQKQACMLIRNLVAHGQAFSKPILDLGAEALIMQARSAHRDCEDVAKAALRDLGCHVELRELWTGQRGNLAP
Protein: TLC domain-containing protein (Q583F9)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MYAMTPERAREYGFVSYYNHTGSEASDKLANNITLTGEEWAQLLTSPVQFILQSGGWGGAGFDVTVLPQLLLCLPWTLAFLIFRIFAQRQLSRFGLWLQVVVPKDGSKATLNNAQRRKLRKFQNQVWLTVYYIISAVFGYAVQCTKPWFGLPVSESNRIALLTPHPYKPDGGLMCYYQSGLGFYFSEMLALPVENDIRRSDFVEYFVHHIVTCALIVFSHCSYEHRFGVYVLFIHDASDIMLAAGKVINYVVSAEGKRAQRLKNNGGGDKQTKAKPSLLYRVIFNEITVNVCFALFTLFFVFFRLVCLPYLALANIVYGVKIRMFTGSYCLLIILLQGVLQGLHVYWFTLIMKIAINSLTGKRVDDIRSEDDDDGDGVEGQAVPKNSKPHRE
Protein: Homogentisate prenyltransferase (F4J8K0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Plastid, chloroplast membrane {ECO:0000256|ARBA:ARBA00004508}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004508}.
Interaction partners:
Sequence:
MELSISQSPRVRFSSLAPRFLAASHHHRPSVHLAGKFISLPRDVRFTSLSTSRMRILAVALTFKSRCVYVNYEIPKDQILVGAAESDDPVLDRIARFQNACWRFLRPHTIRGTALGSTALVTRALIENTHLIKWSLVLKALSGLLALICGNGYIVGINQIYDIGIDKVNKPYLPIAAGDLSVQSAWLLVIFFAIAGLLVVGFNFGPFITSLYSLGLFLGTIYSVPPLRMKRFPVAAFLIIATVRGFLLNFGVYHATRAALGLPFQWSAPVAFITSFVTLFALVIAITKDLPDVEGDRKFQISTLATKLGVRNIAFLGSGLLLVNYVSAISLAFYMPQVFRGSLMIPAHVILASGLIFQTWVLEKANYTKEAISGYYRFIWNLFYAEYLLFPFL
Protein: Retinoblastoma-like protein 2 (130 kDa retinoblastoma-associated protein) (p130) (Retinoblastoma-related protein 2) (RBR-2) (pRb2) (Q08999)
Organism: Homo sapiens (Human)
Function: Key regulator of entry into cell division. Directly involved in heterochromatin formation by maintaining overall chromatin structure and, in particular, that of constitutive heterochromatin by stabilizing histone methylation. Recruits and targets histone methyltransferases KMT5B and KMT5C, leading to epigenetic transcriptional repression. Controls histone H4 'Lys-20' trimethylation. Probably acts as a transcription repressor by recruiting chromatin-modifying enzymes to promoters. Potent inhibitor of E2F-mediated trans-activation, associates preferentially with E2F5. Binds to cyclins A and E. Binds to and may be involved in the transforming capacity of the adenovirus E1A protein. May act as a tumor suppressor.
Subcellular location: Nucleus.
Interaction partners:
- Transcription factor E2F5
- Transcription factor E2F4
- Cyclin-dependent kinase 2
- G1/S-specific cyclin-D3
- Transcription factor E2F1
- Histone deacetylase 1
- Protein lin-9 homolog
- G1/S-specific cyclin-D2
- G1/S-specific cyclin-E1
- Transcription factor E2F2
Sequence:
MPSGGDQSPPPPPPPPAAAASDEEEEDDGEAEDAAPPAESPTPQIQQRFDELCSRLNMDEAARAEAWDSYRSMSESYTLEGNDLHWLACALYVACRKSVPTVSKGTVEGNYVSLTRILKCSEQSLIEFFNKMKKWEDMANLPPHFRERTERLERNFTVSAVIFKKYEPIFQDIFKYPQEEQPRQQRGRKQRRQPCTVSEIFHFCWVLFIYAKGNFPMISDDLVNSYHLLLCALDLVYGNALQCSNRKELVNPNFKGLSEDFHAKDSKPSSDPPCIIEKLCSLHDGLVLEAKGIKEHFWKPYIRKLYEKKLLKGKEENLTGFLEPGNFGESFKAINKAYEEYVLSVGNLDERIFLGEDAEEEIGTLSRCLNAGSGTETAERVQMKNILQQHFDKSKALRISTPLTGVRYIKENSPCVTPVSTATHSLSRLHTMLTGLRNAPSEKLEQILRTCSRDPTQAIANRLKEMFEIYSQHFQPDEDFSNCAKEIASKHFRFAEMLYYKVLESVIEQEQKRLGDMDLSGILEQDAFHRSLLACCLEVVTFSYKPPGNFPFITEIFDVPLYHFYKVIEVFIRAEDGLCREVVKHLNQIEEQILDHLAWKPESPLWEKIRDNENRVPTCEEVMPPQNLERADEICIAGSPLTPRRVTEVRADTGGLGRSITSPTTLYDRYSSPPASTTRRRLFVENDSPSDGGTPGRMPPQPLVNAVPVQNVSGETVSVTPVPGQTLVTMATATVTANNGQTVTIPVQGIANENGGITFFPVQVNVGGQAQAVTGSIQPLSAQALAGSLSSQQVTGTTLQVPGQVAIQQISPGGQQQKQGQSVTSSSNRPRKTSSLSLFFRKVYHLAAVRLRDLCAKLDISDELRKKIWTCFEFSIIQCPELMMDRHLDQLLMCAIYVMAKVTKEDKSFQNIMRCYRTQPQARSQVYRSVLIKGKRKRRNSGSSDSRSHQNSPTELNKDRTSRDSSPVMRSSSTLPVPQPSSAPPTPTRLTGANSDMEEEERGDLIQFYNNIYIKQIKTFAMKYSQANMDAPPLSPYPFVRTGSPRRIQLSQNHPVYISPHKNETMLSPREKIFYYFSNSPSKRLREINSMIRTGETPTKKRGILLEDGSESPAKRICPENHSALLRRLQDVANDRGSH
Protein: INO80 complex subunit 3 (O94704)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Component of the INO80 complex which remodels chromatin by shifting nucleosomes and is involved in DNA repair.
Subcellular location: Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- INO80 complex subunit 4
- Probable actin-related protein 8
- Chromatin-remodeling complex subunit ies6
- INO80 complex subunit 1
- Actin-like protein arp5
- INO80 complex subunit 5
- Chromatin-remodeling ATPase INO80
- Actin-related protein 4
- RuvB-like helicase 2
- HMG box-containing protein C10F6.08c
Sequence:
MASVKSFKRKYLKLRKSFDSVVLETEEIEQKIAEISEVYRRILLENAHLNDLLIDMNSTVLPTPPASPPGSPYWEAKPVSHTVFLESPSDVFTLEKPIASTHRWLSKLTALSKSTNSTLSTPKSFHSPLQSRGISPSSAQSSAAVSSSRKQKRKRTSEGPSERRARKK
Protein: Palmitoyl-protein thioesterase 1 (PPT-1) (EC 3.1.2.22) (Palmitoyl-protein hydrolase 1) (P45478)
Organism: Bos taurus (Bovine)
Function: Removes thioester-linked fatty acyl groups such as palmitate from modified cysteine residues in proteins or peptides during lysosomal degradation. Prefers acyl chain lengths of 14 to 18 carbons.
Subcellular location: Lysosome {ECO:0000269|PubMed:8663305}. Secreted {ECO:0000269|PubMed:7916016}.
Interaction partners:
- Lysosomal thioesterase PPT2
- CLN6 transmembrane ER protein
- Battenin
- Enoyl-[acyl-carrier-protein] reductase, mitochondrial
- Bis
- TLC domain-containing protein.
- Long-chain-fatty-acid--CoA ligase
- Long-chain-fatty-acid--CoA ligase
- Long-chain-fatty-acid--CoA ligase ACSBG1
- Tripeptidyl-peptidase 1
Sequence:
MASSSCLWLLALAFLLGSCASLALGHLDPPAPLPLVIWHGMGDSCCNPLSMGAIKKMVEKKIPGIHVLSLEIGKTLREDVENSFFLNVNSQVTTVCQILAKDPKLQQGYNAMGFSQGGQFLRAVAQRCPSPPMVNLISVGGQHQGVFGLPRCPGESSHICDFIRKTLNAGAYNKAIQERLVQAEYWHDPIREDIYRNHSIFLADINQERGVNESYKKNLMALKKFVMVKFLNDTIVDPVDSEWFGFYRSGQAKETIPLQESTLYTQDRLGLKAMDKAGQLVFLALEGDHLQLSEEWFYAHIIPFLE
Protein: Cytochrome b6-f complex iron-sulfur subunit, chloroplastic (EC 7.1.1.6) (Plastohydroquinone:plastocyanin oxidoreductase iron-sulfur protein) (Rieske iron-sulfur protein) (ISP) (RISP) (Q7X9A6)
Organism: Triticum aestivum (Wheat)
Function: Component of the cytochrome b6-f complex, which mediates electron transfer between photosystem II (PSII) and photosystem I (PSI), cyclic electron flow around PSI, and state transitions.
Subcellular location: Plastid, chloroplast thylakoid membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. Note=The transmembrane helix obliquely spans the membrane in one monomer, and its extrinsic C-terminal domain is part of the other monomer. {ECO:0000250}.
Interaction partners:
- Cytochrome b6
- Cytochrome b6
- Cytochrome b6
- Cytochrome b/b6 N-terminal region profile domain-containing protein
- Cytochrome b-c1 complex subunit 7
- Cytochrome b6-f complex subunit 4
- Cytochrome b/b6 N-terminal region profile domain-containing protein
- Cytochrome b6
- Cytochrome b
- Complex III subunit 9
Sequence:
MASTALSTASNPTQLCRTRASSLCKPVKGLGFGRERIPRNITCMAGSISADRVPDMSKRELMNLLLLGAISLPTFGMLVPYGSFLVPAGSGSNAGGVAAKDKLGNDILVEDWLKTHGPNDRTLAQGLKGDPTYLVVESDKTLATYGINAVCTHLGCVVPWNAAENKFLCPCHGSQYNNQGKVVRGPAPLSLALVHADVDDGKVVFVPWVETDFRTGDNPWWK
Protein: Dynein light intermediate chain (Q382V5)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245, ECO:0000256|RuleBase:RU366047}.
Interaction partners:
Sequence:
MQEAQQTQSKSLFEVLGLNSSERDENHLLARRVVVVGDALSGKRTLVSRLFAAAVQQFPSSCVLLLSPIADGSENFSPYSQTTTDLNEGTRGNRDSSCGISVKPSGIVSPSCPPYDAAASSRSKAEIDGKRAPHFPHGVGIAHSFIFQRLPAGRASLVGSMDDCSSNTSGNSGGPSMFSATGSAAHSILTEYFCCDAPGALATALPTVLTLETSVVLVVVDGSSPWTLHEQIRRWYGHLKGHVAQLLRGELPKQDEVKRVRMTEQQKNFWATQEQVLGLLRNAWCEREGGVAKELVPPSSVVGDVCPLRTLIVCSKTDELEKLSRELEKSVRVSGEAVGGDTSLDADTPLRRTENQTSSPQTQAPWVTESLRSALCTGGLTLLQLVGQLLRKEAIERRSGLVGTGSSVNTTTTATSSSSVEQPQHCCKQEFLLPTSKAITTKGRVEATTGLNADGSPLAATLAGSYSTFVHPFYKSLWSFLFQVLYEFQTLHNRIGSTSALDAQSRRASQFTDSDCSDRAVRKPLVLAGDIDWHISALFHPYTFLPHGVDHVSLLNPLVASTEAINLQNIFGELGEEGVGCCGDITERRSCDESVPLRGDYMRKIETLLAANTVSTERTA
Protein: At4g13370 (Serine/arginine repetitive matrix protein, putative (DUF936)) (Q9T0K8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MASLAPGILLKLLQCMNSGTRPTGDHRSAILQVTGIVPALAGSDLWPNQGFYVQISDSLNSTYVSLSERDTDLILSNRLQLGQFIYLERLEFATPVPRAAGIRPVAGRHAFVGKPEPLIARVSNGSKRDFVIQPVSDSEYSLDPIAVYLNNRRIDDDGDSDVKPNVRQALAPVNQNEENRNQIRNQKPKTTPQRFSSPASSKRSVSSGKKNCSGAVAVTVERDPSPVVSGKGRRSASPVPSKCVVPSLAAAREENRKVAREPSIVVPSRYRQPSPNGRKMNPSPSGRRMSISPGRRLSSGLKMTPMVGDSSGKKKMAVIAAGISKVSEALVGSSAKNGNRKNWEEPLAGDGSAKNKPDHQAILRTQAAMTRRLSDANRRKSGSSSSVCEEKAKSCSSESSLLEEVSAFEGLGITYHERKWTDGSVPLDSISDELAKLGKEAMKRRDFAAKAAARALEEANANECIIRCLSKFSELSSASKVGNPLRIINEFLKIYEDVMKYSKIASENSFSLSSDQQNPISLWVEAALATNLEVVSLVKSHESPSSLKKSMPTRLSPRPSSKTDNIVGMWTDLDGLKETAKFAVNLQSEMQVWFIEFVEESLDNKNAAKRSLDGSSIAAVLSQLKQVNEWLDRVSSNQENKITTMDKIERLKRKIYGFVIHHVGSTYDNSASS
Protein: Beta-theraphotoxin-Cm1a (Beta-TRTX-Cm1a) (CcoTx-I) (Ceratotoxin-1) (CcoTx1) (P84507)
Organism: Ceratogyrus marshalli (Straighthorned baboon tarantula) (Ceratogyrus cornuatus)
Function: Inhibits many voltage-gated sodium channels and one voltage-gated calcium channel (Cav2.2/CACNA1B (IC(50)=400 nM), Nav1.2/SCN2A (IC(50)=3-70 nM), Nav1.1/SCN1A (IC(50)=523-1060 nM), Nav1.7/SCN9A (IC(50)=129.1-5120 nM), Nav1.4/SCN4A (IC(50)=263-888 nM or >10 uM) and Nav1.5/SCN5A (IC(50)=188-323 nM or >10 uM)). It acts by shifting the voltage dependence of channel activation to more depolarized potentials and by blocking the inward component of the sodium current. It shows moderate affinity for lipid bilayers. On Nav1.7/SCN9A, it has been shown to interact with the S3-S4 loop of domain DII (site 4). Is significantly more potent against Nav1.2/SCN2A than the other Nav channel subtypes. In vivo, this toxin causes general ataxia, lack of response to stimuli, and semiparalysis. After a few minutes, the mice are unable to stand, and breathing is reduced in rhythm and intensity. Symptoms gradually increase with progressive slowing of breathing and flaccid paralysis, death occurred within 10 to 20 minutes post injection. Animals remain totally flaccid, and no symptoms of excitatory neurotoxicity are observed.
Subcellular location: Secreted {ECO:0000269|PubMed:16267209}.
Interaction partners:
Sequence:
DCLGWFKSCDPKNDKCCKNYTCSRRDRWCKYDL
Protein: Enhancer of rudimentary homolog 1 (G2TRN4)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Forms part of the erh1-mmi1 complex that recruits the CCR4-NOT complex and the NURS complex to target RNAs. Suppresses the meiotic program during vegetative growth and promotes the meiotic program during mating. Recruitment of the NURS complex to target mRNAs promotes mRNA decay by engagement of the nuclear exosome, and formation of heterochromatin islands at meiotic genes silenced by the exosome. Recruitment of the CCR4-NOT complex to target RNAs promotes heterochromatin formation at RNAi-dependent heterochromatin domains (HOODs), including a subset of meiotic genes, lncRNAs and retrotransposons. Recruitment of the CCR4-NOT complex to rDNA promotes rDNA heterochromatin assembly.
Subcellular location: Nucleus {ECO:0000269|PubMed:23145069, ECO:0000269|PubMed:26942678}. Cytoplasm {ECO:0000269|PubMed:23145069}. Note=Localizes to chromatin regions during vegetative growth, localizes to mei2 nuclear dots during meiosis. {ECO:0000269|PubMed:26942678}.
Interaction partners:
- Peroxisomal membrane protein pex32
- RNA binding exosome specificity factor Mmi1
- NURS complex subunit red1
- Leucine-rich repeat-containing protein sog2
- Uncharacterized protein C7D4.14c
- Guanine nucleotide-binding protein subunit beta
- Uncharacterized helicase C17H9.02
- Uncharacterized protein C16E9.15
- Meiosis-specific transcription factor mei4
- Uncharacterized protein C8F11.08c
Sequence:
MSPPPAESHIILLIQQGSDPKTRIWSDHCSLRSAIEYIVGVYQTNQAVSEKESIDVSRFFNFFDEIYDCVPLVYDRHFRAYIPHEKQWLLHHAQEYLTAARQIP
Protein: Carnitine O-acetyltransferase (Carnitine acetylase) (EC 2.3.1.137) (EC 2.3.1.7) (Carnitine acetyltransferase) (CAT) (CrAT) (Q704S8)
Organism: Rattus norvegicus (Rat)
Function: Catalyzes the reversible transfer of acyl groups from carnitine to coenzyme A (CoA) and regulates the acyl-CoA/CoA ratio. Also plays a crucial role in the transport of fatty acids for beta-oxidation. Responsible for the synthesis of short- and branched-chain acylcarnitines. Active towards some branched-chain amino acid oxidation pathway (BCAAO) intermediates. Trans-2-enoyl-CoAs and 2-methylacyl-CoAs are poor substrates.
Subcellular location: Endoplasmic reticulum {ECO:0000305}. Peroxisome {ECO:0000305}. Mitochondrion inner membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}; Matrix side {ECO:0000305}.
Interaction partners:
- Mitochondrial carnitine/acylcarnitine carrier protein
- Citrate synthase, mitochondrial
- Peroxisomal acyl-coenzyme A oxidase 1
Sequence:
MLAFAARTVVKPLGLLKPSSLMKVSGRFKAHQDALPRLPVPPLQQSLDHYLKALQPIVSEEEWAHTKQLVDEFQTSGGVGERLQKGLERRAKKMENWLSEWWLKTAYLQFRQPVVIYSSPGVLLPKQDFMDLQGQLRFAAKLIEGVLDFKSMIDNETLPVEFLGGQPLCMNQYYQILSSCRVPGLKQDSVVNFLKSKKPPTHITVVHNYQFFELDVYHSDGTPLTSDQIFVQLEKIWNSSLQSNKEPVGILTSNHRNSWAKAYSSLIKDKVNRESVNSIQKSIFTVCLDKQVPRVSDDVYRSHVAGQMLHGGGSKFNSGNRWFDKTLQFIVAEDGSCGMVYEHAAAEGPPIVALVDHVMEYTKKPELVRSPMVPLPMPKKLRFNITPEIKNDIEKAKQNISIMIQDLDIMMLVFHHFGKDFPKSQKLSPDAFIQIALQLAYYRIYGQACATYESASLRMFHLGRTDTIRSASTDSLAFVKGMDDPKVPEQQRVELLRKAVQAHRAYTDRAIRGEAFDRHLLGLKLQAIEDLVSMPDIFMDTSYAIAMHFNLSTSQVPAKTDCVMSFGPVVPDGYGICYNPMEAHINFSVSAYNSCAETNAARMAHYLEKALLDMRTLLQNHPRAKL
Protein: GTP-binding nuclear protein Ran (Ras-related nuclear protein) (Q9VZ23)
Organism: Drosophila melanogaster (Fruit fly)
Function: GTPase involved in nucleocytoplasmic transport, participating both to the import and the export from the nucleus of proteins and RNAs. Switches between a cytoplasmic GDP- and a nuclear GTP-bound state by nucleotide exchange and GTP hydrolysis. Nuclear import receptors such as importin beta bind their substrates only in the absence of GTP-bound RAN and release them upon direct interaction with GTP-bound RAN, while export receptors behave in the opposite way. Thereby, RAN controls cargo loading and release by transport receptors in the proper compartment and ensures the directionality of the transport. Interaction with RANBP1 induces a conformation change in the complex formed by XPO1 and RAN that triggers the release of the nuclear export signal of cargo proteins. RAN (GTP-bound form) triggers microtubule assembly at mitotic chromosomes and is required for normal mitotic spindle assembly and chromosome segregation. Required for normal progress through mitosis (By similarity). GTP-bound Ran modulates both spindle and nuclear envelope assembly, supporting a role during mitosis. During oogenesis, modulates formation of Nup358-containing granules and biogenesis of the nuclear pore complex probably by mediating the transport of their components along microtubules.
Subcellular location: Nucleus {ECO:0000269|PubMed:12121620}. Nucleus envelope {ECO:0000269|PubMed:12121620}. Cytoplasm {ECO:0000269|PubMed:12121620, ECO:0000305|PubMed:12653959}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:12121620}. Note=Localizes around the microtubule spindle during mitosis. {ECO:0000269|PubMed:12121620}.
Interaction partners:
- LD26789p
- Ran GTPase-activating protein
- Exportin-1
- E3 SUMO-protein ligase RanBP2
- Importin subunit beta
- Regulator of chromosome condensation
- Elongation factor 1-alpha 1
- Elongation factor 1-alpha 2
- Nuclear pore complex protein Nup153
- Eukaryotic translation initiation factor 5A
Sequence:
MAQEGQDIPTFKCVLVGDGGTGKTTFVKRHMTGEFEKKYVATLGVEVHPLIFHTNRGAIRFNVWDTAGQEKFGGLRDGYYIQGQCAVIMFDVTSRVTYKNVPNWHRDLVRVCENIPIVLCGNKVDIKDRKVKAKSIVFHRKKNLQYYDISAKSNYNFEKPFLWLARKLVGDPNLEFVAMPALLPPEVKMDKDWQAQIERDLQEAQATALPDEDEEL
Protein: Heavy metal-associated isoprenylated plant protein 5 (AtHIP05) (Farnesylated protein 2) (AtFP2) (Q9SJL2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Heavy-metal-binding protein (By similarity). Involved in disease resistance.
Interaction partners:
- Heavy metal-associated isoprenylated plant protein 16
- Pyruvate, phosphate dikinase regulatory protein 2
- NADH dehydrogenase 1 alpha subcomplex subunit 13-B
- Heavy metal-associated isoprenylated plant protein 31
- Heavy metal-associated isoprenylated plant protein 39
- NADH dehydrogenase 1 alpha subcomplex subunit 13-A
Sequence:
MGEVQEGPKVEQEKKPAATVVPVETTDGKPKSGGGDSAAAAAPPVAAVVSAFVYKVDMHCEGCAKKIKRMVKHFDGVKDVTADTGGNKLLVVGKIDPVKLQEKLEEKTKRKVVLANPPPKVEGPVAAAVGEKKADGGDKEAAPPAPAPAAPKESVVPLKIRLHCEGCIQKIKKIILKIKGVETVAIDGAKDVVTVKGTIDVKELVPLLTKKLKRTVEPLVPAKKDDGAAENKKTEAAAPDAKKEAPSAGVNEAKKEGSDGGEKKKEVGDGGEKKKEGGDGGEKKKEAGDGGEKKKDGGGVPAPVAMVNKMDYYGYSAYPTAPMHWQEGHVYGQSYSMTGQNYPVGGQSYPGSGYNYASESYVPYAQPNVNAPGMFSDENPNGCSVM
Protein: Inward rectifier potassium channel 16 (Inward rectifier K(+) channel Kir5.1) (Potassium channel, inwardly rectifying subfamily J member 16) (Q9Z307)
Organism: Mus musculus (Mouse)
Function: Inward rectifier potassium channels are characterized by a greater tendency to allow potassium to flow into the cell rather than out of it. Their voltage dependence is regulated by the concentration of extracellular potassium; as external potassium is raised, the voltage range of the channel opening shifts to more positive voltages. The inward rectification is mainly due to the blockage of outward current by internal magnesium. KCNJ16 may be involved in the regulation of fluid and pH balance. In the kidney, together with KCNJ10, mediates basolateral K(+) recycling in distal tubules; this process is critical for Na(+) reabsorption at the tubules.
Subcellular location: Membrane {ECO:0000250|UniProtKB:Q9NPI9}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q9NPI9}. Basolateral cell membrane {ECO:0000250|UniProtKB:Q9NPI9}. Note=In kidney distal convoluted tubules, located in the basolateral membrane in the presence of KCNJ10. {ECO:0000250|UniProtKB:Q9NPI9}.
Interaction partners:
- ATP-sensitive inward rectifier potassium channel 10
- ATP-sensitive inward rectifier potassium channel 15
Sequence:
MSYYGSSYRIVNVDSKYPGYPPEHAIAEKRRARRRLLHKDGSCNVYFKHIFGEWGSYMVDIFTTLVDTKWRHMFVIFSLSYILSWLIFGSIFWLIAFHHGDLLSDPDITPCVDNVHSFTAAFLFSLETQTTIGYGYRCVTEECSVAVLTVILQSILSCIINTFIIGAALAKMATARKRAQTIRFSYFALIGMRDGKLCLMWRIGDFRPNHVVEGTVRAQLLRYSEDSEGRMTMAFKDLKLVNDQIILVTPVTIVHEIDHESPLYALDRKAVAKDNFEILVTFIYTGDSTGTSHQSRSSYIPREILWGHRFHDVLEVKRKYYKVNCLQFEGSVEVYAPFCSAKQLDWKDQQLNNLEKTSPARGSCNSDTNTRRRSFSAVAVVSSCENPEETVLSPQDECKEMPYQKALLTLNRISMESQM
Protein: Pentatricopeptide repeat-containing protein At1g12620 (Q9ASZ8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Uncharacterized protein At1g63310
- F3F19.7
- DEAD-box ATP-dependent RNA helicase 47, mitochondrial
Sequence:
MRGLIQTRLLETGTLRTALFLSCYGRVFSSVSDGKGKVSYRERLRSGIVDIKEDDAVDLFQEMTRSRPRPRLIDFSRLFSVVARTKQYDLVLDLCKQMELKGIAHNLYTLSIMINCCCRCRKLSLAFSAMGKIIKLGYEPDTVTFSTLINGLCLEGRVSEALELVDRMVEMGHKPTLITLNALVNGLCLNGKVSDAVLLIDRMVETGFQPNEVTYGPVLKVMCKSGQTALAMELLRKMEERKIKLDAVKYSIIIDGLCKDGSLDNAFNLFNEMEIKGFKADIIIYTTLIRGFCYAGRWDDGAKLLRDMIKRKITPDVVAFSALIDCFVKEGKLREAEELHKEMIQRGISPDTVTYTSLIDGFCKENQLDKANHMLDLMVSKGCGPNIRTFNILINGYCKANLIDDGLELFRKMSLRGVVADTVTYNTLIQGFCELGKLEVAKELFQEMVSRRVRPDIVSYKILLDGLCDNGEPEKALEIFEKIEKSKMELDIGIYNIIIHGMCNASKVDDAWDLFCSLPLKGVKPDVKTYNIMIGGLCKKGSLSEADLLFRKMEEDGHSPNGCTYNILIRAHLGEGDATKSAKLIEEIKRCGFSVDASTVKMVVDMLSDGRLKKSFLDMLS
Protein: Thylakoid membrane protein TERC, chloroplastic (Protein PIGMENT DEFECTIVE 149) (Protein TELLURITE RESISTANCE C) (AtTerC) (F4JZG9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Integral thylakoid membrane protein that plays a crucial role in thylakoid membrane biogenesis and thylakoid formation in early chloroplast development. Is essential for de novo synthesis of photosystem II (PSII) core proteins and required for efficient insertion of thylakoid membrane proteins, presumably via interaction with ALB3. May assist synthesis of thylakoid membrane proteins at the membrane insertion step.
Subcellular location: Plastid, chloroplast thylakoid membrane {ECO:0000269|PubMed:18429937, ECO:0000269|PubMed:24612058}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Origin of replication complex subunit 5
- Origin of replication complex subunit 2
- Origin of replication complex subunit 3
- Origin of replication complex subunit 6
- DNA replication licensing factor MCM3
- DNA replication licensing factor MCM4
- DNA replication licensing factor MCM7
- Origin of replication complex subunit 1B
- Origin of replication complex subunit 1A
- Cell division control protein 6 homolog
Sequence:
MSLASVIHHGILPPAKSDRIFLTIPVFPPDFRARGWTKSPFSLLINPSLASAANRRLSHLPPIACSRGIDQEDEEKESRELLPHKNDENATTSRSSSSVDSGGLKDYQQEETYKTSFKTVALCVGTAVAFGIGIGLKEGVGKASEFFAGYILEQSLSVDNLFVFVLVFKYFKVPLMYQNKVLTYGIAGAIVFRFTLILLGTATLQKFEAVNLLLAAVLLYSSFKLFASEEDDTDLSDNFIVKTCQRFIPVTSSYDGNRFFTKHDGILKATPLLLTVAVIELSDIAFAVDSIPAVFGVTRDPFIVLTSNLFAILGLRSLYTLISEGMDELEYLQPSIAVVLGFIGVKMILDFFGFHISTEASLGVVALSLSTGVLLSLTNKSSDS