wanglab/gogpt-training-data huggingface dataset:
Protein: FACT complex subunit SPT16 (Cell division control protein 68) (Facilitates chromatin transcription complex subunit SPT16) (Suppressor of Ty protein 16) (P32558)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the FACT complex, a general chromatin factor that acts to reorganize nucleosomes. The FACT complex is involved in multiple processes that require DNA as a template such as mRNA elongation, DNA replication and DNA repair. During transcription elongation the FACT complex acts as a histone chaperone that both destabilizes and restores nucleosomal structure. It facilitates the passage of RNA polymerase II and transcription by promoting the dissociation of one histone H2A-H2B dimer from the nucleosome, then subsequently promotes the reestablishment of the nucleosome following the passage of RNA polymerase II. Transcription elongation is promoted by the repression of transcription initiation from cryptic sites. Also acts in establishing transcription initiation complexes and promotes SPT15/TBP-binding to a TATA box. Together with replication factor-A protein (RPA), FACT may play a role in nucleosome deposition during DNA replication.
Subcellular location: Nucleus {ECO:0000269|PubMed:10413469}. Chromosome {ECO:0000269|PubMed:10413469}. Note=Colocalizes with RNA polymerase II on chromatin (PubMed:10413469, PubMed:14585989, PubMed:14739930). Recruited to actively transcribed loci (PubMed:14585989). Associates with the coding region of HTA1 (PubMed:19683497). {ECO:0000269|PubMed:10413469, ECO:0000269|PubMed:14585989, ECO:0000269|PubMed:14739930, ECO:0000269|PubMed:19683497}.
Interaction partners:
- Histone H2A.1
- Transcription elongation factor SPT4
- Cell division control protein 73
- Transcription elongation factor SPT5
- Histone H4
- RNA polymerase-associated protein LEO1
- RNA polymerase-associated protein CTR9
- FACT complex subunit POB3
- Histone H2A.2
- Histone H3
Sequence:
MEELNIDFDVFKKRIELLYSKYNEFEGSPNSLLFVLGSSNAENPYQKTTILHNWLLSYEFPATLIALVPGKVIIITSSAKAKHLQKAIDLFKDPESKITLELWQRNNKEPELNKKLFDDVIALINSAGKTVGIPEKDSYQGKFMTEWNPVWEAAVKENEFNVIDISLGLSKVWEVKDVNEQAFLSVSSKGSDKFMDLLSNEMVRAVDEELKITNAKLSDKIENKIDDVKFLKQLSPDLSALCPPNYKFNFDLLDWTYSPIIQSGKKFDLRVSARSTNDQLYGNGCILASCGIRYNNYCSNITRTFLIDPSEEMANNYDFLLTLQKEIVTNILKPGRTPKEVYESVIEYIEKTKPELVPNFTKNIGSLIGLEFRDSNFILNVKNDYRKIQRGDCFNISFGFNNLKDSQSANNYALQLADTVQIPLDETEPPRFLTNYTKAKSQISFYFNNEEEDNNKKKSSPATKVPSKPDRNSKILRTKLRGEARGGAEDAQKEQIRKENQKKLHEKLEKNGLLRFSAADANGPDSEPRQYFKKYESYVRDSQLPTNIRDLRIHVDWKSQTIILPIYGRPVPFHINSYKNGSKNEEGEYTYLRLNFNSPGSSGGISKKVEELPYEESADNQFVRSITLRSKDGDRMSETFKQIADLKKEATKREQERKALADVVQQDKLIENKTGRTKRLDQIFVRPNPDTKRVPSTVFIHENGIRFQSPLRTDSRIDILFSNIKNLIFQSCKGELIVVIHIHLKNPILMGKKKIQDVQFYREASDMSVDETGGGRRGQSRFRRYGDEDELEQEQEERRKRAALDKEFKYFADAIAEASNGLLTVENTFRDLGFQGVPNRSAVFCMPTTDCLVQLIEPPFLVINLEEVEICILERVQFGLKNFDMVFVYKDFNKPVTHINTVPIESLDFLKQWLTDMDIPYTVSTINLNWATIMKSLQDDPYQFFLDGGWNFLATGSDDEASDESEEEVSEYEASEDDVSDESAFSEDEEGSEVDDDISGDESEDYTGDESEEGEDWDELEKKAARADRGANFRD
Protein: Chloroacetanilide N-alkylformylase, ferredoxin reductase component (Ferredoxin--NAD(+) reductase) (EC 1.18.1.3) (X5CY81)
Organism: Rhizorhabdus wittichii (strain DC-6 / KACC 16600) (Sphingomonas wittichii)
Function: Component of the chloroacetanilide N-alkylformylase multicomponent enzyme system involved in the degradation of chloroacetanilide herbicides (N-alkoxyalkyl-N-chloroacetyl-substituted aniline derivatives). In vitro, catalyzes the transfers of electrons from ferredoxin (CndB1) to NADH. N-dealkylase utilizes NADH, but not NADPH, as the electron donor.
Interaction partners:
Sequence:
MAQYDVLIVGAGHGGAQAAVALRQNKFEGTIAIVGDEPELPYERPPLSKEYFSGEKSFDRILIRPATFWAERNVDMLLGKRVASVDPAGHSVTLTDGSTIGYGKLVWATGGAPRKLACSGHHLSGVHGVRTREDADRMLGEMERTTSVVVIGGGYIGLEAAAVLSKAGKKVTVLEALDRVLARVAGEALSRFYEAEHRAHGVDVQLGAKVDCIVGDDQDRVTGVQMHDGSVIPADMVIVGIGIIPAVEPLIAAGAAGGNGVDVDEYCRTSLPDIYAIGDCAMHANAFAEGARIRLESVQNANDQATTAAKHILGGTDAYHAVPWFWSNQYDLRLQTMGLSIGYDETIVRGDPANRSFSVVYLKNGRVLALDCVNAVKDYVQGKALVTGGVSPDKASLANPEIPLKTLLPA
Protein: Uncharacterized protein (Q384E3)
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:
MRALYQFVAGALFSASLFVFADGLIVATQNALPYNFLMWLPSLLMFCGMFVLCYVDAGAISNRYDLMGDGDSSRDRVFFFASVLFMVSGFAVSLWKAIDPYTNAGVPWPGASLVIQSALLIASFALLFWQKTQDSNSFL
Protein: Threonine dehydratase 1 biosynthetic, chloroplastic (EC 4.3.1.19) (SlTD1) (Threonine deaminase 1) (A0FKE6)
Organism: Solanum lycopersicum (Tomato) (Lycopersicon esculentum)
Function: Has a housekeeping role in isoleucine biosynthesis (Probable).
Subcellular location: Plastid, chloroplast {ECO:0000305}.
Interaction partners:
- ACT domain-containing protein
- ACT domain-containing protein
- Acetolactate synthase
- low-specificity L-threonine aldolase
- Acetolactate synthase
- Acetolactate synthase
- tryptophan synthase
- Uncharacterized protein
- alanine--glyoxylate transaminase
- threonine synthase
Sequence:
MEVLRFTAVKSLNSCVRPEFTAMSSVIVPISTVKVSGTRKSKKKALICAKATEILSSPATVTEPLKAEPAEAPVPLLRVSPSSLQCEPGYLLPNSPVLGTGGVTGYEYLTNILSSKVYDVAYETPLQKAPKLSERLGVNVWLKREDLQPVFSFKIRGAYNMMAKLPKEQLEKGVICSSAGNHAQGVALSAQRLGCDAVIVMPVTTPDIKWKSVKRLGATVVLVGDSYDEAQAYAKKRAESEGRTFIPPFDHPDVIVGQGTVGMEINRQLKDNIHAIFVPVGGGGLIAGIAAYLKRVAPDIKIIGVEPLDANALALSLHHGQRVMLDQVGGFADGVAVKVVGEETYRLCEELIDGVVLVGRDAICASIKDMFEEKRSILEPAGALALAGAEAYCKYYGLKGENVVAITSGANMNFDRLRLVTELADVGRQREAVLATFMPEDPGSFKKFAEMVGPMNITEFKYRYNSDKERALVLYSVGLHTILELEGMVERMESADLQTINLTDNDLVKDHLRHLMGGRTNVHNELLCRFTFPEKPGALMKFLDAFSPRWNISLFHYRAQGDTGANVLVGIQVPPDEVVEFEGRADSLGYEYAMESLNEAYQLIMH
Protein: Laminarase-resistance protein LRE1 (P25579)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Overexpression affects chitinase expression, cell separation and budding pattern, and increases trehalose accumulation and heat resistance by inhibiting protein kinase CBK1. Overexpression also suppresses temperature-induced hyperosmosensitivity and sensitivity to cell wall degrading enzymes. Overexpression of both LRE1 and PBN1 confers resistance to laminarinase.
Interaction partners:
- Serine/threonine-protein kinase CBK1
Sequence:
MPNTHTQHVQISEPNPVNTLSTPSKRGHRHRRSLAISGDFDFLKQPAAIVNLPPPQAAENCPSTAPTAVSSTLSPIRYNRFPCKTNEDAGTLDLPEPRFYPLSPKNNLQTPSPRFFISEEPSFSSPVKGVPDAIINLDDALKTRPRSFKSHRRSESAPPDLEVMVDKGNCAAGSNSMIKEEEDSLIEPESKNEYYEQKLPTALLSPLRPSLCVSEQAIDVDDSALNGSPTHHNHGMQNANARNSNTFNSLKIKGQKQRYYHYTKQLPLTVGCDSQSPKEQRSAASMTINQAMTPSSLAYTPSKLASTPATPVSFYDSNADINLESDNFPLKDNPRYAKDGYPKKCGNSQLNRVLDSDKRQDFSGESRRRRSGSPISHMQHRNLIDNMKGRRNSNTINSIFNYKSQHYEMPYDDMMKNENINAQSMPFSVNGVNNENSIGGVITRADDAPLQHSVVKSCTPDGKEEMNRLKSNDSNEYSKSEGQIRTNSQLSKDILMGEPGDMVDLSSFVNAQRKASNETGDLVFSLSQDDDALKTFHASNSAATSNESWCISDDALGKQAQDSEVRRKRKSKLGLFRHIFSRK
Protein: Ras-related protein Rab-11C (Q550H6)
Organism: Dictyostelium discoideum (Social amoeba)
Subcellular location: Membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}.
Interaction partners:
- Ras-related protein Rab-11A
- Ras-related protein Rab-11B
- Rab GDP dissociation inhibitor
- Uncharacterized protein
- Rac guanine nucleotide exchange factor B
Sequence:
MPQEEEAEYLFKIVIIGDSAVGKSNLLNRFTRNEFTEKTKATIGVDFGTKSIEIDNKTITAQCWDTAGQERFRAVTSGYYRGAVGAMIVYDITSKISFKNVTRWLNELREMAEQDILIMMVGNKSDLEMSREVPTKEAQAFAESNKISFLETSALNSTNVNQSFERLLTDIYHLVSSKKPMVVDDTQNWLVPNQGKKLTPLSDPAPQLTANTTSTHQEKKSGCC
Protein: Pre-mRNA-splicing factor 18 (PRP18 homolog) (hPRP18) (Q99633)
Organism: Homo sapiens (Human)
Function: Participates in the second step of pre-mRNA splicing.
Subcellular location: Nucleus speckle {ECO:0000250}. Note=Colocalizes with spliceosomal snRNPs. {ECO:0000250}.
Interaction partners:
- Pre-mRNA-splicing factor SLU7
- Pre-mRNA-splicing factor ATP-dependent RNA helicase PRP16
- Pre-mRNA-processing factor 17
- U5 small nuclear ribonucleoprotein 200 kDa helicase
- ATP-dependent RNA helicase DHX8
- Splicing factor YJU2
- Pre-mRNA-processing-splicing factor 8
- Pre-mRNA-splicing factor CWC25 homolog
- Cell division cycle 5-like protein
- Protein BUD31 homolog
Sequence:
MDILKSEILRKRQLVEDRNLLVENKKYFKRSELAKKEEEAYFERCGYKIQPKEEDQKPLTSSNPVLELELAEEKLPMTLSRQEVIRRLRERGEPIRLFGETDYDAFQRLRKIEILTPEVNKGLRNDLKAALDKIDQQYLNEIVGGQEPGEEDTQNDLKVHEENTTIEELEALGESLGKGDDHKDMDIITKFLKFLLGVWAKELNAREDYVKRSVQGKLNSATQKQTESYLRPLFRKLRKRNLPADIKESITDIIKFMLQREYVKANDAYLQMAIGNAPWPIGVTMVGIHARTGREKIFSKHVAHVLNDETQRKYIQGLKRLMTICQKHFPTDPSKCVEYNAL
Protein: Arginase (EC 3.5.3.1) (P39138)
Organism: Bacillus subtilis (strain 168)
Function: Involved in the catabolism of arginine.
Interaction partners:
- Ornithine aminotransferase
- Arginine decarboxylase
- Amino-acid permease RocE
- 1-pyrroline-5-carboxylate dehydrogenase
- Ornithine carbamoyltransferase
- Arginine biosynthesis bifunctional protein ArgJ
- Urease subunit beta
- Uncharacterized metallohydrolase YodQ
- Urease subunit gamma
- Urease subunit alpha
Sequence:
MDKTISVIGMPMDLGQARRGVDMGPSAIRYAHLIERLSDMGYTVEDLGDIPINREKIKNDEELKNLNSVLAGNEKLAQKVNKVIEEKKFPLVLGGDHSIAIGTLAGTAKHYDNLGVIWYDAHGDLNTLETSPSGNIHGMPLAVSLGIGHESLVNLEGYAPKIKPENVVIIGARSLDEGERKYIKESGMKVYTMHEIDRLGMTKVIEETLDYLSACDGVHLSLDLDGLDPNDAPGVGTPVVGGISYRESHLAMEMLYDAGIITSAEFVEVNPILDHKNKTGKTAVELVESLLGKKLL
Protein: Nuclear transcription factor Y subunit gamma (CAAT box DNA-binding protein subunit C) (Nuclear transcription factor Y subunit C) (NF-YC) (Transactivator HSM-1/2) (Q13952)
Organism: Homo sapiens (Human)
Function: Component of the sequence-specific heterotrimeric transcription factor (NF-Y) which specifically recognizes a 5'-CCAAT-3' box motif found in the promoters of its target genes. NF-Y can function as both an activator and a repressor, depending on its interacting cofactors.
Subcellular location: Nucleus.
Interaction partners:
- Nuclear transcription factor Y subunit alpha
- Nuclear transcription factor Y subunit beta
- MHC class II transactivator
- Huntingtin-associated protein 1
- DNA polymerase epsilon subunit 3
- DNA-binding protein REPIN1
- Inhibitor of growth protein 2
- CCAAT/enhancer-binding protein zeta
- DNA-binding protein RFXANK
- Serum paraoxonase/lactonase 3
Sequence:
MSTEGGFGGTSSSDAQQSLQSFWPRVMEEIRNLTVKDFRVQELPLARIKKIMKLDEDVKMISAEAPVLFAKAAQIFITELTLRAWIHTEDNKRRTLQRNDIAMAITKFDQFDFLIDIVPRDELKPPKRQEEVRQSVTPAEPVQYYFTLAQQPTAVQVQGQQQGQQTTSSTTTIQPGQIIIAQPQQGQTTPVTMQVGEGQQVQIVQAQPQGQAQQAQSGTGQTMQVMQQIITNTGEIQQIPVQLNAGQLQYIRLAQPVSGTQVVQGQIQTLATNAQQGQRNASQGKPRRCLKETLQITQTEVQQGQQQFSQFTDGQRNSVQQARVSELTGEAEPREVKATGNSTPCTSSLPTTHPPSHRAGASCVCCSQPQQSSTSPPPSDALQWVVVEVSGTPNQLETHRELHAPLPGMTSLSPLHPSQQLYQIQQVTMPAGQDLAQPMFIQSANQPSDGQAPQVTGD
Protein: Transcriptional regulatory protein UME1 (WD repeat-containing transcriptional modulator 3) (Q03010)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Catalytic component of the RPD3 histone deacetylase complexes RPD3C(L) and RPD3C(S) responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events.
Subcellular location: Cytoplasm. Nucleus.
Interaction partners:
- Histone deacetylase complex subunit CTI6
- Transcriptional regulatory protein PHO23
- Histone deacetylase RPD3
- Transcriptional regulatory protein RCO1
- Transcriptional regulatory protein RXT2
- Chromatin modification-related protein EAF3
- Transcriptional regulatory protein SDS3
- Transcriptional regulatory protein SIN3
- Transcriptional regulatory protein DEP1
- Transcriptional regulatory protein RXT3
Sequence:
MSTLDIAEDNKIKNEEFKIWKKSIPSLYQHISSLKPIFGSGVDESPSTLRSIVFTNDSSCNKSKGVLSVPLLYSQGSEIFEVDCIVPLGLHYKKPESISEPLVQPDYTMESQKVEQTVLIPKWEFKGETIAKMIYVDNSEINVKVIALSTNGSLAWFREGVKSPVYTMMEPSTSLSSASSGNQNKPCVDFAISNDSKTLTVTKEKHLDNENATIKLIDNSGKIGEVLRTIPVPGIKNIQEIKFLNNQIFATCSDDGIIRFWGNEIGKKPLWILNDSLDGKTTCFAASPFVDTLFMTGTSGGALKVWDIRAVIALGDADAELNINQGHNKVNELFKVHHFYSEQVSKIEFSSISPMEVVTIGGLGNVYHWNFEPVFAIYNEIHEDFQGIISDELEAESMAFYHTEGCRREIGENNKVNTVAYHKYIEDLVATVDSDGLLTVYKPFTGKVLDGSREVGAAKS
Protein: Amino acid transporter protein JHI-21 (Juvenile hormone Inducible-21, isoform A) (Juvenile hormone Inducible-21, isoform B) (Juvenile hormone Inducible-21, isoform C) (Juvenile hormone Inducible-21, isoform D) (Juvenile hormone Inducible-21, isoform E) (LD39658p) (Q9VKC2)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- alpha-glucosidase
- LD25378p
- GH08870p
- Amino acid transporter
- Amino acid transporter
Sequence:
MTDRYANGVTTSLVEPTNGCAAPGNPNPADGEEKIVLKRKLTLINGVAIIVGTIIGSGIFIAPTGVFIYTESVGSSLLIWLTCGILSTIGALCYAELGTCITRSGGDYAYLLVSFGPLVGFLRLWIALLIIRPTTQTIVALSFAHYAVKPFFPECDPPQNAVKLLAAICLTLLTTINCLSVKVSMKVQDVFTVGKLLALIMIILSGLYYMATGELENFRNPWEGIYTARNIGYAFYSGLFAFGGWNYLNFVTEELQDPYKNLPRAIWIAMPLVTSIYVLVNLAYFAVVNKPEMLSSLAVAVTFGNRVFGPLAFMVPIFVALSTFGGVNGVLFTSARLFATGAQEGHLPKFFQLFHVKQQTPIPSLIFTCLMSLLMLLTDNVYQLINYFSSVLWLSVVASIAGMLWLRHKRPDLPRPIKVHLALPITFMVSCVTLVLLPNLEEPQNLLIGIGITLAGIPFYYAFIARKKKPKCYGRLSNSVVEICRAIFNTTIIESNEAIN
Protein: Tetrahydromethanopterin S-methyltransferase subunit E (EC 7.2.1.4) (N5-methyltetrahydromethanopterin--coenzyme M methyltransferase subunit E) (P80186)
Organism: Methanothermobacter marburgensis (strain ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 / Marburg) (Methanobacterium thermoautotrophicum)
Function: Part of a complex that catalyzes the formation of methyl-coenzyme M and tetrahydromethanopterin from coenzyme M and methyl-tetrahydromethanopterin. This is an energy-conserving, sodium-ion translocating step.
Subcellular location: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Tetrahydromethanopterin S-methyltransferase subunit B
- Tetrahydromethanopterin S-methyltransferase subunit A 1
- Tetrahydromethanopterin S-methyltransferase subunit C
- Tetrahydromethanopterin S-methyltransferase subunit G
- Tetrahydromethanopterin S-methyltransferase subunit D
- Tetrahydromethanopterin S-methyltransferase subunit H
- Tetrahydromethanopterin S-methyltransferase subunit F
- Tetrahydromethanopterin S-methyltransferase subunit A 2
- Methyl-coenzyme M reductase I operon protein D
- Methyl-coenzyme M reductase I operon protein C
Sequence:
MDPMITGLGVVALMGAAATIAGAAEDLESDVGSQSNPNSQVQLAPQMGHLHRIINKAVSGEPVAYGTWCGIAGSVAFVLMNSMQLPVIMAIAIGAVIAAMVHTTYAVTSHMGRIVSQSQFNQPLFMDMLVQHLGPIAGHGFIVTFCTVGLSYLMTLPIPGFAHPFPLPLLAVLWGITIGAIGSSTGDVHYGAEREYQQYPFGGGIPVAIHGDITTKAELGARNSMDVVHFCAKYGGPLTGFAFGAIVFLSFWNTIVFGITGGIISGLIIVLLLIILNNRLEVFARNRYGPYKEEE
Protein: Complement C1q tumor necrosis factor-related protein 3 (Collagenous repeat-containing sequence 26 kDa protein) (CORS26) (Secretory protein CORS26) (Q9BXJ4)
Organism: Homo sapiens (Human)
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
Sequence:
MLWRQLIYWQLLALFFLPFCLCQDEYMESPQTGGLPPDCSKCCHGDYSFRGYQGPPGPPGPPGIPGNHGNNGNNGATGHEGAKGEKGDKGDLGPRGERGQHGPKGEKGYPGIPPELQIAFMASLATHFSNQNSGIIFSSVETNIGNFFDVMTGRFGAPVSGVYFFTFSMMKHEDVEEVYVYLMHNGNTVFSMYSYEMKGKSDTSSNHAVLKLAKGDEVWLRMGNGALHGDHQRFSTFAGFLLFETK
Protein: Type-1 angiotensin II receptor A (xAT) (Angiotensin 2 receptor, type 1-A) (Angiotensin II receptor, type 1-A) (P32303)
Organism: Xenopus laevis (African clawed frog)
Function: Receptor for angiotensin II, a vasoconstricting peptide, which acts as a key regulator of blood pressure and sodium retention by the kidney. The activated receptor in turn couples to G-alpha proteins G(q) (GNAQ, GNA11, GNA14 or GNA15) and thus activates phospholipase C and increases the cytosolic Ca(2+) concentrations, which in turn triggers cellular responses such as stimulation of protein kinase C (By similarity).
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:P30556}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P30556}.
Interaction partners:
Sequence:
MSNASTVETSDVERIAVNCSKSGMHNYIFIAIPIIYSTIFVVGVFGNSMVVIVIYSYMKMKTVASIFLMNLALSDLCFVITLPLWAAYTAMHYHWPFGNFLCKVASTAITLNLYTTVFLLTCLSIDRYSAIVHPMKSRIWRTAMVARLTCVGIWLVAFLASMPSIIYRQIYLFHDTNQTVCAIVYDSGHIYFMVGMSLAKNIVGFLIPFLIILTSYTLIGKTLKEVYRAQRARNDDIFKMIVAVVLLFFFCWIPYQVFTFLDVLIQMDVIQNCKMYDIVDTGMPITICIAYFNSCLNPFLYGFFGKNFRKHFLQLIKYIPPKMRTHASVNTKSSLVSSSLSDTKRASKKIALQMTDNEEHCK
Protein: Major vault protein (MVP) (Q5EAJ7)
Organism: Strongylocentrotus purpuratus (Purple sea urchin)
Function: Required for normal vault structure. Vaults are multi-subunit structures that may act as scaffolds for proteins involved in signal transduction. Vaults may also play a role in nucleo-cytoplasmic transport (By similarity).
Subcellular location: Cytoplasm {ECO:0000255|PROSITE-ProRule:PRU00571, ECO:0000269|PubMed:15710043, ECO:0000269|PubMed:9331335}. Nucleus {ECO:0000269|PubMed:15710043, ECO:0000269|PubMed:9331335}.
Interaction partners:
Sequence:
MASKRGSNQDESIFRIPPYYYIHVLDHNDNVTKVVVGPKTYIRQDHERVIFGPEKMITIPPRHYCIIENPVVRNDTDQVVYDNLGQVKLFHADQEIRLAREPFPLYPGEVLKQAVTALKVVQANAALRLRAILDFEDGTQKRVAGDEWLFEGPGTYIPRKEVVVDETIRATIIRPNQAIKLRARKETNDREGTARVTGEEWQVKKVGAYLPGAYEEVVDTVNAYVLTEKNALHLRATRTFVDMKGKTRKNGEEWLINMADTDAHIPDVYEEVVGVVDINTLTNRQYCVIVDPVGPDGKPQLGQKKLVKGEVSFFLQPGETLEQGIQSVFILGEDEGLILRAQESFKDANAAGAVRQPGDRWMIRGPCEYVPTVELEVVTRRKAIPLDENEGVYIRDTKTGKVRAVTGETYMLSQDEELWAKELSPAVEELLQSAKDPVAERSDRRGDRAAPRAREKTRVISFRVPHNAAVQIYDYKEKKARVVFGPELVMLGPDEQFTQLSLSGGKPKRPNVIKALCLLLGPDFCTDIITIETADHARLQLQLSYNWHFDVPDKTDVAASAKLFSVPDFIGDACKAIASRIRGAVAGVQFDDFHKNSAKIIRASVFGFDEKNKVRERFLFPQNSLVITSIDIQSVEPVDQRTRDALQKSVQLAIEITTNSQEATARHEAERLEQEARGRLERQKIMDEAEAEKSRKELLELQANSAAVESTGQAKAEAQSRAEAARIEGEAAVDQARLKAEAAKIESESELQRLTNAREAETKYVREQNALEVNKTKQMSDIETERFRNMVQSIGADTIKAMAMAGPEMQVKLLSSLGLKSTLITDGSTPINLFNTAQGLLGGFSAKRGIEHVEEED
Protein: Dynactin subunit 4 (Q54VS0)
Organism: Dictyostelium discoideum (Social amoeba)
Subcellular location: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000256|ARBA:ARBA00004300}. Cytoplasm, cytoskeleton, stress fiber {ECO:0000256|ARBA:ARBA00004529}. Cytoplasm, myofibril {ECO:0000256|ARBA:ARBA00004657}.
Interaction partners:
- Dynactin subunit 5
- Dynactin subunit 6
- Dynactin subunit 2
- Dynactin 150 kDa subunit
- F-actin-capping protein subunit beta
- F-actin-capping protein subunit alpha
- ER membrane protein complex subunit 1
- ER membrane protein complex subunit 3
- ER membrane protein complex subunit 4
- ER membrane protein complex subunit 6
Sequence:
MYSKRVENSFQFNKDLLNNNIIKYSCNCGKAYHVSELYYCSGCLKTNCKFCITEEIDCFYCPNCLEHVSSVEANLNGNRCKKCFDCPICFNILTYSASTNATTGNETFFLNCAFCKWNSINSGEKEFRFDSHSIKNSKESSESQLQFNKVLEVVNKESIELTSLKDKKTLTRIKIAQAMKQFLGQQSKHQKYNQRKNFLKPDENQRWIQSSTPHPLPDNKLIPTSPLASTTTSSSSSTLLLTNQMIKKSIQSQPITTQDIEDMQQKRIDSRVFKKTNDDGDGGGDGDDELYDDDIDLEEINKIKDCDEISNLMQRYHQVSNQCKELKGLIPQHRQLLTRRSKRCKRCDRLLVKPDINPGKIEFKRSHFAYSYIPRVTISKIQWIDQDLFQVFLTFTNPLHSYIFMSFPMEIKGSMVSLEDNSQLVDLYTNETFISGLLDEIDDNEKEAIIDQLKTFEEQNKRYFTNGSTSNNYRNGNKLTLGFIGKVGVEDALFSNYNNNTDEVTHLIIHLPDQLSLNSINNNEVDPPKFKSKFSSIKFTIVVEFSLKSTTTNNTSGPNAAEAAATTTSSGGLGSSGTIPESSSSQKTLLKILFDIPSDKFSNAEL
Protein: ATP-sensitive inward rectifier potassium channel 12 (Inward rectifier K(+) channel Kir2.2) (Potassium channel, inwardly rectifying subfamily J member 12) (F1NHE9)
Organism: Gallus gallus (Chicken)
Function: Inward rectifying potassium channel that is activated by phosphatidylinositol 4,5-bisphosphate and that probably participates in controlling the resting membrane potential in electrically excitable cells. Inward rectifier potassium channels are characterized by a greater tendency to allow potassium to flow into the cell rather than out of it. The inward rectification is probably due to the blockage of outward current by cytoplasmic polyamines and/or magnesium ions.
Subcellular location: Membrane {ECO:0000269|PubMed:21874019}; Multi-pass membrane protein {ECO:0000269|PubMed:21874019}. Cell membrane {ECO:0000250|UniProtKB:Q14500}. Cell membrane, sarcolemma, T-tubule {ECO:0000250|UniProtKB:P52188}.
Interaction partners:
Sequence:
MTAGRVNPYSIVSSEEDGLRLTTMPGINGFGNGKIHTRRKCRNRFVKKNGQCNVEFTNMDDKPQRYIADMFTTCVDIRWRYMLLLFSLAFLVSWLLFGLIFWLIALIHGDLENPGGDDTFKPCVLQVNGFVAAFLFSIETQTTIGYGFRCVTEECPLAVFMVVVQSIVGCIIDSFMIGAIMAKMARPKKRAQTLLFSHNAVVAMRDGKLCLMWRVGNLRKSHIVEAHVRAQLIKPRITEEGEYIPLDQIDIDVGFDKGLDRIFLVSPITILHEINEDSPLFGISRQDLETDDFEIVVILEGMVEATAMTTQARSSYLASEILWGHRFEPVLFEEKNQYKVDYSHFHKTYEVPSTPRCSAKDLVENKFLLPSTNSFCYENELAFMSRDEDEEDDDSRGLDDLSPDNRHEFDRLQATIALDQRSYRRESEI
Protein: At4g15730 (CW-type Zinc Finger) (Q8GY51)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MGEDYELEEGEMNCSSDEAVVDLDVDLSYIDKKVQNVLGHLQKGFGEEARDRFGPEIFDYGSFLPTYKRLPAVPSCQRSSLGNHAVQRISNSLPGKNVVQKFQSPPATSCKLVRNQDPQNYQTSGSLLAQAPGKVPINKGNARTPANDLPHNKPIRVRIKMGSEILSQSVAMVCKDLGLDGSPNSPPRISQDDSSRMLPHTSLGKTSESPSRILQEMTAISVPEDLLMSPLPDSLLLVKDKKKQYTLLDNQPMIKTGKKSSIQIQNKFSDVLCCEKTPIGRRRKEVDCFHATTWNETKKHKVLSTGQLARDNSACGLGGASLTTDGFTTKSNLQEGCRKDGESDPRVANKIKFVGLHAVKEKKTCPTKLQQNRSKYRIGDKVLSKMPLKDAAYIGHNSMDTGFDFAVAPSSTSVDLDYWAQCESCEKWRLLPYDLNTEKLPDKWLCSMQTWLPGMNHCGVSEEETTNAIKSFHASEGHGPDTGVKLLSDVRNADKIYQPLTSGSLPNPIEKKSNVEDLSQGVSSNILVDAAKPMRSNPHIFKNKNMKLPGETPTATQISADLSHDFFQDKIDQKAKRRAAGAGCQIKVKKKKEADKEESDGSKHIKTGDGNKLARVIKAEEIHWNQDPKWTPAERKRKRHDNDFCTLNVERDPKKRLLVSKKKPDHKPQLITASGSLCTKAQGNINSTVRKIRLMGYKQGKDGKNSKLFADGEENEPSMEKAVTTKISVHESKANQRNELFQADCFQEHLNGDASCRYFSGGSGQISGIETSNSSKVLGSHKSGRMYVEEVKASPVESVSSSPARSSCPTNDILQEAEKLRKLADCFKSSGFEYEYKEINFKAALRFLLGASVLEMCSTDNVEVGKMSHIEAYHTAAKLSESCAHQYETSQEMAAATLAYKCTEVACMRLVYGRSLGLSGEWNELQKMVQMTPQGESPSSSASDVDSFNHQGVIKKSAKTRRGLSHVAGNLLPVARSQLNFVPLLDFTGSMNLAMEASAKSQNAFKAVTDTSEERKHGDCISAIKKVVDFSFHDVEALIKMIEVAMDALSSSRFGGPKC
Protein: Rough deal (Q9V9W7)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Centromere/kinetochore protein zw10
- Protein zwilch
- Protein abnormal spindle
- Monopolar spindle 1, isoform B
- Kinesin-like protein Klp61F
- Structural maintenance of chromosomes protein
- Bub1-related kinase
- Mitotic spindle assembly checkpoint protein MAD2A
- Fanconi anemia group D2 protein homolog
- CENP-meta, isoform C
Sequence:
MWSNFEASSLEDETISNIFSSRGIFQISSEEEVNKYPDVMASVQCGKMVIGIDKSLLLLEDELVAKCSFLAFGAAIEAIAISSSGNLIVCGLSDGEVHGVFIKGLLLFSVAVNLEDVSLTGGTFRSIHQLDQRFYFTCKNGSIYSLSDIDETCLETLGNMSLNENETIACEKALLEDVTIQRLSKGRSSCSVDCAVLLKRLLTGNISAENNQDDLEAQPGLVITGDQSTMNFRNAANDVTRINLPAQYGSLKQIFNLEHYIIALTDSGHLVEICPYTRTVYMCQTTQQKNLLIEDLLVMECSEDNIELLVLTKSTAEGRFIKIVEYPTLNVKNEVEVPDHAWLVRQPKCAVNLYYLAAKEVNQSSIPSVVEMMLVSETDPSDRFKKLICKGRLEEAEEFGKQFELCLQPIYEAKAKRILVELCNSNSQNVDTKFQDLLQLLSQVESKAFIKSHRMINLNSRHILERYLHEVKKRLTFEDDEEDMLEIDEQLHRLKTLAIIDPYECNTDWQKFIYDNNLVRMVKSLFNTDMPTACLIWRRHSSSILPLLNEDELRTLLGFIPSNTKPFNVVQWLRQFIPMVSNTHPSIMPFITDWSIEMTRNLQYSPHWPDIGLEFCTKILDIFEEIQFTYSDVRRQQERNVGKLRDLVNALQDLSVLKTNYNMGFTLDNYMQDSIDATALSILQHVQLDKLQRLVKNFMYPIFQEKGRQPLDVIKQYISQLVASRLSSSSWLDRAMACIELLHNEDSRLECALSVLQNAPVPWPDTLAPLIRLRASTHPLAVKINAEYEIQVIKIMKVKYGWPADSSDINLELFMMRIVKLNLPDMLDDISALTKAAPELSTSANFNCCYQMARRGQVEMAYEFFKKLNGEKNSKSAKEVVEIMANILENSSSASFESDIKVQEHLNVLELFKLFLPHVESVYERRYLVIKHRFRLRKFGILLSCSSELIPLHRRHCLLDEAIERIIERAQATLNVSAFIASEISELCTALGLPKVFGLHRICQRIGCLPLSCALAYHVVSFVDCVPANAGEFVNLALELLVQQIESAKGKNQETASSLQLINENDPLSFYLAYELLTSALLHESSRRHDLVELIKYIRVAVIHYPLDAIKSHYDGKEQAVNEHICRALDGISVALGETTINFSCALNGSFDVKTLTVPTTTKKRYSVSMFDEVEVQPIQQQPQKKSVGGRMAIVKFLARTLLLMVIETEPNNSLLMQVRNELPENTKADVESACADFFLSLEHLTKVKEHDAWYVMSQYLLDFQKQNCRTKRIINEGFITLQLRRIFRNAMGSKDVNFIELFTMLVVDSEALALLEKLSVEVKTDLQKINFLTLSAMYHEHIEDLDSVHMIRTKRLKLFYYLEFCQQDHRIKGKFNADMDNIEDLLKEFHNKQLDVQLLERMSKDFGFDYQKILITQILSILSAQELRFEVKRDTFGDEELVMLSSAQEMRDMCQPYINEINNVELFTSKLKHFIEDINIYFYELYMCVINILMYFDSAPKEMEIWMNILHFLRHKMITRRRNRPGQVETDTWLKSQRENGVMPKISRYRLPFKPIVEQPLKDILDSELNVDNCQSWFPLIQMYTALKGSKDSSQNCDYFCMSAVKNSISEYKSKNDSESWSLHPTNNAFLQSILRLVEKVNNPNKAFLILYFVSNYARDGADQVEASYECWKFVKEKGHLITDPKSREQVAKVKRRYPIQKTQHLLYVYGLTDEKLLRQVENPTELIQALYHHELILKSSKVDINALVAEIAKLHDLCLATIQYRLLQKWLALTMESAGDGTILEETFMEEQNWPEQANGAESSNSQDASENVNRAFYILSSWPKAEAVKFLVGLIFKGGSVNTSTQLQMYECYSKLNDGSNSFTNTISQRQFISIKCVHELKALGYKSNLEKFSDDHCNKIDILKMIWQRNAQNPLSLEVMANICLGFDIHLPQIWNGILKRMVMFHMVRELNALLDVLSCRPHLLHLDGLAQAWDYVLCHPLQNAVELRSFKQEEVLHKTLLRLQGCPVVHALNLLQFAQLCIVVHRPHMAASLLSFCQSSEQRQKIKKMIHSHPVENLRQQILDLEDAGILPVVLNFALKELNL