wanglab/gogpt-training-data huggingface dataset:
Protein: Cadherin-1 (ARC-1) (Epithelial cadherin) (E-cadherin) (Uvomorulin) (CD antigen CD324) [Cleaved into: E-Cad/CTF1; E-Cad/CTF2; E-Cad/CTF3] (P09803)
Organism: Mus musculus (Mouse)
Function: Cadherins are calcium-dependent cell adhesion proteins. They preferentially interact with themselves in a homophilic manner in connecting cells; cadherins may thus contribute to the sorting of heterogeneous cell types. CDH1 is involved in mechanisms regulating cell-cell adhesions, mobility and proliferation of epithelial cells. Has a potent invasive suppressor role. It is a ligand for integrin alpha-E/beta-7 (By similarity).
Subcellular location: Cell junction, adherens junction {ECO:0000269|PubMed:12494996, ECO:0000269|PubMed:27375112, ECO:0000269|PubMed:30639848}. Cell membrane {ECO:0000269|PubMed:27760340}; Single-pass type I membrane protein. Endosome {ECO:0000250|UniProtKB:P12830}. Golgi apparatus, trans-Golgi network {ECO:0000250|UniProtKB:P12830}. Cytoplasm {ECO:0000269|PubMed:27375112, ECO:0000269|PubMed:27760340}. Cell junction, desmosome {ECO:0000250|UniProtKB:P12830}. Note=Colocalizes with DLGAP5 at sites of cell-cell contact in intestinal epithelial cells. Anchored to actin microfilaments through association with alpha-, beta- and gamma-catenin. Sequential proteolysis induced by apoptosis or calcium influx, results in translocation from sites of cell-cell contact to the cytoplasm. Colocalizes with RAB11A endosomes during its transport from the Golgi apparatus to the plasma membrane (By similarity). Recruited to desmosomes at the initial assembly phase and also accumulates progressively at mature desmosome cell-cell junctions (By similarity). Localizes to cell-cell contacts as keratinocyte differentiation progresses (PubMed:27375112). {ECO:0000250, ECO:0000250|UniProtKB:P12830, ECO:0000269|PubMed:27375112}.
Interaction partners:
- Junction plakoglobin
- Catenin delta-1
- Killer cell lectin-like receptor subfamily G member 1
- Catenin beta-1
- Catenin alpha-1
- Integrin alpha-E
- Epidermal growth factor receptor
- Cadherin-2
- Ras GTPase-activating-like protein IQGAP1
- Occludin
Sequence:
MGARCRSFSALLLLLQVSSWLCQELEPESCSPGFSSEVYTFPVPERHLERGHVLGRVRFEGCTGRPRTAFFSEDSRFKVATDGTITVKRHLKLHKLETSFLVRARDSSHRELSTKVTLKSMGHHHHRHHHRDPASESNPELLMFPSVYPGLRRQKRDWVIPPISCPENEKGEFPKNLVQIKSNRDKETKVFYSITGQGADKPPVGVFIIERETGWLKVTQPLDREAIAKYILYSHAVSSNGEAVEDPMEIVITVTDQNDNRPEFTQEVFEGSVAEGAVPGTSVMKVSATDADDDVNTYNAAIAYTIVSQDPELPHKNMFTVNRDTGVISVLTSGLDRESYPTYTLVVQAADLQGEGLSTTAKAVITVKDINDNAPVFNPSTYQGQVPENEVNARIATLKVTDDDAPNTPAWKAVYTVVNDPDQQFVVVTDPTTNDGILKTAKGLDFEAKQQYILHVRVENEEPFEGSLVPSTATVTVDVVDVNEAPIFMPAERRVEVPEDFGVGQEITSYTAREPDTFMDQKITYRIWRDTANWLEINPETGAIFTRAEMDREDAEHVKNSTYVALIIATDDGSPIATGTGTLLLVLLDVNDNAPIPEPRNMQFCQRNPQPHIITILDPDLPPNTSPFTAELTHGASVNWTIEYNDAAQESLILQPRKDLEIGEYKIHLKLADNQNKDQVTTLDVHVCDCEGTVNNCMKAGIVAAGLQVPAILGILGGILALLILILLLLLFLRRRTVVKEPLLPPDDDTRDNVYYYDEEGGGEEDQDFDLSQLHRGLDARPEVTRNDVAPTLMSVPQYRPRPANPDEIGNFIDENLKAADSDPTAPPYDSLLVFDYEGSGSEAASLSSLNSSESDQDQDYDYLNEWGNRFKKLADMYGGGEDD
Protein: Little elongation complex subunit 2 (Interactor of little elongator complex ELL subunit 2) (NMDA receptor-regulated protein 2) (Q659A1)
Organism: Homo sapiens (Human)
Function: Component of the little elongation complex (LEC), a complex required to regulate small nuclear RNA (snRNA) gene transcription by RNA polymerase II and III.
Subcellular location: Nucleus {ECO:0000269|PubMed:23932780}. Note=Colocalizes with COIL in subnuclear Cajal and histone locus bodies. Translocates in the LEC complex to Cajal and histone locus bodies at snRNA genes in a ICE1-dependent manner. Associates to transcriptionally active chromatin at snRNA genes.
Interaction partners:
- Little elongation complex subunit 1
- Zinc finger CCCH domain-containing protein 8
- RNA polymerase II elongation factor ELL
- ELL-associated factor 1
- RNA polymerase II elongation factor ELL3
- Zinc finger protein 346
- N-alpha-acetyltransferase 15, NatA auxiliary subunit
- RNA polymerase II elongation factor ELL2
- ELL-associated factor 2
- AF4/FMR2 family member 4
Sequence:
MSSKMVISEPGLNWDISPKNGLKTFFSRENYKDHSMAPSLKELRVLSNRRIGENLNASASSVENEPAVSSATQAKEKVKTTIGMVLLPKPRVPYPRFSRFSQREQRSYVDLLVKYAKIPANSKAVGINKNDYLQYLDMKKHVNEEVTEFLKFLQNSAKKCAQDYNMLSDDARLFTEKILRACIEQVKKYSEFYTLHEVTSLMGFFPFRVEMGLKLEKTLLALGSVKYVKTVFPSMPIKLQLSKDDIATIETSEQTAEAMHYDISKDPNAEKLVSRYHPQIALTSQSLFTLLNNHGPTYKEQWEIPVCIQVIPVAGSKPVKVIYINSPLPQKKMTMRERNQIFHEVPLKFMMSKNTSVPVSAVFMDKPEEFISEMDMSCEVNECRKIESLENLYLDFDDDVTELETFGVTTTKVSKSPSPASTSTVPNMTDAPTAPKAGTTTVAPSAPDISANSRSLSQILMEQLQKEKQLVTGMDGGPEECKNKDDQGFESCEKVSNSDKPLIQDSDLKTSDALQLENSQEIETSNKNDMTIDILHADGERPNVLENLDNSKEKTVGSEAAKTEDTVLCSSDTDEECLIIDTECKNNSDGKTAVVGSNLSSRPASPNSSSGQASVGNQTNTACSPEESCVLKKPIKRVYKKFDPVGEILKMQDELLKPISRKVPELPLMNLENSKQPSVSEQLSGPSDSSSWPKSGWPSAFQKPKGRLPYELQDYVEDTSEYLAPQEGNFVYKLFSLQDLLLLVRCSVQRIETRPRSKKRKKIRRQFPVYVLPKVEYQACYGVEALTESELCRLWTESLLHSNSSFYVGHIDAFTSKLFLLEEITSEELKEKLSALKISNLFNILQHILKKLSSLQEGSYLLSHAAEDSSLLIYKASDGKVTRTAYNLYKTHCGLPGVPSSLSVPWVPLDPSLLLPYHIHHGRIPCTFPPKSLDTTTQQKIGGTRMPTRSHRNPVSMETKSSCLPAQQVETEGVAPHKRKIT
Protein: Splicing factor 3A subunit 3 (SF3a60) (Spliceosome-associated protein 61) (SAP 61) (Q12874)
Organism: Homo sapiens (Human)
Function: Involved in pre-mRNA splicing as a component of the splicing factor SF3A complex that contributes to the assembly of the 17S U2 snRNP, and the subsequent assembly of the pre-spliceosome 'E' complex and the pre-catalytic spliceosome 'A' complex. Involved in pre-mRNA splicing as a component of pre-catalytic spliceosome 'B' complexes.
Subcellular location: Nucleus speckle {ECO:0000269|PubMed:8022796}. Nucleus {ECO:0000269|PubMed:10882114, ECO:0000269|PubMed:21349847, ECO:0000269|PubMed:29360106, ECO:0000269|PubMed:30315277}.
Interaction partners:
- U2 small nuclear ribonucleoprotein B''
- U4/U6.U5 tri-snRNP-associated protein 1
- Pre-mRNA-processing factor 6
- Small nuclear ribonucleoprotein E
- Small nuclear ribonucleoprotein-associated proteins B and B'
- Probable ATP-dependent RNA helicase DDX46
- PHD finger-like domain-containing protein 5A
- Splicing factor 3B subunit 2
- U5 small nuclear ribonucleoprotein 200 kDa helicase
- Small nuclear ribonucleoprotein F
Sequence:
METILEQQRRYHEEKERLMDVMAKEMLTKKSTLRDQINSDHRTRAMQDRYMEVSGNLRDLYDDKDGLRKEELNAISGPNEFAEFYNRLKQIKEFHRKHPNEICVPMSVEFEELLKARENPSEEAQNLVEFTDEEGYGRYLDLHDCYLKYINLKASEKLDYITYLSIFDQLFDIPKERKNAEYKRYLEMLLEYLQDYTDRVKPLQDQNELFGKIQAEFEKKWENGTFPGWPKETSSALTHAGAHLDLSAFSSWEELASLGLDRLKSALLALGLKCGGTLEERAQRLFSTKGKSLESLDTSLFAKNPKSKGTKRDTERNKDIAFLEAQIYEYVEILGEQRHLTHENVQRKQARTGEEREEEEEEQISESESEDEENEIIYNPKNLPLGWDGKPIPYWLYKLHGLNINYNCEICGNYTYRGPKAFQRHFAEWRHAHGMRCLGIPNTAHFANVTQIEDAVSLWAKLKLQKASERWQPDTEEEYEDSSGNVVNKKTYEDLKRQGLL
Protein: AAEL013105-PA (Q16K62)
Organism: Aedes aegypti (Yellowfever mosquito) (Culex aegypti)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
Interaction partners:
- AAEL006071-PA
- carbonic anhydrase
- AAEL013106-PA
- AAEL013104-PA
Sequence:
MKTRLLTTLTWLALVQVLVVLVNHRGCALATVNLTESNGSTPYVVSEPEIPYEELEEPRVLPLQALPVSVKASSSESPNGADADIRNKHRFNQNIHGPDQPHADINTVLKVILEEPEINDEPFTTTHGYPTFSAYDNIVPSKPLNLSVLEVTSTTIKITWREPEKLNGAIHGYRVYYVHQNQTLLHLPILKADAAVNSVYTYTLSNLKPYTDYKIIVAAFTKKFDGEPSEVSQRTDISGPSAPKVVNLTCHSQHELLFGWHIPQTYYNTIDYYIISYRNLEHSEYKDIRLSANSSIVETSMIIPNLTTNMVYEVKVRAASASVINPKQIILGSYSEPKKISLQLHCEKIPQPSQRQVYDDYNLAVLGGIVFSCFGLLLIVLSFLLWKKCFHAAYYYLDDPPACQGANTAGLIDWEAPCEVAGEVRGPIPVTEFAKHVASLHVDGDIGFSKEYEAIQGEALNDEYPSEHSQHPDNKGKNRYLNVIAYDHSRVHLRQVPGQKKHLDYINANYIDGYQRPRSFIGTQGPLPGTFDCFWRMIWEQRVAIIVMITNLVERGRRKCDMYWPKDGAEMYGVIQVRLIREDVMATYTVRTLQIKHTKLKKKKASQSEKLVYQYHYTNWPDHGTPDHPLPVINFVKKSTAANPSDAGPIVVHCSAGVGRTGTYIVLDAMLKQIESKGMLNVFGFLRYIRAQRNYLVQTEEQYIFIHDALVEAIDSGETNIKMDAIGGLVNNIDFIDNQYKLITSYQPKEINLTSALKSVNAIKNRSSLVPLEGSRVHLTPKPGVEGSDYINASWLHGFRRLRDFVVTQHPLIETFKDFWQMVWDHNAQTVVLLSSADNMSFLQFWPNESEPMESDYYRIRMVSETSENNYIVRNFVIQSIQDDYELSVRMFENPMWPDMANPRSIYDFAVRVHERCAQYRNGPIVVVDRYHWKYF
Protein: Centrosomal protein of 128 kDa (Cep128) (Q6ZU80)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:14654843}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000269|PubMed:21399614}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000269|PubMed:21399614}. Note=Associates with the mother centriole.
Interaction partners:
- Centrosomal protein of 170 kDa
- Coiled-coil domain-containing protein 120
- Coiled-coil domain-containing protein 68
- Centriolin
- Ninein
- Outer dense fiber protein 2
- Kinesin-like protein KIF2A
- Dynactin subunit 1
- Centrosomal protein of 89 kDa
- Centrosomal protein of 164 kDa
Sequence:
MAESSSESDHFRCRDRLSPWAARSTHRGTRSLPTVEVTEKVNTITSTLQDTSRNLRQVDQMLGRYREYSNGQAGAIEHLKESLEQSIDQLRSQRLLRNSGGRSISVTSLSASDLDGGTGSELHHFPPTSPLKDYGDPQGIKRMRSRTGVRFVQETDDMTQLHGFHQSLRDLSSEQIRLGDDFNRELSRRSRSDAETKRALEELTEKLNEAQKQEVVSDRVERRLQELEREMRTERELVERRQDQLGLMSLQLQEALKKQEAKADEHEGAIKNKLRQTETEKNQLEQELELSRRLLNQSEGSRETLLHQVEELRTQLTKAEGDRKGLQHQVSQISKQQSNYQDEQGEDWRFRRGVEREKQDLEKQMSDLRVQLNFSAMASELEEVKRCMERKDKEKAHLASQVENLTRELENGEKQQLQMLDRLKEIQNHFDTCEAERKHADLQISELTRHAEDATKQAERYLSELQQSEALKEEAEKRREDLKLKAQESIRQWKLKHKKLERALEKQSETVDELTGKNNQILKEKDELKTQLYAALQQIENLRKELNDVLTKRALQEEELHSKEEKLRDIKSHQADLELEVKNSLDTIHRLESELKKQSKIQSQMKVEKAHLEEEIAELKKSQAQDKAKLLEMQESIKDLSAIRADLANKLAEEERAKKAVLKDLSDLTAQAKSRDEETATIITQLKLERDVHQRELKDLTSSLQSVKTKHEQNIQELMKHFKKEKSEAENHIRTLKAESLEEKNMAKIHRGQLEKLKSQCDRLTEELTQNENENKKLKLKYQCLKDQLEEREKHISIEEEHLRRMEEARLQLKDQLLCLETEQESILGVIGKEIDAACKTFSKDSVEKLKVFSSGPDIHYDPHRWLAESKTKLQWLCEELKERENREKNLRHQLMLCRQQLRNLTENKESELQCLFQQIERQEQLLDEIHREKRDLLEETQRKDEEMGSLQDRVIALETSTQVALDHLESVPEKLSLLEDFKDFRDSCSSSERTDGRYSKYRVRRNSLQHHQDDTKYRTKSFKGDRTFLEGSHTRGLDHSSSWQDHSRFLSSPRFSYVNSFTKRTVAPDSASNKEDATMNGTSSQPKKEEYGS
Protein: Twisted gastrulation protein homolog 1-B (Q98SR9)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Involved in dorsal-ventral patterning. Appears to function predominantly as a ventralizing factor, through its actions as a BMP signaling agonist, acting through both chd-dependent and chd-independent mechanisms. May also antagonize BMP signaling, probably via formation of ternary complexes with chd and BMPs, resulting in dorsalization.
Subcellular location: Secreted {ECO:0000250}.
Interaction partners:
- 5'-AMP-activated protein kinase subunit beta-1a
- 5'-AMP-activated protein kinase subunit beta-1b
- BCL2-interacting protein 4
- Chordin
Sequence:
MGSSSSSSVVLLLLLLSSLSIALACNKALCASDVSKCLIQELCQCRPADGNCSCCKECMLCLGSLWEECCDCVGMCNPRSMSESPATGRSTVEDLFQPIPSLFRALTEGDAPTHTLVLTLPLAEELQYQHNLHNYLETLHNTQHNNTTSVPENSIHSSYHTQDKQCTVVYFDECVSIRQCKQYCESMGGSKYRWFHNACCQCIGPECVDYGSKSVRCLNCLY
Protein: Protein crumbs homolog 1 (P82279)
Organism: Homo sapiens (Human)
Function: Plays a role in photoreceptor morphogenesis in the retina (By similarity). May maintain cell polarization and adhesion (By similarity).
Subcellular location: [Isoform 1]: Apical cell membrane {ECO:0000250|UniProtKB:Q8VHS2}; Single-pass type I membrane protein {ECO:0000255}. Secreted {ECO:0000305}. Cell projection, cilium, photoreceptor outer segment {ECO:0000250|UniProtKB:Q8VHS2}. Photoreceptor inner segment {ECO:0000250|UniProtKB:Q8VHS2}.; SUBCELLULAR LOCATION: [Isoform 2]: Secreted.
Interaction partners:
- Protein PALS1
- InaD-like protein
- Protein crumbs homolog 2
- Protein crumbs homolog 3
Sequence:
MALKNINYLLIFYLSFSLLIYIKNSFCNKNNTRCLSNSCQNNSTCKDFSKDNDCSCSDTANNLDKDCDNMKDPCFSNPCQGSATCVNTPGERSFLCKCPPGYSGTICETTIGSCGKNSCQHGGICHQDPIYPVCICPAGYAGRFCEIDHDECASSPCQNGAVCQDGIDGYSCFCVPGYQGRHCDLEVDECASDPCKNEATCLNEIGRYTCICPHNYSGVNCELEIDECWSQPCLNGATCQDALGAYFCDCAPGFLGDHCELNTDECASQPCLHGGLCVDGENRYSCNCTGSGFTGTHCETLMPLCWSKPCHNNATCEDSVDNYTCHCWPGYTGAQCEIDLNECNSNPCQSNGECVELSSEKQYGRITGLPSSFSYHEASGYVCICQPGFTGIHCEEDVNECSSNPCQNGGTCENLPGNYTCHCPFDNLSRTFYGGRDCSDILLGCTHQQCLNNGTCIPHFQDGQHGFSCLCPSGYTGSLCEIATTLSFEGDGFLWVKSGSVTTKGSVCNIALRFQTVQPMALLLFRSNRDVFVKLELLSGYIHLSIQVNNQSKVLLFISHNTSDGEWHFVEVIFAEAVTLTLIDDSCKEKCIAKAPTPLESDQSICAFQNSFLGGLPVGMTSNGVALLNFYNMPSTPSFVGCLQDIKIDWNHITLENISSGSSLNVKAGCVRKDWCESQPCQSRGRCINLWLSYQCDCHRPYEGPNCLREYVAGRFGQDDSTGYVIFTLDESYGDTISLSMFVRTLQPSGLLLALENSTYQYIRVWLERGRLAMLTPNSPKLVVKFVLNDGNVHLISLKIKPYKIELYQSSQNLGFISASTWKIEKGDVIYIGGLPDKQETELNGGFFKGCIQDVRLNNQNLEFFPNPTNNASLNPVLVNVTQGCAGDNSCKSNPCHNGGVCHSRWDDFSCSCPALTSGKACEEVQWCGFSPCPHGAQCQPVLQGFECIANAVFNGQSGQILFRSNGNITRELTNITFGFRTRDANVIILHAEKEPEFLNISIQDSRLFFQLQSGNSFYMLSLTSLQSVNDGTWHEVTLSMTDPLSQTSRWQMEVDNETPFVTSTIATGSLNFLKDNTDIYVGDRAIDNIKGLQGCLSTIEIGGIYLSYFENVHGFINKPQEEQFLKISTNSVVTGCLQLNVCNSNPCLHGGNCEDIYSSYHCSCPLGWSGKHCELNIDECFSNPCIHGNCSDRVAAYHCTCEPGYTGVNCEVDIDNCQSHQCANGATCISHTNGYSCLCFGNFTGKFCRQSRLPSTVCGNEKTNLTCYNGGNCTEFQTELKCMCRPGFTGEWCEKDIDECASDPCVNGGLCQDLLNKFQCLCDVAFAGERCEVDLADDLISDIFTTIGSVTVALLLILLLAIVASVVTSNKRATQGTYSPSRQEKEGSRVEMWNLMPPPAMERLI
Protein: glucose-6-phosphate 1-epimerase (EC 5.1.3.15) (Q9V3D1)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MATTAAAMAATSVVVLDRGNNTTCTINLHGATVVSWRVNNQEQLFVSKLASFDGKKAIRGGIPFVFPQFGAWSFGPQHGFARITRWHLERPPDRLHNGDVEAIFSLMDNDFTRSIWNYQFRITYRLILREKELHFHIGVYNPSKELSFTFNMLLHTYLKVPDVRRCQITGLQGCHFIDKTRENALYQEGREVVTVNEWTDRIYQHTPQEHVITNVVSGRKMRLHKYNFPDTVIWNPWIDRSREMSDFGDDEFPNMLCVEAGNVTSPVILLPGTAFEASQILQIIIEGNVSRKTKRNR
Protein: Zinc transporter ZIP12 (Solute carrier family 39 member 12) (Zrt- and Irt-like protein 12) (ZIP-12) (Q5FWH7)
Organism: Mus musculus (Mouse)
Function: Acts as a zinc-influx transporter.
Subcellular location: Membrane {ECO:0000269|PubMed:23716681}; Multi-pass membrane protein {ECO:0000255}. Note=At low Zn(2+) extracellular concentration, is redistributed from the perinuclear space to the cytoplasm and plasma membrane. {ECO:0000269|PubMed:23716681}.
Interaction partners:
- Zinc transporter ZIP9
- Zinc transporter ZIP11
- Zinc transporter ZIP1
- Zinc transporter 6
- Proton-coupled zinc antiporter SLC30A2
- Probable proton-coupled zinc antiporter SLC30A4
- Proton-coupled zinc antiporter SLC30A9, mitochondrial
- Zinc transporter ZIP2
- Probable proton-coupled zinc antiporter SLC30A3
- Zinc transporter 7
Sequence:
MCFWTNLSVWMILLSHSLSLVSSTETGKTLTQNNSRAGSQGLLEVLRVLSAGDHWSLNHPQSLIKILLERTGCPQRTDWTQGDCKLCLEADALLLTAGGNLEDELREEVVQRVSLLLLYYIIHQEEICSSKLNMSNREYEFYLHSLLGLRQDEDSYFLSEKETDDILAFTRKYFGTSSSQCMETKILQRESGIQGSNGADEKTLPQLAATIIALSLQGVCLGRKALPSPDDFTEYIFSFLNSTNTLHLSEIEQLLNMLTTRRTCAKEDKYLHQYQRKQNTEEHSLRDPKTSTAMDKESDDHSPSWDQACFSARQLVEIFLQNHSSLSISKEDFKQLSPGIIQQLLSCSCQMPKDQQAKPPPTTLEKYGYSTVAVTLLTLGSMLGTALVLFHSCEENYSLILQLFVGLAVGTLSGDALLHLIPQVLGLHKQEAEFGHFHESQSPIWKLLGLLGGIHGFFLIEKCFILLVSPNTKGLPLVNEHVGHTHHLGLNPELNDQSSGGKSISTIQLKGPEDSQTTVLPIGNVPASNRNGKTISLLAIMILVGDSLHNFADGLVIGTAFSSSLESGVTTTIAILCHEIPHEMGDFAVLLSSGLSVRTAILMNFLSALTAFAGLYIGLSVSADPRVQDWILTVTAGMFLYLSLVGMLPEMTHVQTQRPWMTFLLQNVGLVLGWFSLLLLAVYEQNIKI
Protein: UbiA prenyltransferase domain-containing protein 1 homolog (EC 2.5.1.-) (Protein heixuedian) (Q9V3R8)
Organism: Drosophila melanogaster (Fruit fly)
Function: Prenyltransferase that mediates the formation of menaquinone-4 (MK-4), a vitamin K2 isoform, thereby acting as a mitochondrial electron carrier. Mediates the conversion of phylloquinone (PK) into MK-4, probably by cleaving the side chain of phylloquinone (PK) to release 2-methyl-1,4-naphthoquinone (menadione; K3) and then prenylating it with geranylgeranyl pyrophosphate (GGPP) to form MK-4. MK-4 acts as a membrane electron carrier downstream of a electron transport chain complex, improving mitochondrial oxygen consumption.
Subcellular location: Mitochondrion membrane {ECO:0000269|PubMed:22582012}; Multi-pass membrane protein {ECO:0000269|PubMed:22582012}.
Interaction partners:
- 3-hydroxy-3-methylglutaryl-coenzyme A reductase
- Uncharacterized protein, isoform B
- GH01188p
- LD47749p
- 4-hydroxybenzoate polyprenyltransferase, mitochondrial
Sequence:
MATSSQLLPNGNLSRNGKTKTEDGEEVEAVVGARAAGADAGVALTGRLTGHPSTSGTFMKLKTYLLALRPWSLSASLVPTLLGSALAYRSQWAEEFSLATFFLTAFTVVTVHCAGNVVNTYFDFIKGIDKQKADDRTLVDHILTKDEVVSLGAILYMAGCGGFVLLAVLSPAKMEHLALIYFGGLSSSFLYTGGIGFKYIALGDLVILILFGPISVLFAFMSQTGHLDWTTMGYAIPLALNTEAILHSNNTRDADNDRRAGIVTLAILIGRTASHVLYAMLLFAPYSLFFIFGLKYSLWFLLPLVTLPQAFQIEKRFRNEQTMHLVPRQTAKLNFFFGILYVVACCCAHQLPTFGLRRN
Protein: Uncharacterized protein (Q57TT6)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- rRNA processing protein, putative
- Ribosome biogenesis protein, putative
- Ribosome production factor 2 homolog
- rRNA biogenesis protein, putative
- Histone-binding protein RBBP4-like N-terminal domain-containing protein
- Nucleolar complex protein 2
- Nucleolar GTP-binding protein 1
- Pescadillo homolog
- U3 small nucleolar RNA-associated protein 13 C-terminal domain-containing protein
- Nucleolar GTP-binding protein 2
Sequence:
MLTSLSWVPKGGMKPIPIRTGDDIDTVRAKLRRRNPELGVEEDETIPHEGTNLADSGDASSDDAGDTGGMCFGGGADTILEQVESDDEDEINDTNFKETDLVFATALADAAQPRLELYVYDEPENNIYVHHDMEVAAFPLSTAWLTDGTMSICAVGTMRPFVELWNLDVMDAVEPACLLGGCVKWEDNYRKRVKSSLLQEGSHKDSVICVRWNTCAQHILASGSADTTIKMWDLNTSSCIGTYTEPEKVQSLDWHRSEANLLLSGGFDATMVLRDCRSPSSAALRFATGSTVEHVEFDPHSGGRVLYASTSTGNWAAFEARMNAEALWQMQVHEADTTFSASPHVPGLLAAGGKDNMISLWDARDTTCPPKEIVKRSYRTGAVMSLSFHPNSPHVLGACGSKGEPLVYIITDDVQRVFC
Protein: Farnesyl diphosphate synthase (D5LB37)
Organism: Rhodobacter capsulatus (Rhodopseudomonas capsulata)
Interaction partners:
Sequence:
MFSERLKEIQDAVETAMAAAIGRLPAGDLRDAMAYAAQGGKRLRAFLAIESAAIHGISMAQAMPAALAVEALHAYSLVHDDMPCMDNDDLRRGLPTVHKKWDDATAVLAGDALQTLAFELCTDPVLGSAENRVALVAALAQASGAEGMVYGQALDIAAETAAVPLTLDEIIRLQAGKTGALISFAAQAGAILAGADRGPLTAYATALGLAFQIADDILDVEGNEEAAGKRLGKDAEAHKATFVSLLGLAGAKSRAADLVAEAEAALAPYGEAASTLRACARYVIERDK
Protein: Protein PAT1 homolog 2 (PAT1-like protein 2) (Protein PAT1 homolog a) (Pat1a) (hPat1a) (C9JE40)
Organism: Homo sapiens (Human)
Function: RNA-binding protein that acts as a translational repressor.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:20584987, ECO:0000269|PubMed:28965849}. Nucleus {ECO:0000250|UniProtKB:A2ARM1}.
Interaction partners:
- U6 snRNA-associated Sm-like protein LSm4
- U6 snRNA-associated Sm-like protein LSm1
- 5'-3' exoribonuclease 1
- Probable ATP-dependent RNA helicase DDX6
- U6 snRNA-associated Sm-like protein LSm7
- U6 snRNA-associated Sm-like protein LSm2
- CCR4-NOT transcription complex subunit 3
- CCR4-NOT transcription complex subunit 4
- U6 snRNA-associated Sm-like protein LSm5
- U6 snRNA-associated Sm-like protein LSm6
Sequence:
MNCLEGPGKTCGPLASEEELVSACQLEKEEENEGEEEEEEEDEEDLDPDLDPDLEEEENDLGDPAVLGAVHNTQRALLSSPGVKAPGMLGMSLASLHFLWQTLDYLSPIPFWPTFPSTSSPAQHFGPRLPSPDPTLFCSLLTSWPPRFSHLTQLHPRHQRILQQQQHSQTPSPPAKKPWSQQPDPYANLMTRKEKDWVIKVQMVQLQSAKPRLDDYYYQEYYQKLEKKQADEELLGRRNRVESLKLVTPYIPKAEAYESVVRIEGSLGQVAVSTCFSPRRAIDAVPHGTQEQDIEAASSQRLRVLYRIEKMFLQLLEIEEGWKYRPPPPCFSEQQSNQVEKLFQTLKTQEQNNLEEAADGFLQVLSVRKGKALVARLLPFLPQDQAVTILLAITHHLPLLVRRDVADQALQMLFKPLGKCISHLTLHELLQGLQGLTLLPPGSSERPVTVVLQNQFGISLLYALLSHGEQLVSLHSSLEEPNSDHTAWTDMVVLIAWEIAQMPTASLAEPLAFPSNLLPLFCHHVDKQLVQQLEARMEFAWIY
Protein: A-kinase anchoring protein alpha (Q2VEB4)
Organism: Mus musculus (Mouse)
Subcellular location: Nucleus membrane {ECO:0000256|ARBA:ARBA00004126}.
Interaction partners:
Sequence:
MLTMSVTLSPLRSQDPDPMATDASPMAINMTPTVEQEEGEGEEAVEDVGAEQQYGKPPPLHTAADWKIVLHLPEIETWLRMTSERVRDLTYSVQQDADSKHVDVHLVQLKDICEDISDHVEQIHALLETEFSLKLLSYSVNVIVDIHAVQLLWHQLRVSVLVLRERILQGLQDANGNYTRQTDILQAFSEETTEGRLDSLTEVDDSGQLTIKCSQNYLSLDCGITAFELSDYSPSEDLLGGLGDMTTSQAKTKSFDSWSYSEMEKEFPELIRSVGLLTVATEPVPSSCGAANEDSSQVILSEDHRGGHEEDGALEPGEQLGSTLETSSLGDTLTNAAEHPPETANQDSTSSPQLGAKKSQPGPCEMMTPKRSIRDCFNYNEDSPTQPTLPKRGLFLKETLKNERRGSDGKGRVVDLKPELSRSTPSLVEPPDRSKLCLVLQSSYPSSPSAASQSYECLHKVGIGNLENIVRSHIKEISSSLGRLTDCHKEKPRLKKPHKTLAEVSLCKIPKRGTGSGKQSENTRSSVVPTMVSPGAPKATARPATDSASTTSGDTCHQRNRGGKLPAQSKASSSSPCSHSSESSLGSDNIKSPLPLLSKSQKGSPPAPCHATQNGQVVEAWYGSDEYLALPSHLKQTEVLALKLENLTKLLPQKPRGETIQDIDDWELSEMNSDSEIYPTYHIKKKHTRLGTVSPSSSSDIASSLGESIESGPLSDILSDEDLCMPLSGMKKFTDEKSERPSSSEKNESHSATKSALIQKLMKDIQHQDNYEAIWERIEVGFVNKLDEFIQWLNEAMETTENWTPPKAETDSLRLYLETHLSFKLNVDSHCALKEAVEEEGHQLLELIASHKAGLKDMLKMIASQWKELQRQIKRQHSWILRALDTIKAEILATDVSVEDEEGTGSPKAEAQLCYLEAQRDAVEQMSLKLYSEQYTSGSKRKEEFADMSKAHSVGSNGLLDFDSEYQELWDWLIDMESLVMDSHDLMMSEEQQQHLYKRYSVEMSIRHLKKTELLSKVEALKKGGLSLPNDILEKVDSINEKWELLGKTLREKIQDTMAGHSGSGPRDLLSPESGSLVRQLEVRIKELKRWLRDTELFIFNSCLRQEKEGTSAEKQLQYFKSLCHEIKQRRRGVASILRLCQHLLDDRDTCNLNADHQPMQLIIVNLERRWEAIVMQAVQWQTRLRKKMGKESETLNVIDPGLMDLNGMSEDALEWDETDISNKLISVHEESNDLDQDLEPMVPTVKLEETHHKDSGYEEEAGDCGGSQYTSNITAPSSPHIYQVYSLHNVEFHEDSHTQFLKSSPKFTGTVQPTVLTKSLSKDSSFSSTKSLPDLLGGSSLVRPYSCQSGDLSQNSGSESGIVSEGDNEMPTNSDMSLFSMVDGSPSNPETQHLDPQMGDAANVLEQKFKDEGECIKLSSVSQASVSPVGCVNGKAGDLNSITKHTTDCLGDELQGKHEVFTFYDYSYLQGSKLKFPMIMKQPQSEKAHLEDPLLRGFYFDKKSCKPKHQTSESQPDAPLHEKILASAPHEMGRSSYKSSDIEKALTGIQNARQLSLLSRSSSVESLSPGGDLFGLGIFKNGSDSLQRSTSLESWLTSYKSNEDLFSCHSSGDISVSSGSVGELSKRTLDLLNRLENIQSPSEQKIKRSVSDITLQSSSQKMSFSGQMSLDVASSINEDSPASLTELSSSDELSLCSEDIVLHKNKVPESNASFRKRLNRSVADESDVNVSMIVNVSCTSACTDDEDDSDLLSSSTLTLTEEELCLKDEDDDSSIATDDEIYEESNLMSGLDYIKNELQTWIRPKLSLSREKKRPSVTDEIKVNKDGGSTERANPSDTLDIEALLNCSIKRLSENNGNGKNPPRTHDLGTKGENKKNTYDVTKDPHVADMENGNVESTPEREKEKPEIPEASANLASNVKKISESKHDEYEALMDGSDDSSVTGKEFGPPNDRHPPQIGADPQHPERGDCTSVQNSCSGLLLETGGGSRQDSDGLKSLSNDAPSVARNAAGCCLLEQNETEESASISSSTSCCNCKPDVFHQKDDEDCSVHDFVKEIIDMASTALKSKSQPESEVAAPTSLTQIKEKVLEHSHRPIHLRKGDFYSYLSLSSHDSDCGEVTNYIDEKSNTPLPPDTVDSGLDDKEDVDCFFEACVEDEPADEEARLSSALPNESEVQDEAAKPEQMTASSSVFRDETDTVPLSGLSPQKGADDAKEGDGASHTSQGCVESAEPTTPPGKAKREGSSRKQSVSGTPEENAASAKPKIQAFSLNAKQPKGKAALYPSPQTLTCKEKLVSFHEDRHSNMHR
Protein: Cofilin-1-A (ADF/cofilin-1) (XAC1) (P45695)
Organism: Xenopus laevis (African clawed frog)
Function: May play a role in the regulation of cell morphology and cytoskeletal organization (By similarity). Binds to F-actin and exhibits pH-sensitive F-actin depolymerizing activity. Required for formation of the cleavage furrow during cytokinesis.
Subcellular location: Nucleus matrix {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Cytoplasm, cell cortex {ECO:0000269|PubMed:8603919}. Membrane {ECO:0000269|PubMed:8603919}. Note=Cellular localization varies throughout development and may be related to phosphorylation levels. Shows diffuse cortical cytoplasm localization in oocytes, with membrane-association increasing after fertilization, particularly in the vegetal hemisphere.
Interaction partners:
Sequence:
MASGVMVSDDVIKVFNEMKVRHQLSPEDAKKRKKAVVFCLSDDKKTIILEPGKEILQGDIGCNVEDPYKTFVKMLPRNDCRYALYDALYETKETKKEDLVFVFWAPEEASLKSKMIYASSKDAIKKRLPGIKHEWQINTYEDVNDPCNLADKLGGNTVVSLEGKSVRS
Protein: Cyclin-A2-3 (Cyc3c-At) (Cyclin-3c) (G2/mitotic-specific cyclin-A2-3) (CycA2;3) (Q38819)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Negatively regulates endocycles and acts as a regulator of ploidy levels in endoreduplication. Promotes divisions in the guard cells (GCs) after the guard mother cells (GMC) symmetric division.
Subcellular location: Nucleus {ECO:0000269|PubMed:16415207}.
Interaction partners:
- Cyclin-dependent kinase B1-1
- Cyclin-dependent kinase A-1
- Cyclin-dependent kinase B2-1
- Cyclin-dependent kinase B1-2
- Cyclin-dependent kinase B2-2
- Cyclin-dependent kinases regulatory subunit 1
- Wee1-like protein kinase
- Retinoblastoma-related protein 1
- Cell division control protein 6 homolog
- Transcription factor E2FA
Sequence:
MGKENAVSRPFTRSLASALRASEVTSTTQNQQRVNTKRPALEDTRATGPNKRKKRAVLGEITNVNSNTAILEAKNSKQIKKGRGHGLASTSQLATSVTSEVTDLQSRTDAKVEVASNTAGNLSVSKGTDNTADNCIEIWNSRLPPRPLGRSASTAEKSAVIGSSTVPDIPKFVDIDSDDKDPLLCCLYAPEIHYNLRVSELKRRPLPDFMERIQKDVTQSMRGILVDWLVEVSEEYTLASDTLYLTVYLIDWFLHGNYVQRQQLQLLGITCMLIASKYEEISAPRIEEFCFITDNTYTRDQVLEMENQVLKHFSFQIYTPTPKTFLRRFLRAAQASRLSPSLEVEFLASYLTELTLIDYHFLKFLPSVVAASAVFLAKWTMDQSNHPWNPTLEHYTTYKASDLKASVHALQDLQLNTKGCPLSAIRMKYRQEKYKSVAVLTSPKLLDTLF
Protein: Superficial pseudohyphal growth protein 1 (Q12507)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Probable transcription factor required for superficial pseudohyphal development in response to nitrogen starvation.
Subcellular location: Nucleus {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:16289536}.
Interaction partners:
Sequence:
MDEMHSSDTLLLRTPKSKKKIGLVIPSTPSKKCKYSSGFIAEDTTPSKRFRLYQAKFKTSSKNVKAQTLSVSIKKNQGEITNPFMTEGYNDYRNIVSPGLSFDNDCFSEHELVSPLSDISSINSTSPDVEKIDSLDPFGVDSFVWNCKPLVNKEALELHRMIHSSFPMSPLESNSDVPLLLPKLKKRLSPVNRSTFKPTRYEPSHRLLKPKKSILTVPAKSLNLIVSSSRGSLNDATIFATEINSTLSNEENKLPAISSIWEKLTIPVNSSIKEKYKKLKDQIYGQASNFGEDEDNEEDNEDDLPDAAVIRGYEFQSGRRDELTQCNELQSTKDYKKVQWAKVLEQ