wanglab/gogpt-training-data huggingface dataset:
Protein: G protein-coupled receptor GPR1 (Q12361)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Seems to associate with GPA2 and act as G protein-coupled receptor that senses glucose and controls filamentous growth. It acts upstream of adenylate cyclase and is required for glucose activation of cAMP synthesis in concert with a glucose phosphorylation-dependent mechanism.
Subcellular location: Cell membrane {ECO:0000269|PubMed:9524122}; Multi-pass membrane protein {ECO:0000269|PubMed:9524122}.
Interaction partners:
- Guanine nucleotide-binding protein alpha-2 subunit
- Ras-like protein 2
- Adenylate cyclase
- Ras-like protein 1
- Guanine nucleotide-binding protein subunit beta 1
- High glucose sensor RGT2
- Guanine nucleotide-binding protein subunit beta 2
- Inhibitory regulator protein IRA2
- Low glucose sensor SNF3
- Inhibitory regulator protein IRA1
Sequence:
MITEGFPPNLNALKGSSLLEKRVDSLRQLNTTTVNQLLGLPGMTSTFTAPQLLQLRIIAITASAVSLIAGCLGMFFLSKMDKRRKVFRHDLIAFLIICDFLKAFILMIYPMIILINNSVYATPAFFNTLGWFTAFAIEGADMAIMIFAIHFAILIFKPNWKWRNKRSGNMEGGLYKKRSYIWPITALVPAILASLAFINYNKLNDDSDTTIILDNNNYNFPDSPRQGGYKPWSAWCYLPPKPYWYKIVLSWGPRYFIIIFIFAVYLSIYIFITSESKRIKAQIGDFNHNVLEEEKEKKKLFGLGHWGKAKWYFRSYFKLPLLHLLRNLKNFFTISFIDPNEETDDSGSSNGTFNFGESSNEIPTLFRKTNTGSDENVSASGGVRLLDYNSAKPLDMSKYAMSEQPDLERNNPFDCENDITLNPSELVSKQKEHKVTFSVENEGLDTRKSSMLGHQTFSCQNSLESPLAMYDNKNDNSDITSNIKEKGGIINNNSNNDDDDNNNNNDNDNDNNNSNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNSNNIKNNVDNNNTNPADNIPTLSNEAFTPSQQFSQERVNNNADRCENSSFTNVQQHFQAQTYKQMKKRRAQIQKNLRAIFIYPLSYIGIWLFPIIADALQYNHEIKHGPTMWVTYIDTCVRPLSCLVDVIVYLFKEKPWNYSWAKTESKYLIEKYILKGELGEKEILKFCHSNWGKRGWYYRGKWKKRKCWKYSTNPLKRILWFVERFFKQLFELKLHFSFYDNCDDFEYWENYYSAKDSNDNKRTESDETKTNSSDRSLPSNSLELQAMLNNITAEEVEVPLFWRIIHHIPMLGGIDLDELNRLLKIRYNNDHFSLPGLKFALNQNKSHDKHQDVSTNSMVKSSFFSSNIVTNDDENSIEEDKNLRYSDASASENYLVKPTIPGTTPDPIIEAQNDNDSSDSSGIDLIAFLRNGPL
Protein: SIGLEC-I (Sialic acid binding Ig-like lectin 15) (A7E1W8)
Organism: Mus musculus (Mouse)
Interaction partners:
- TYRO protein tyrosine kinase-binding protein
- Elongation factor 1-alpha 2
- Myelin-associated glycoprotein
- Sialoadhesin
- B-cell receptor CD22
Sequence:
MEGSLQLLACLACVLQMGSLVKTRRDASGDLLNTEAHSAPAQRWSMQVPAEVNAEAGDAAVLPCTFTHPHRHYDGPLTAIWRSGEPYAGPQVFRCTAAPGSELCQTALSLHGRFRLLGNPRRNDLSLRVERLALADSGRYFCRVEFTGDAHDRYESRHGVRLRVTAAAPRIVNISVLPGPAHAFRALCTAEGEPPPALAWSGPAPGNSSAALQGQGHGYQVTAELPALTRDGRYTCTAANSLGRAEASVYLFRFHGAPGTSTLALLLGALGLKALLLLGILGARATRRRLDHLVPQDTPPRSQAQESNYENLSQMSPPGHQLPRVCCEELLSHHHLVIHHEK
Protein: Troponin C, slow skeletal and cardiac muscles (A0A8I6A4Q5)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MLIQSCHPMLDTEFKAAFDIFVLGAEDGCISTKELGKVMRMLGQNPTPEELQEMIDEVDEDGSGTVDFDEFLVMMVRCMKDDSKGKSEEELSDLFRMFDKNADGYIDLDELKMMLQATGETITEDDIEELMKDGDKNNDGRIDYDEFLEFMKGVE
Protein: LIM and senescent cell antigen-like-containing domain protein 2 (Particularly interesting new Cys-His protein 2) (PINCH-2) (Q91XD2)
Organism: Mus musculus (Mouse)
Function: Adapter protein in a cytoplasmic complex linking beta-integrins to the actin cytoskeleton, bridges the complex to cell surface receptor tyrosine kinases and growth factor receptors.
Subcellular location: Cell junction, focal adhesion {ECO:0000269|PubMed:12651156}. Cell membrane {ECO:0000269|PubMed:12651156}; Peripheral membrane protein {ECO:0000269|PubMed:12651156}; Cytoplasmic side {ECO:0000269|PubMed:12651156}.
Interaction partners:
- Scaffold protein ILK
- Alpha-parvin
- Ras suppressor protein 1
- Beta-parvin
- Gamma-parvin
- Cytoplasmic protein NCK2
Sequence:
MTGSNMSECLADAMCQRCQARFAPTERIVNSNGELYHEHCFVCAQCFRPFPEGLFYEFEGRKYCEHDFQMLFAPCCGFCGEFVIGRVIKAMNANWHPGCFRCELCDVELADLGFVKNAGRHLCRPCHNREKAKGLGKFICQRCHLAIDEQPLMFKNDPYHPDHFSCSNCGKELTSDARELKGELYCLPCHDKMGIPICGACRRPIEGRVVNALGKQWHVEHFVCAKCEKPFLGHRHYEKKGLAYCETHYNQLFGDVCYNCSHVIEGDVVSALSKAWCVNCFSCSTCNMKLTLKNKFVEFDMKPVCKRCYERFPLELKKRLKKLSDLSSRKAQPKSVDVNSL
Protein: Crossover junction endonuclease MUS81 (EC 3.1.22.-) (Q9V3T1)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|RuleBase:RU369042}.
Interaction partners:
- Methyl methanesulfonate sensitivity 4
- DNA excision repair protein ERCC-1
- DNA repair endonuclease XPF
- Structure-specific endonuclease subunit SLX1 homolog
- DNA repair protein Rad51 homolog
- Structure-specific endonuclease subunit SLX4
- RecQ-like DNA helicase Blm
- Exonuclease 1
- DEAD-box ATP-dependent DNA helicase Fancm
- DNA topoisomerase 3-beta
Sequence:
METRLEVLLREPNPLFTRWLERWLREAERREQKSQFSLRQALESLKSYPLPLASGRDCSILRGFGGTLCQLIDEELRHHRGLQLLPQEAVVQERYEQQVQAVVRKVQEKQLEHQKRQNKCDRPRKLTKKDLAELAALEERERVVRMKPGQFQLLLLVDTQETSGKNKRVLDQTRSYLESLGARHEVRRLTIGDFLWVAQDQEGNELVLPYIVERKRMDDLASSIRDGRFHEQKHRLQHCGLQHIIYLVEDYGDNEQLGLPLDSLQQALTNAKVQTGVRVVRTANHYRSMSYLAGMSRTLGQIFAGKKLHSVDRGAIDQSTCLLTHSDLGLLKFRALYEDSAKNAQLTVREVFVQQLLQLHSLSLERAMAIVERYPTPRWLLDAYAECADQKQARLLLASIPCGPLERPLGDKISQCLHEFYSTHFR
Protein: Microfibril-associated glycoprotein 3 (P55082)
Organism: Homo sapiens (Human)
Function: Component of the elastin-associated microfibrils.
Subcellular location: Cell membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.
Interaction partners:
- Microfibrillar-associated protein 2
- Microfibrillar-associated protein 1
- Fibrillin-2
Sequence:
MKLHCCLFTLVASIIVPAAFVLEDVDFDQMVSLEANRSSYNASFPSSFELSASSHSDDDVIIAKEGTSVSIECLLTASHYEDVHWHNSKGQQLDGRSRGGKWLVSDNFLNITNVAFDDRGLYTCFVTSPIRASYSVTLRVIFTSGDMSVYYMIVCLIAFTITLILNVTRLCMMSSHLRKTEKAINEFFRTEGAEKLQKAFEIAKRIPIITSAKTLELAKVTQFKTMEFARYIEELARSVPLPPLILNCRAFVEEMFEAVRVDDPDDLGERIKERPALNAQGGIYVINPEMGRSNSPGGDSDDGSLNEQGQEIAVQVSVHLQSETKSIDTESQGSSHFSPPDDIGSAESNCNYKDGAYENCQL
Protein: Peptidyl-prolyl cis-trans isomerase 9 (PPIase 9) (EC 5.2.1.8) (Cyclophilin-9) (Rotamase 9) (Q09637)
Organism: Caenorhabditis elegans
Function: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Thought to function as a catalyst in the folding and modification of cuticle collagens.
Interaction partners:
- Activator of Hsp90 ATPase AHSA1-like N-terminal domain-containing protein
- Co-chaperone protein daf-41
- Heat shock protein 90
- DnaJ homolog subfamily B member 13
- Stress-induced-phosphoprotein 1
- Probable cytochrome P450 CYP44
- Histidine kinase/HSP90-like ATPase domain-containing protein
- Putative cytochrome P450 CYP13A7
- Nsp1_C domain-containing protein
- Tetratricopeptide repeat protein 7B
Sequence:
MAAEKRVFLDISVDENLIGRIEIRLFVEDAPKTCENFRALCTGEVGMTPNNKARLHYKQNEFHRIVKKFMIQGGDITEGDGRGGFSIYGRYFDDEKFKLKHSRPYLLSMANKGPNSNSSQFFITTAAAPHCNGKHVVFGEVVKGQNVVDYIDNLAVDDKSKPLAKVLISNCGELVKKKKPLKTDEELAAALEEKNNNARDNEIPKCPKSWLYRDDDNEKKHEMRNDKRREYRSRRSRSRSHEKNRDYKKENRGDSSRSQPRRDENGITVRGRGGVRFRRERSATPEHWRRNAPTKWVHDSHKHPEEDLV
Protein: B-cell CLL/lymphoma 11A (Zinc finger protein) isoform 2 (B-cell CLL/lymphoma 11A (Zinc finger protein), isoform CRA_c) (D9YZV9)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MSRRKQGKPQHLSKREFSPEPLEAILTDDEPDHGPLGAPEGDHDLLTCGQCQMNFPLGDILIFIEHKRKQCNGSLCLEKAVDKPPSPSPIEMKKASNPVEVGIQVTPEDDDCLSTSSRGICPKQEHIADKLLHWRGLSSPRSAHGALIPTPGMSAEYAPQGICKDEPSSYTCTTCKQPFTSAWFLLQHAQNTHGLRIYLESEHGSPLTPRVGIPSGLGAECPSQPPLHGIHIADNNPFNLLRIPGSVSREASGLAEGRFPPTPPLFSPPPRHHLDPHRIERLGAEEMALATHHPSAFDRVLRLNPMAMEPPAMDFSRRLRELAGNTSSPPLSPGRPSPMQRLLQPFQPGSKPPFLATPPLPPLQSAPPPSQPPVKSKSCEFCGKTFKFQSNLVVHRRSHTGEKPYKCNLCDHACTQASKLKRHMKTHMHKSSPMTVKSDDGLSTASSPEPGTSDLVGSASSALKSVVAKFKSENDPNLIPENGDEEEEEDDEEEEEEEEEEEEELTESERVDYGFGLSLEAARHHENSSRGAVVGVGDESRALPDVMQGMVLSSMQHFSEAFHQVLGEKHKRGHLAEAEGHRDTCDEDSVAGESDRIDDGTVNGRGCSPGESASGGLSKKLLLGSPSSLSPFSKRIKLEKEFDLPPAAMPNTENVYSQWLAGYAASRQLKDPFLSFGDSRQSPFASSSEHSSENGSLRFSTPPGELDGGISGRSGTGSGGSTPHISGPGPGRPSSKEGRRSDTCSSHTPIRRSTQRAQDVWQFSDGSSRALKF
Protein: Amyloid-beta A4 precursor protein-binding family A member 1 (Adapter protein X11alpha) (Neuron-specific X11 protein) (Neuronal Munc18-1-interacting protein 1) (Mint-1) (O35430)
Organism: Rattus norvegicus (Rat)
Function: Putative function in synaptic vesicle exocytosis by binding to Munc18-1, an essential component of the synaptic vesicle exocytotic machinery. May modulate processing of the amyloid-beta precursor protein (APP) and hence formation of APP-beta.
Subcellular location: Cytoplasm {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Nucleus {ECO:0000269|PubMed:20531236}. Note=Only a small proportion of the protein is nuclear.; SUBCELLULAR LOCATION: [Isoform 2]: Golgi apparatus {ECO:0000250}.
Interaction partners:
- Peripheral plasma membrane protein CASK
- Syntaxin-binding protein 1
- Peripheral plasma membrane protein CASK
- Amyloid-beta precursor protein
- Protein lin-7 homolog B
- Syntaxin-1A
- Protein lin-7 homolog A
- Protein lin-7 homolog C
- Neurexin-1
- Kinesin-like protein KIF17
Sequence:
MNHLEGSAEVEVADEAPGGEVNESVEADLEHPEVEEEQQPSPPPPAGHAPEDHRAHPAPPPPPPPQEEEEERGECLARSASTESGFHNHTDTAEGDVLAAARDGYEAERAQDADDESAYAVQYRPEAEEYTEQAEAEHAEAAQRRALPNHLHFHSLEHEEAMNAAYSGYVYTHRLFHRAEDEPYAEPYADYGGLQEHVYEEIGDAPELEARDGLRLYERERDEAAAYRQEALGARLHHYDERSDGESDSPEKEAEFAPYPRMDSYEQEEDIDQIVAEVKQSMSSQSLDKAAEDMPEAEQDLERAPTPGGGHPDSPGLPAPAGQQQRVVGTPGGSEVGQRYSKEKRDAISLAIKDIKEAIEEVKTRTIRSPYTPDEPKEPIWVMRQDISPTRDCDDQRPVDGDSPSPGSSSPLGAESSITPLHPGDPTEASTNKESRKSLASFPTYVEVPGPCDPEDLIDGIIFAANYLGSTQLLSDKTPSKNVRMMQAQEAVSRIKTAQKLAKSRKKAPEGESQPMTEVDLFISTQRIKVLNADTQEPMMDHPLRTISYIADIGNIVVLMARRRMPRSNSQENVEASHPSQDAKRQYKMICHVFESEDAQLIAQSIGQAFSVAYQEFLRANGINPEDLSQKEYSDLLNTQDMYNDDLIHFSKSENCKDVFIEKQKGEILGVVIVESGWGSILPTVIIANMMHGGPAEKSGKLNIGDQIMSINGTSLVGLPLSTCQSIIKGLKNQSRVKLNIVRCPPVTTVLIRRPDLRYQLGFSVQNGIICSLMRGGIAERGGVRVGHRIIEINGQSVVATPHEKIVHILSNAVGEIHMKTMPAAMYRLLTAQEQPVYI
Protein: rRNA adenine N(6)-methyltransferase (EC 2.1.1.-) (A0A0C4DGB1)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MPKVKSGAIGRRRGRQEQRRELKSAGGLMFNTGIGQHILKNPLIINSIIDKAALRPTDVVLEVGPGTGNMTVKLLEKAKKVVACELDPRLVAELHKRVQGTPVASKLQVLVGDVLKTDLPFFDTCVANLPYQISSPFVFKLLLHRPFFRCAILMFQREFALRLVAKPGDKLYCRLSINTQLLARVDHLMKVGKNNFRPPPKVESSVVRIEPKNPPPPINFQEWDGLVRITFVRKNKTLSAAFKSSAVQQLLEKNYRIHCSVHNIVSAAVYPVKQI
Protein: CUB-like domain-containing protein (Q9XUD5)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MLQKLLVCLSAIATVSAAGNGCKLGKVINKPVIEGTPVYWPPSWTETKPAPQLEKEQSCSWIVTIPRGYYAKLIISGKTTDKDSRFETVDAAGNLVQTSQENMEPYYFPGPKFTLAVSNEGSDTFAFKVVWFTLPIMNDDAAIGANGLVMNVTSQVIAMQYYSIGDSLTLMAFPVNPKNYYSLRSTLVFDGHDCTSFNYISNLYQLYQTKEQWVSSQDEIIIVNLEASSSNDKLLIQASKYLTGTGEMVELHPQANSIYNGTVNGGTQMSSLVAVTDLSMQMIDVQMESDATVTVYYGSPDASTLNKSYTRTQLKNALPLSFRGPFVQFVVSSGKAVFTFKS
Protein: Demilune cell and parotid protein 1 (L7N1X9)
Organism: Mus musculus (Mouse)
Interaction partners:
- Protein S100-A10
- Alpha- and gamma-adaptin-binding protein p34
- Demilune cell and parotid protein 2
- Caspase-1
- NACHT, LRR and PYD domains-containing protein 3
- Demilune cell and parotid protein 3
- Protein FAM72A
- BPI fold-containing family A member 2
Sequence:
MFQLEAMLALLILAFLGTPTVLTQDYHGPEVGKHSCTSAPEGKNITSIRVFLKGRLIVGIQLNYDDNKDGQVYGSTAGKEMVARLSKEEHIIAAQGTYTPSALTQIIFTTNQPRQLMVGYYVGNSEYSSFPNDPSHVLKGACVSWRAGGIKSILFLWGSENSSCVKYGHSG
Protein: AF4/FMR2 family member 3 (Lymphoid nuclear protein related to AF4) (Protein LAF-4) (P51827)
Organism: Mus musculus (Mouse)
Function: Putative transcription activator that may function in lymphoid development and oncogenesis.
Subcellular location: Nucleus.
Interaction partners:
- Protein AF-9
- Cyclin-dependent kinase 9
- Btk-PH-domain binding protein translocated to, 1)
- Cyclin-T1
- AF4/FMR2 family member 4
- RNA polymerase II elongation factor ELL
- ELL-associated factor 1
- Cyclin-T2
- RNA polymerase II elongation factor ELL3
- RNA polymerase II elongation factor ELL2
Sequence:
MDSFDLALLQEWDLESLWGEDILSQRNDSLVLEVQASASRCRSVYEPDRNALRRKERERRSQETQQDSGSFNSGYSLFSEPYKTNKGDELSNRIQNTLGNYDEMKDFLTDRSNQSHLVGVPKPGVPQTPVNKIDEHFGAESRAQPQPSTVCSTASSTPAAVPVQQGKRGAMGWQKAGHPPSDGQQRAAQQGSLRTLLGDGVGRQQTRAKQVCNMETGLQTQERPPAMAAKHGGSGHCVQNFPPSLASKPSLVQQKPTAYVRPMDGQDQAPDESPKLKSSTETAVHCTAYRGVPANKPESARAKAKLAKFSIPKQAEESRSGENNSCVEEIIREMTWLPPLSAIQAPAKVEPSKFPFPNKDSQLVSSGHSNPKKADAEPGSPDNGASNTSTLEDDLKLSSDDEEGEQQAAQRTALRALADSSVVQQTNCRGSAPSSKGGGSSSSSGGSSSSSDSESTSGSDSETESSSSSSESEGSKPPHCSSPEAEPASSNKWQLDKWLNKVNPHKPPILIQNESHGPERNQYYTPPVKDEGQDCGKLPEICQASLRDKELKTTCKEEQRPRTANKAPGSKSVKQKSPPAAVAVTAAALPPAVPSAPTESAPAPTRRSAGKKPTRRTERTSAGDGANCHRPEEPVAPDTLGASVVGPLEPPKTRPCGNNRTGHRKELRSSVTCEKRRTRGLSRIVPKSKEFIETESSSSSSSSDSDLESEQEEYVLSKAPTTTGSEQRLKEAASSNNNSNSNSSTSRASVGSINARTTSDIAKELEEQFYTLVPFGRNELLSPLKDSDEVRSLWVKIDLTLLSRIPEHLSQEPGVLSAPSAKDTDSAPASHALDAPAEKTLPKSKRKRKCDNEDDYREIKKVQGRKESASRLAASTNNTLSGNHCNVNVNSLAIPINKNEKMLRSPTSPLSDTCKHKYASEDLTSSSRPHGNGLLTSASSNKEPKAESQLQTIAGDLTKASHNSSENGTLHSKSRPQTEPWSPGSNGHRDCKRQKLIFDDMPRSADYFMREAKRMKHKADAMVEKFGKALNYAEAALSFIECGNAMEQGPMESKSPYTMYSETVELIRYAMRLKTHSGPNATPEDKQLAALCYRCLALLYWRMFRLKRDHAVKYSKALIDYFKNSSKAAQAPSPWGSSGKSTGSPSPMSPNPSPASSVGSQGSLSSSSGLSPSTIVSIPQRIHQMAANHVSITNSILHSYDYWEMADNLAKENREFFNDLDLLMGPVTLHSSMEHLVQYSQQGLHWLRSSVHLS
Protein: Ras-related protein Rab-39B (Q96DA2)
Organism: Homo sapiens (Human)
Function: Small GTPases Rab involved in autophagy. The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes. Rabs cycle between an inactive GDP-bound form and an active GTP-bound form that is able to recruit to membranes different sets of downstream effectors directly responsible for vesicle formation, movement, tethering and fusion. May regulate the homeostasis of SNCA/alpha-synuclein. Together with PICK1 proposed to ensure selectively GRIA2 exit from the endoplasmic reticulum to the Golgi and to regulate AMPAR compostion at the post-synapses and thus synaptic transmission (By similarity).
Subcellular location: Cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Cytoplasmic vesicle membrane {ECO:0000269|PubMed:26399558}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Golgi apparatus {ECO:0000269|PubMed:20159109, ECO:0000269|PubMed:24349490}. Note=Partial colocalization with markers that cycle from the cell surface to the trans-Golgi network. {ECO:0000250|UniProtKB:Q8BHC1}.
Interaction partners:
- Guanine nucleotide exchange factor C9orf72
- Guanine nucleotide exchange protein SMCR8
- WD repeat-containing protein 41
- Sequestosome-1
- Rab GDP dissociation inhibitor alpha
- Ras-related protein Rab-8A
Sequence:
MEAIWLYQFRLIVIGDSTVGKSCLIRRFTEGRFAQVSDPTVGVDFFSRLVEIEPGKRIKLQIWDTAGQERFRSITRAYYRNSVGGLLLFDITNRRSFQNVHEWLEETKVHVQPYQIVFVLVGHKCDLDTQRQVTRHEAEKLAAAYGMKYIETSARDAINVEKAFTDLTRDIYELVKRGEITIQEGWEGVKSGFVPNVVHSSEEVVKSERRCLC
Protein: Sal-like protein 2 (Zinc finger protein 795) (Zinc finger protein SALL2) (Zinc finger protein Spalt-2) (Sal-2) (hSal2) (Q9Y467)
Organism: Homo sapiens (Human)
Function: Probable transcription factor that plays a role in eye development before, during, and after optic fissure closure.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- POU domain, class 3, transcription factor 2
- Transcription factor SOX-2
Sequence:
MSRRKQRKPQQLISDCEGPSASENGDASEEDHPQVCAKCCAQFTDPTEFLAHQNACSTDPPVMVIIGGQENPNNSSASSEPRPEGHNNPQVMDTEHSNPPDSGSSVPTDPTWGPERRGEESSGHFLVAATGTAAGGGGGLILASPKLGATPLPPESTPAPPPPPPPPPPPGVGSGHLNIPLILEELRVLQQRQIHQMQMTEQICRQVLLLGSLGQTVGAPASPSELPGTGTASSTKPLLPLFSPIKPVQTSKTLASSSSSSSSSSGAETPKQAFFHLYHPLGSQHPFSAGGVGRSHKPTPAPSPALPGSTDQLIASPHLAFPSTTGLLAAQCLGAARGLEATASPGLLKPKNGSGELSYGEVMGPLEKPGGRHKCRFCAKVFGSDSALQIHLRSHTGERPYKCNVCGNRFTTRGNLKVHFHRHREKYPHVQMNPHPVPEHLDYVITSSGLPYGMSVPPEKAEEEAATPGGGVERKPLVASTTALSATESLTLLSTSAGTATAPGLPAFNKFVLMKAVEPKNKADENTPPGSEGSAISGVAESSTATRMQLSKLVTSLPSWALLTNHFKSTGSFPFPYVLEPLGASPSETSKLQQLVEKIDRQGAVAVTSAASGAPTTSAPAPSSSASSGPNQCVICLRVLSCPRALRLHYGQHGGERPFKCKVCGRAFSTRGNLRAHFVGHKASPAARAQNSCPICQKKFTNAVTLQQHVRMHLGGQIPNGGTALPEGGGAAQENGSEQSTVSGARSFPQQQSQQPSPEEELSEEEEEEDEEEEEDVTDEDSLAGRGSESGGEKAISVRGDSEEASGAEEEVGTVAAAATAGKEMDSNEKTTQQSSLPPPPPPDSLDQPQPMEQGSSGVLGGKEEGGKPERSSSPASALTPEGEATSVTLVEELSLQEAMRKEPGESSSRKACEVCGQAFPSQAALEEHQKTHPKEGPLFTCVFCRQGFLERATLKKHMLLAHHQVQPFAPHGPQNIAALSLVPGCSPSITSTGLSPFPRKDDPTIP
Protein: Prokineticin-1 (Endocrine-gland-derived vascular endothelial growth factor) (EG-VEGF) (Q8R414)
Organism: Rattus norvegicus (Rat)
Function: Potently contracts gastrointestinal (GI) smooth muscle. Induces proliferation, migration and fenestration (the formation of membrane discontinuities) in capillary endothelial cells derived from endocrine glands. Has little or no effect on a variety of other endothelial and non-endothelial cell types. Induces proliferation and differentiation, but not migration, of enteric neural crest cells. Directly influences neuroblastoma progression by promoting the proliferation and migration of neuroblastoma cells. Positively regulates PTGS2 expression and prostaglandin synthesis. May play a role in placentation. May play a role in normal and pathological testis angiogenesis (By similarity).
Subcellular location: Secreted {ECO:0000250}.
Interaction partners:
- Prokineticin receptor 1
- Prokineticin receptor 2
Sequence:
MRGAVQVFIMLLLATVSDCAVITGACERDVQCGAGTCCAISLWLRGLRLCTPLGREGEECHPGSHKIPFFRKRQHHTCPCSPSLLCSRFPDGRYRCSQDLKNVNF
Protein: Ponticulin-like protein C2 (Q54LC3)
Organism: Dictyostelium discoideum (Social amoeba)
Subcellular location: Cell membrane {ECO:0000305}; Lipid-anchor, GPI-anchor {ECO:0000305}.
Interaction partners:
- CMP/dCMP-type deaminase domain-containing protein
- PhoPQ-activated pathogenicity-related protein
- Probable phosphoglycerate mutase
- Secreted protein A
Sequence:
MKFTKPLLLLIVAIIASSNAAETFSNFQVTNSDASSPCVTTPVELKVNTCQSACGSILNVLPVTGSTSKFTFNQFGAQDTKCAATPTSSNEFTCVDGKSKVAIGTTTYSVVCVPDKTNSSESDSSDSTRIGASFALFALALLSMLAL
Protein: Putative pheromone response factor (Q8T0X9)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MKATFTILVLQVVICLAGATEYQLTLDKDGLLAPCENQPGNPSGFEAMVDTSSLKVHNLGSKVRIEGEQKVVWKDVQPGDTLKVFGQVYRLDKGTWQKTMFTASSNNFCKNMFDKNQYWYNFWTKYISNSDEIKEKCLTTPGAVLKYKDYELDLKTSLNVPNLDGRYKLVVQIEAFDKRNVRRPVPICIEFRGTSGQV
Protein: Sushi domain containing 5 (G3UW60)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MSAGPLWPAPGSLPALCAALLLLALQPPPVRAEGKLFMLGSQNGSQGLDLEAARLSCRSRGAHLVSAAELKRVVRDCASAVCTTGWLADGTLGTTVCSKGSGEQPVSRAVDVRIDSHPVPGAKYNALCIKDEERPCGDPPSFPHTILQGRTGLEMGDELLYLCAPGSVPGHRETAFTLLCNSCGEWYGLVQACGKDEAEAHIDYEENFPDDRSVSFRELMEDSRAEGEKEKAQEDASDETPKQDRLVFTSVSKENIAQVKAFVPTTGSPGAGGSVRTDWPRSRLHRKYSLWFPAETFHKPELGKDEGDETKEPLPARDNHSEEKPAPEESETRLVYATTYSPSEPFVDRNDSKAEDPGVSSSDDSWLDGYPVTDGAWRKVEAGQEDDEDKGDGSVGPDESGLTTPDKEPENVTVTPSESVIHSSISPSQMLDVEALVPGPINVSETESSHTRDVDSTSSQSTIPRRVTTQPSPKVTSPHELASSTQETVTTTLQPTHKRTPSTDVEATQPPAGVTAPEVQDNFPYLLSEDFLGQEGPGPGASEKFLPTSAPCVGDECPSFRKGPVIATVVTVLCLLLLLVVAGAVWGYRRCQHKSSVYKLNVGQRQARHYQQQIEMEKV
Protein: Structural maintenance of chromosomes protein 2 (SMC protein 2) (SMC-2) (Chromosome assembly protein XCAP-E) (Chromosome-associated protein E) (P50533)
Organism: Xenopus laevis (African clawed frog)
Function: Central component of the condensin complex, a complex required for conversion of interphase chromatin into mitotic-like condense chromosomes. The condensin complex probably introduces positive supercoils into relaxed DNA in the presence of type I topoisomerases and converts nicked DNA into positive knotted forms in the presence of type II topoisomerases.
Subcellular location: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}. Chromosome {ECO:0000250}. Note=In interphase cells, the majority of the condensin complex is found in the cytoplasm, while a minority of the complex is associated with chromatin. A subpopulation of the complex however remains associated with chromosome foci in interphase cells. During mitosis, most of the condensin complex is associated with the chromatin. At the onset of prophase, the regulatory subunits of the complex are phosphorylated by CDC2, leading to condensin's association with chromosome arms and to chromosome condensation. Dissociation from chromosomes is observed in late telophase (By similarity). {ECO:0000250}.
Interaction partners:
Sequence:
MHVKSIIIDGFKSYAQRTEINGFDPLFNAITGLNGSGKSNILDSICFLLGISNLTQVRASNLQDLVYKNGQAGITKATVSITFDNYDKKQSPLGFEAHDEITVTRQVVIGGRNKYLINGVNANNTRVQDLFCSVGLNVNNPHFLIMQGRITKVLNMKPPEILAMIEEAAGTRMYECKKIAAQKTIEKKEAKLKEIQTILEEEITPTIHKLKEERSSYLEYQKIMREIEHLSRLYVAYQFVCAEETKVRSAEELKEMQDSILKLQDTMAENERKVKELGKEIAELEKMRDQEVGGALRSLEEALSEAQRADTKVQSALDLKKQNMKAEREKKRKELVKSMEEDAKVLTAKEKEVKKITDGLSSLQEASQKDVEAFTSAQQHFNAVSAGLSSNEDGEEATLAGQMMACKNETSKAETEAKQAQMKLKHAQQELKTKQAEVKKMDGGYKKDNEAFEAVKKSKEKLEVEMKKLNYEDGREEQLLEKRRGLSRDVNRLREAYESLMARFPNLQFEYKDPEKNWDSDRVKGLVASLISIKDVSTATALEVVAGGRLYNVVVDTEVTGKKLLEKGELKRRFTIIPLNKISARCLGKDTVNVAKNLVGADNVNLALSLVGYESELQKAMEYVFGTTLVCDTMDNAKKVTFDKRIMTKTVTLGGDTFDPQGTLSGGARSQNASVLVRLQELKDVQDELKAKETELQEVEKELMTLKNTVERYRQLKQQWEMKSEEAELLQTKLQQSSYHKQQEELDSLKQTIEESEETLKNTKEVQKKAEEKFKVLEHKMKNAEAERERELKEAQQKLDTAKKKADASNKKMKEKQQEVDALVLELEELKREQTTYKQQIETVDEAMKAYQEQADSMASEVSKNKEAVKKAQDELAKQKEIIMGHDKEIKTKSSEAGKLRENNNDLQLKIKELEHNISKHKKDSADAAAKVAKMLNDYEWIASEKHLFGQANTAYDFKTNNPKEAGQRLHKLQEKKEKLGRNVNMRAMNMLTQAEERYNDLMKRKRIVENDKSKILTTIEELDQKKNEALNIAWQKVNKDFGSIFSTLLPGANAMLAPPEGQSVLDGLEFKVALGNTWKENLTELSGGQRSLVALSLILAMLLFKPAPIYILDEVDAALDLSHTQNIGQMLRTHFRHSQFIVVSLKDGMFNNANVLFKTKFVDGVSTVARFAQNQNGGSSAGQQRSDKSKTKERRNRMEVDK
Protein: Sperm acrosome-associated protein 9 (Acrosome and sperm tail protein) (MAST) (Q7TPM5)
Organism: Mus musculus (Mouse)
Function: Microtubule inner protein (MIP) part of the dynein-decorated doublet microtubules (DMTs) of multiciliated respiratory cells and the distal singlet microtubules of monoflagellated spermatozoa. May stabilize the protofilaments to which they are bound.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:24256100}. Cytoplasmic vesicle, secretory vesicle, acrosome {ECO:0000269|PubMed:24256100}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000269|PubMed:27914912}. Cytoplasm, cytoskeleton, flagellum axoneme {ECO:0000269|PubMed:27914912, ECO:0000269|PubMed:37865089, ECO:0000269|PubMed:37989994}. Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000250|UniProtKB:Q96E40}. Nucleus {ECO:0000250|UniProtKB:Q4V8P4}. Note=In caudal sperms localizes onto sperm head. Is also present on midpiece and principle piece of sperm tails. Acrosome and sperm tail localization is regulated by Y-chromosome. {ECO:0000269|PubMed:24256100}.
Interaction partners:
- Cilia- and flagella-associated protein 90
- Cilia- and flagella-associated protein 144
- Protein FAM209
- Uncharacterized protein C11orf97 homolog
- Adenylate kinase 8
- Ankyrin repeat domain 29
Sequence:
MNEVKESLRSIEQKYKLFQQQQFTFIAALEHCRENAHDKIRPISSIEQVQSYMEHYCNNSTHRRILIMFMDICSELSKLCQHFEALHSGTPVTNSLLEKCKTLVSQSNDLSSLRAKYPHEVVNHLSCDEARNHYGGVVSLIPIVLDFMKEWIAHSEKLPRKVLQHGTT
Protein: Neuronal PAS domain-containing protein 3 (Neuronal PAS3) (Basic-helix-loop-helix-PAS protein MOP6) (Class E basic helix-loop-helix protein 12) (bHLHe12) (Member of PAS protein 6) (PAS domain-containing protein 6) (Q8IXF0)
Organism: Homo sapiens (Human)
Function: May play a broad role in neurogenesis. May control regulatory pathways relevant to schizophrenia and to psychotic illness (By similarity).
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981, ECO:0000269|PubMed:12746393}.
Interaction partners:
- Aryl hydrocarbon receptor nuclear translocator 2
- Mitochondrial ribonuclease P catalytic subunit
- Aryl hydrocarbon receptor nuclear translocator
Sequence:
MAPTKPSFQQDPSRRERITAQHPLPNQSECRKIYRYDGIYCESTYQNLQALRKEKSRDAARSRRGKENFEFYELAKLLPLPAAITSQLDKASIIRLTISYLKMRDFANQGDPPWNLRMEGPPPNTSVKVIGAQRRRSPSALAIEVFEAHLGSHILQSLDGFVFALNQEGKFLYISETVSIYLGLSQVELTGSSVFDYVHPGDHVEMAEQLGMKLPPGRGLLSQGTAEDGASSASSSSQSETPEPVESTSPSLLTTDNTLERSFFIRMKSTLTKRGVHIKSSGYKVIHITGRLRLRVSLSHGRTVPSQIMGLVVVAHALPPPTINEVRIDCHMFVTRVNMDLNIIYCENRISDYMDLTPVDIVGKRCYHFIHAEDVEGIRHSHLDLLNKGQCVTKYYRWMQKNGGYIWIQSSATIAINAKNANEKNIIWVNYLLSNPEYKDTPMDIAQLPHLPEKTSESSETSDSESDSKDTSGITEDNENSKSDEKGNQSENSEDPEPDRKKSGNACDNDMNCNDDGHSSSNPDSRDSDDSFEHSDFENPKAGEDGFGALGAMQIKVERYVESESDLRLQNCESLTSDSAKDSDSAGEAGAQASSKHQKRKKRRKRQKGGSASRRRLSSASSPGGLDAGLVEPPRLLSSPNSASVLKIKTEISEPINFDNDSSIWNYPPNREISRNESPYSMTKPPSSEHFPSPQGGGGGGGGGGGLHVAIPDSVLTPPGADGAAARKTQFGASATAALAPVASDPLSPPLSASPRDKHPGNGGGGGGGGGGAGGGGPSASNSLLYTGDLEALQRLQAGNVVLPLVHRVTGTLAATSTAAQRVYTTGTIRYAPAEVTLAMQSNLLPNAHAVNFVDVNSPGFGLDPKTPMEMLYHHVHRLNMSGPFGGAVSAASLTQMPAGNVFTTAEGLFSTLPFPVYSNGIHAAQTLERKED