wanglab/gogpt-training-data huggingface dataset:
Protein: E3 ubiquitin-protein ligase MARCHF1 (EC 2.3.2.27) (Membrane-associated RING finger protein 1) (Membrane-associated RING-CH protein I) (MARCH-I) (RING-type E3 ubiquitin transferase MARCHF1) (Q6NZQ8)
Organism: Mus musculus (Mouse)
Function: E3 ubiquitin-protein ligase that mediates ubiquitination of TFRC, CD86, FAS and MHC class II proteins, such as HLA-DR alpha and beta, and promotes their subsequent endocytosis and sorting to lysosomes via multivesicular bodies. By constitutively ubiquitinating MHC class II proteins in immature dendritic cells, down-regulates their cell surface localization thus sequestering them in the intracellular endosomal system.
Subcellular location: Cytoplasmic vesicle membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000255}. Late endosome membrane {ECO:0000269|PubMed:19880452}; Multi-pass membrane protein {ECO:0000255}. Early endosome membrane {ECO:0000269|PubMed:19880452}; Multi-pass membrane protein {ECO:0000255}. Golgi apparatus, trans-Golgi network membrane {ECO:0000269|PubMed:19880452}; Multi-pass membrane protein {ECO:0000255}. Lysosome membrane {ECO:0000269|PubMed:19880452}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MLGWCEAIARNPHRIPNTTRTPETSGDVADASQTSTLNEKSPGRSASRSSNISKASSPTTGTAPRSQSRLSVCPSTQDICRICHCEGDEESPLITPCRCTGTLRFVHQSCLHQWIKSSDTRCCELCKYDFIMETKLKPLRKWEKLQMTTSERRKIFCSVTFHVIAVTCVVWSLYVLIDRTAEEIKQGNDNGVLEWPFWTKLVVVAIGFTGGLVFMYVQCKVYVQLWRRLKAYNRVIFVQNCPDTANKLEKNFPCNVNTEIKDAVVVPVPQTGSNTLPTAEGAPPEVIPV
Protein: Immunoglobulin lambda constant 1 (Ig lambda chain C region MGC) (Ig lambda-1 chain C region) (P0CG04)
Organism: Homo sapiens (Human)
Function: Constant region of immunoglobulin light chains. Immunoglobulins, also known as antibodies, are membrane-bound or secreted glycoproteins produced by B lymphocytes. In the recognition phase of humoral immunity, the membrane-bound immunoglobulins serve as receptors which, upon binding of a specific antigen, trigger the clonal expansion and differentiation of B lymphocytes into immunoglobulins-secreting plasma cells. Secreted immunoglobulins mediate the effector phase of humoral immunity, which results in the elimination of bound antigens. The antigen binding site is formed by the variable domain of one heavy chain, together with that of its associated light chain. Thus, each immunoglobulin has two antigen binding sites with remarkable affinity for a particular antigen. The variable domains are assembled by a process called V-(D)-J rearrangement and can then be subjected to somatic hypermutations which, after exposure to antigen and selection, allow affinity maturation for a particular antigen.
Subcellular location: Secreted {ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414}. Cell membrane {ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414}.
Interaction partners:
Sequence:
GQPKANPTVTLFPPSSEELQANKATLVCLISDFYPGAVTVAWKADGSPVKAGVETTKPSKQSNNKYAASSYLSLTPEQWKSHRSYSCQVTHEGSTVEKTVAPTECS
Protein: Probable Sn-glycerol-3-phosphate-binding lipoprotein UgpB (P71619)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- Trehalose import ATP-binding protein SugC
- Probable Sn-glycerol-3-phosphate transport integral membrane protein ABC transporter UgpA
- Probable Sn-glycerol-3-phosphate transport integral membrane protein ABC transporter UgpE
- Trehalose transport system permease protein SugB
- Probable sugar-transport integral membrane protein ABC transporter UspB
- Trehalose transport system permease protein SugA
- Probable sugar-transport integral membrane protein ABC transporter
- Trehalose import ATP-binding protein SugC
- Probable sugar-transport integral membrane protein ABC transporter UspA
- Probable sugar-transport integral membrane protein ABC transporter
Sequence:
MDPLNRRQFLALAAAAAGVTAGCAGMGGGGSVKSGSGPIDFWSSHPGQSSAAERELIGRFQDRFPTLSVKLIDAGKDYDEVAQKFNAALIGTDVPDVVLLDDRWWFHFALSGVLTALDDLFGQVGVDTTDYVDSLLADYEFNGRHYAVPYARSTPLFYYNKAAWQQAGLPDRGPQSWSEFDEWGPELQRVVGAGRSAHGWANADLISWTFQGPNWAFGGAYSDKWTLTLTEPATIAAGNFYRNSIHGKGYAAVANDIANEFATGILASAVASTGSLAGITASARFDFGAAPLPTGPDAAPACPTGGAGLAIPAKLSEERKVNALKFIAFVTNPTNTAYFSQQTGYLPVRKSAVDDASERHYLADNPRARVALDQLPHTRTQDYARVFLPGGDRIISAGLESIGLRGADVTKTFTNIQKRLQVILDRQIMRKLAGHG
Protein: Matrilysin (EC 3.4.24.23) (Matrin) (Matrix metalloproteinase-7) (MMP-7) (Pump-1 protease) (Uterine metalloproteinase) (Q10738)
Organism: Mus musculus (Mouse)
Function: Degrades casein, gelatins of types I, III, IV, and V, and fibronectin. Activates procollagenase (By similarity).
Subcellular location: Secreted, extracellular space, extracellular matrix {ECO:0000305}.
Interaction partners:
- Metalloproteinase inhibitor 3
- CD44 antigen
- Stromelysin-1
- 72 kDa type IV collagenase
- Metalloproteinase inhibitor 1
- Osteopontin
- Metalloproteinase inhibitor 2
- Cathepsin K
- Nidogen-1
- Neutrophil collagenase
Sequence:
MQLTLFCFVCLLPGHLALPLSQEAGDVSAHQWEQAQNYLRKFYPHDSKTKKVNSLVDNLKEMQKFFGLPMTGKLSPYIMEIMQKPRCGVPDVAEYSLMPNSPKWHSRIVTYRIVSYTSDLPRIVVDQIVKKALRMWSMQIPLNFKRVSWGTADIIIGFARRDHGDSFPFDGPGNTLGHAFAPGPGLGGDAHFDKDEYWTDGEDAGVNFLFAATHEFGHSLGLSHSSVPGTVMYPTYQRDYSEDFSLTKDDIAGIQKLYGKRNTL
Protein: Organic cation/carnitine transporter 2 (High-affinity sodium-dependent carnitine cotransporter) (Solute carrier family 22 member 5) (Q9Z0E8)
Organism: Mus musculus (Mouse)
Function: Sodium-ion dependent, high affinity carnitine transporter. Involved in the active cellular uptake of carnitine. Transports one sodium ion with one molecule of carnitine. Also transports organic cations such as tetraethylammonium (TEA) without the involvement of sodium. Also relative uptake activity ratio of carnitine to TEA is 11.3. May also contribute to regulate the transport of organic compounds in testis across the blood-testis-barrier (By similarity).
Subcellular location: Apical cell membrane {ECO:0000269|PubMed:15523054, ECO:0000269|PubMed:20722056}; Multi-pass membrane protein {ECO:0000269|PubMed:15523054}. Basal cell membrane {ECO:0000250|UniProtKB:O76082}; Multi-pass membrane protein {ECO:0000255}. Cell membrane {ECO:0000250|UniProtKB:O76082}; Multi-pass membrane protein {ECO:0000250|UniProtKB:O76082}. Note=Colocalizes with PDZK1 on apical membranes of kidney proximal tubules (PubMed:15523054). In intestinal cells, apical expression is induced by TNF (PubMed:20722056). {ECO:0000269|PubMed:15523054, ECO:0000269|PubMed:20722056}.
Interaction partners:
- Solute carrier family 2, facilitated glucose transporter member 9
Sequence:
MRDYDEVTAFLGEWGPFQRLIFFLLSASIIPNGFNGMSIVFLAGTPEHRCLVPHTVNLSSAWRNHSIPLETKDGRQVPQKCRRYRLATIANFSELGLEPGRDVDLEQLEQESCLDGWEYDKDVFLSTIVTEWDLVCKDDWKAPLTTSLFFVGVLMGSFISGQLSDRFGRKNVLFLTMGMQTGFSFLQVFSVNFEMFTVLFVLVGMGQISNYVAAFVLGTEILSKSIRIIFATLGVCIFYAFGFMVLPLFAYFIRDWRMLLLALTVPGVLCGALWWFIPESPRWLISQGRIKEAEVIIRKAAKINGIVAPSTIFDPSELQDLNSTKPQLHHIYDLIRTRNIRVITIMSIILWLTISVGYFGLSLDTPNLHGDIYVNCFLLAAVEVPAYVLAWLLLQYLPRRYSISAALFLGGSVLLFMQLVPSELFYLSTALVMVGKFGITSAYSMVYVYTAELYPTVVRNMGVGVSSTASRLGSILSPYFVYLGAYDRFLPYILMGSLTILTAILTLFFPESFGVPLPDTIDQMLRVKGIKQWQIQSQTRMQKDGEESPTVLKSTAF
Protein: Replication Factor A 28 kDa subunit, putative (Q57ZN9)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Replication protein A subunit
- BRCT domain-containing protein
- DNA polymerase eta
- DNA primase
- DNA primase large subunit
- DNA polymerase alpha subunit B
- DNA polymerase
- Uncharacterized protein
- Exonuclease, putative
- Endo/exonuclease Mre11
Sequence:
MEGSGSNFFTGAAANSNAATQQRRVHPIRPVTIKQLLEAQRVGEGVTVIDGREVTQATVVGRVVGYENDSDNRFSGGALTAKHHGYRITDGTGVVVVRQWMDADQQDDPLPLQCYVRAAGTVKMWQNSPIVTGTVRLVSDCNELNYHFLDVILTHLRLTQGSRRPSSAAPAAVPNTASAVGVQNMFPGGDGKVFTTDVVINTIRQKARGEEGLSMDEISAAALQYGFSGQDVRNAIRTLMEEGKIYQTHDCKFGI
Protein: Peptidyl-prolyl cis-trans isomerase CYP18-2 (PPIase CYP18-2) (EC 5.2.1.8) (Cyclophilin of 18 kDa 2) (Cyclophilin-18-2) (Q9SIH1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Pre-mRNA-splicing factor SYF2
- Pre-mRNA-processing-splicing factor 8A
- DExH-box ATP-dependent RNA helicase DExH12
- Cell division cycle 5-like protein
- P-loop containing nucleoside triphosphate hydrolases superfamily protein
- CwfJ-like family protein
- UPF0235 protein At5g63440
- At2g29210/F16P2.41
- Pre-mRNA-splicing factor ATP-dependent RNA helicase DEAH7
- 7-dehydrocholesterol reductase-like protein
Sequence:
MSARPEGSPPEVTLETSMGPFTVEMYYKHSPRTCRNFLELSRRGYYDNVLFHRIVKDFIVQGGDPTGTGRGGESIYGSKFEDEINKELKHTGAGILSMANAGPNTNGSQFFITLAPQPSLDGKHTIFGRVCRGMEVIKRLGSVQTDNTDRPIHEVKILRTKVID
Protein: Peptidyl-prolyl cis-trans isomerase FKBP5 (PPIase FKBP5) (EC 5.2.1.8) (51 kDa FK506-binding protein) (51 kDa FKBP) (FKBP-51) (54 kDa progesterone receptor-associated immunophilin) (Androgen-regulated protein 6) (FF1 antigen) (FK506-binding protein 5) (FKBP-5) (FKBP54) (p54) (HSP90-binding immunophilin) (Rotamase) (Q13451)
Organism: Homo sapiens (Human)
Function: Immunophilin protein with PPIase and co-chaperone activities. Component of unligated steroid receptors heterocomplexes through interaction with heat-shock protein 90 (HSP90). Plays a role in the intracellular trafficking of heterooligomeric forms of steroid hormone receptors maintaining the complex into the cytoplasm when unliganded. Acts as a regulator of Akt/AKT1 activity by promoting the interaction between Akt/AKT1 and PHLPP1, thereby enhancing dephosphorylation and subsequent activation of Akt/AKT1. Interacts with IKBKE and IKBKB which facilitates IKK complex assembly leading to increased IKBKE and IKBKB kinase activity, NF-kappaB activation, and IFN production.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q64378}. Nucleus {ECO:0000250|UniProtKB:Q64378}.
Interaction partners:
- Heat shock protein HSP 90-beta
- Glucocorticoid receptor
- Heat shock protein HSP 90-alpha
- PH domain leucine-rich repeat-containing protein phosphatase 1
- Prostaglandin E synthase 3
- Heat shock 70 kDa protein 4
- Progesterone receptor
- Peptidyl-prolyl cis-trans isomerase FKBP4
- RAC-alpha serine/threonine-protein kinase
- Serine/threonine-protein kinase mTOR
Sequence:
MTTDEGAKNNEESPTATVAEQGEDITSKKDRGVLKIVKRVGNGEETPMIGDKVYVHYKGKLSNGKKFDSSHDRNEPFVFSLGKGQVIKAWDIGVATMKKGEICHLLCKPEYAYGSAGSLPKIPSNATLFFEIELLDFKGEDLFEDGGIIRRTKRKGEGYSNPNEGATVEIHLEGRCGGRMFDCRDVAFTVGEGEDHDIPIGIDKALEKMQREEQCILYLGPRYGFGEAGKPKFGIEPNAELIYEVTLKSFEKAKESWEMDTKEKLEQAAIVKEKGTVYFKGGKYMQAVIQYGKIVSWLEMEYGLSEKESKASESFLLAAFLNLAMCYLKLREYTKAVECCDKALGLDSANEKGLYRRGEAQLLMNEFESAKGDFEKVLEVNPQNKAARLQISMCQKKAKEHNERDRRIYANMFKKFAEQDAKEEANKAMGKKTSEGVTNEKGTDSQAMEEEKPEGHV
Protein: Cyclin T1 (D3ZC98)
Organism: Rattus norvegicus (Rat)
Interaction partners:
- Cyclin-dependent kinase 9
- Bromodomain containing 4
- Cyclin-dependent kinase 12
- ALF transcription elongation factor 4
- Cyclin-dependent kinase 13
- Cyclin-H
- Cyclin-dependent kinase 7
- Elongation factor for RNA polymerase II 2
- Cyclin T2
- Elongation factor for RNA polymerase II
Sequence:
MEGERKNNNKRWYFTREQLENSPSRRFGVDSDKELSYRQQAANLLQDMGQRLNVSQLTINTAIVYMHRFYMIQSFTQFHRYSMAPAALFLAAKVEEQPKKLEHVIKVAHTCLHPQESLPDTRSEAYLQQVQDLVILESIILQTLGFELTIDHPHTHVVKCTQLVRASKDLAQTSYFMATNSLHLTTFSLQYTPPVVACAYQAAMKTKPDDRGADENTSEQTILNMISQTSSDTTIAGLMSMSAASTGAVPSLPASEESSSSLTSVDMLQGERWLSSQPPFKLEASQGHRTSENLALIGVDHSLQHDGSNAFVSQKQTSKSVPSAKVSLKEYRAKHAEELAAQKRQLENMEANVKSQYAYAAQNLLSHDSHSSVILKMPIEGSENPERPFLDKADKSALKMRLPVAGGDKAASSKPEEIKMRIKVHSAGDKHNSVEDSVAKSREHKEKQRTHPSNHHHHHNHHSHKHSHLQLPVGPVSKRPSDPKHSSQTSTLAHKTYSLSSTLSSSSSTRKRGPPEETGAAVFDHPAKIAKSTKSSSLNFPFPPLPTMTQLPGHSSDTSGLPFSQPSCKTRVPHVKLDKGPPGANGHNTTQSIDYQDTVNMLHSLLSAQGVQPTQPPAFEFVHSYGEYMNPRAAGISRSGNTDKPRPPPLPSEPPPPLPPLPK
Protein: Cytohesin 1-like protein (Cytohesin-1a) (Q6PW01)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- ADP-ribosylation factor 6
- FERM domain-containing protein 4A
- ADP-ribosylation factor-like 4, like.
- ADP-ribosylation factor-like protein 4A
- Large ribosomal subunit protein mL45
Sequence:
MVLKSEDGVVPDDLTPEEQKELENIRRRKQELLDDIQRLKDEIAEVTSEIENLGSTEERKNMQRNKQVAMGRKKFNMDPKKGIQFLIENDLLKNTSEDIARFLYKGEGLNKTAIGDYLGERDDFNIQVLHAFVELHEFTDLNLVQALRQFLWSFRLPGEAQKIDRMMEAFAQRYCQCNPGVFQSTDTCYILSFAIIMLNTSLHNPNVKDKPTVERFISMNRGINDGGDLPEELLRNLYESIKNEPFKIPEDDGNDLTHTFFNPDREGWLLKLGGRVKTWKRRWFILTDNCLYYFEYTTDKEPRGIIPLENLSIREVEDKKPNCFELFIPDNKDQVIKACKTEADGRVVEGNHTFYRISAPTTEEKDEWMNSIKAAISRDPFYEMLAARKKKVSSMKRH
Protein: Protein LDB16 (Low dye-binding protein 16) (P25587)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: May be involved in protein-linked oligosaccharide phosphorylation since the deletion reduces the negative charge of the cell surface.
Subcellular location: Membrane {ECO:0000269|PubMed:14562095}; Multi-pass membrane protein {ECO:0000269|PubMed:14562095}. Lipid droplet {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Seipin
- Lipid droplet organization protein LDO45
- Lipid droplet organization protein LDO16
- Protein PET10
- Diacylglycerol O-acyltransferase 1
- Peroxisomal membrane protein PEX30
- Acyl-coenzyme A diphosphatase YFT2
Sequence:
MFVVDWSVQLCMGVISPLFRALVQLPLSIFVWNGFQLVALPINIPLRLFLGTSLSRLVAQTSTLDFYVVLTLFQYFAVLCAFGSIIGLIFGFILGVFHSICGVPSVYISLEWKRWFAPIRTVLERASTSIVNIMRGQTIAPIPMPKPNPTHISKPNMKKFHDEPGADDMTITHDVNCYITPCQTPTNEKIQHYNNDSFNTTTTDDEPTDIWDRSDTYQNSFVTNETLMSLSNRAKLRRNASDADIVNIKILRRNSR
Protein: PAN domain-containing protein At5g03700 (Q9LZR8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MEGLCLNSFTRVLLLLFVFLVFSHKWQRVNAVEPVLELVKGFEAKPDSSIDSFQPLLTDSNGNFSFGFLRVNGSRLSLAVTHPNLTDPLWVLDPTRSASWSHKTKLFFNGSLVIIDPSSRLEWSTHTNGDRLILRNDSNLQVVKTSTFVEWESFDFPGNTLVESQNFTSAMALVSPNGLYSMRLGSDFIGLYAKVSEESQQFYWKHSALQAKAKVKDGAGPILARINPNGYLGMYQTGSIPIDVEAFNSFQRPVNGLLILRLESDGNLRGYLWDGSHWALNYEAIRETCDLPNPCGPYSLCTPGSGCSCIDNRTVIGECTHAASSPADFCDKTTEFKVVRRDGVEVPFKELMDHKTTSSLGECEEMCVDNCKCFGAVYNNGSGFCYLVNYPIRTMLGVADPSKLGYFKVREGVGKKKSRVGLTVGMSLLAVIALVLMVAMVYVGFRNWRREKRVLEEDNGLSPGPYKNLGSDSFNSVEMSRR
Protein: RING/U-box superfamily protein (F4IIX4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MASLRPSFGSVLRDRNQRHNDDVVFKKNLKAQVKTAPPAISDESSENRVDSLIGNKRKKNNKSRPGSPEKPRTRKGNNFSDNLGGASSLVQIWEARLNRSNGGNSAIHSQSIEISSEASVQEIHLLAPSIDGESESENESKSPDQTVEIESGTLNSVSDIIRRLSNEQKLTASNNGGAVDMPIVKTPTLEKSSFQVVTCSPRIRGRQAYSDLLVHLERERHRELESLLGRNAVSRFPQRGRLQSMLRLRSLKRGLAIQDRHRGTTKSDLNRFQPSSTILHLREKLREKAANAAAEAGLKKGQQSTVETESMQSKETSGILHSPSTERLSPQKRNIEEAILRKNETETKMSYLQLKKAIVAEVLERESDNTSPLTSVTPQEPRILRNEEAGKLESGTEGTQETPFLETQEMSFQSGWEEQEEYEDEQSYYGDMSYDWFTEISRPRTYWEDLRKSRYLEVMNTKSDKDDICRLLERRTVSGFLQSGLREKIDKLIMSRVQIHPAHRIEEATKEEEKYDIGEEKDEDRDDLSQSSSQIFAPSPAGSWSSLDTGVTSTPTHNLHSTLQLEMSELRDSVKTCLDVNASLQKSVHLENPFKRKCCVCNETQVETLLYRCGHMCTCLRCANELQYNGGKCPICHAKILDVVRVFVDSRT
Protein: UspA domain-containing protein (A0A0H3LAL2)
Organism: Mycobacterium tuberculosis (strain ATCC 35801 / TMC 107 / Erdman)
Interaction partners:
Sequence:
MNQSHKPPSIVVGIDGSKPAVQAALWAVDEAASRDIPLRLLYAIEPDDPGYAAHGAAARKLAAAENAVRYAFTAVEAADRPVKVEVEITQERPVTSLIRASAAAALVCVGAIGVHHFRPERVGSTAAALALSAQCPVAIVRPHRVPIGRDAAWIVVEADGSSDIGVLLGAVMAEARLRDSPVRVVTCRQSGVGDTGDDVRASLDRWLARWQPRYPDVRVQSAAVHGELLDYLAGLGRSVHMVVLSASDQEHVEQLVGAPGNAVLQEAGCTLLVVGQQYL
Protein: Metacaspase-3 (EC 3.4.22.-) (TbMCA3) [Cleaved into: Large subunit p20; Small subunit p10] (Q8T8E6)
Organism: Trypanosoma brucei brucei
Function: Cysteine protease that cleaves specifically after arginine or lysine residues. In the bloodstream form, may cleave inactive metacaspase-4 MCA4 prior to MCA4 secretion.
Subcellular location: Recycling endosome {ECO:0000305|PubMed:16507595}.
Interaction partners:
Sequence:
MAVDPRCLLSLCSTISKASSAKGTNDFVKIGMELWQTAQPYLVQALGLQPPPPKVDVDAAVANAGDAHGEQPWVATPLPGQTVRALFIGINYYGTSAALSGCCNDVKQMLATLQKKGLPINEAVILVDEDNFPGRTDQPTRDNIVRYMAWLVKDAKPGDVLFFHYSGHGTQCKSRGDSDEKYDQCIAPVDFQKSGCIVDDDIHKLLFSRLPEKVRLTAVFDCCHSGSIMDLPFTYVCSGGEQASGTPHMKRIREGNDVLGDVMMISGCADEQTSADVKNTATFGTGSTGAGGAATQCITCMLMNNQSLSYGKLLIETRDMLKRKRFKQVPQLSASKAIDLDQTFSLTEMFSVDRSVQ
Protein: PH domain-containing protein (Q9XXM9)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MISERIQRSQSPVDVSLALSEDSTITITELNNRNGSTFNANSINATPVMRRRRSQMSGVRQRNYRILDQNESKYILQQQSAAAIEEKKGTLLRRKSSKKLIEPLPMIITPPVLMARTQCCAVCYKEKSTGYSVSSRTQSYPLEAMSSVTTDRSTEEETARLSFVSSSTGYSSARSSLRSSDGGDESNNNSAGNRDSAISNTFSLSSQSSARRSALLTKGSLTHLDRIAIELLDTERTYVEDLNAVIKGYMDFLVEDREKLKVTLDAISSLFGCIERIFAFNKQLYNQLDAADLDCVKMSRCFVESSGKFEDYIEYCTNYHRMMSTLYHLQQQPLVARALQERQLALNHSLQLSAYLLKPVQRILKYHLFLENILKNMPSTTHPEELIQVKRAHEVMTSQAARINDEKKKAEHIERVGQLQSTLQKWKADEIQISNLSAYGDLLLEATFRQAGSKTTRLLFLFEEMLLIVKQRGANYVCKDYIMCSNLMLNEWICPEEPLSFQVLSFDNPRAQYVFMASSMEQKRTWMQELKRMMLDHYSVEIPEKTKQLMLSIDNTRIVPFGRPEFAEVSMKNHKKVPKYLEKRRKSVDAKEESNRRRSLSASRLLGGSKTSISEPIKEEQKCTCHMNGGIYNGANPTTSKSIISHPSLTYQQSHPTQSTDPNYCRPPVCRTQSAATIDLNQVHITEPNSAAVMSSRSRYQQARNRRLPPRHNQESRSTSSRRMGEEEIDRTFDQLYEELVSFGDSTKPTVTSNRSQRLRSEAPQSTVTTITVAATPATATLSIAECANTRLRSKSLTRLDEYEAEPISLKPSIERRYSKVDQLKKRSRKYQVNQEPEAADVLRPSVGRFSLTDHEIIIHGEEPYKRSSGRQRTPLTAQQTAELDDYFPSSNSMNSAPQTCSSSATPSLMSIIRQYENA
Protein: Insulinoma-associated protein 1 (Zinc finger protein IA-1) (Q63ZV0)
Organism: Mus musculus (Mouse)
Function: Sequence-specific DNA-binding transcriptional regulator that plays a key role in neurogenesis and neuroendocrine cell differentiation during embryonic and/or fetal development. Binds to the consensus sequence 5'-[TG][TC][TC][TT][GA]GGG[CG]A-3' in target promoters. Acts as a transcriptional repressor of NEUROD1 and INS expression via its interaction with cyclin CCND1 in a cell cycle-independent manner. Negatively regulates skeletal muscle-specific gene expression in endocrine cells of the pituitary by inhibiting the Notch signaling pathway. Represses target gene transcription by recruiting chromatin-modifying factors, such as HDAC1, HDAC2, HDAC3, KDM1A and RCOR1 histone deacetylases. Binds to its own promoter, suggesting autoregulation as a self-control feedback mechanism. Competes with histone H3 for the same binding site on the histone demethylase complex formed by KDM1A and RCOR1, and thereby inhibits demethylation of histone H3 at 'Lys-4' (By similarity). Promotes the generation and expansion of neuronal basal progenitor cells in the developing neocortex. Involved in the differentiation of endocrine cells of the developing anterior pituitary gland, of the pancreas and intestine, and of sympatho-adrenal cells in the peripheral nervous system. Promotes cell cycle signaling arrest and inhibition of cellular proliferation.
Subcellular location: Nucleus {ECO:0000269|PubMed:12079283, ECO:0000269|PubMed:24227653}.
Interaction partners:
- Neurogenin-3
- Neurogenic differentiation factor 1
- Lysine-specific histone demethylase 1A
- Achaete-scute homolog 1
- Paired box protein Pax-6
Sequence:
MPRGFLVKRSKKSTPVSYRVRGGEDSDRALLLSPGCGGARAEPPVPSPGPLPPPPPPALAERAHAALAAALACAPGPPPPPPPGPRAAHFGNPEAAHPAPLYSPTRPVSREHEKHKYFERSFNLGSPVSAESFPTPAALLAGGGSGANGAGGGGGGTCGGDALLFAPAELKMGTAFSAGAEAARGPGTGPPLSPAAALRPPGKRPAPPAAVATEPPAKAAKAPSAKKPKAIRKLHFEDEVTTSPVLGLKIKEGPVEAPRGRAGGATRPLGEFICQLCKEEYADPFALAQHKCSRIVRVEYRCPECAKVFSCPANLASHRRWHKPRPVPAAARAPEPEAATRAEAREAAGGGSSDRDTPSPGGVSESGSEDGLYECHHCAKKFRRQAYLRKHLLAHHQALQAKGAPPPPPPPPPPAEDILAFYAGPDEKAPQEASGDGEAAGVLGLSATAQCHLCPVCGETFPSKGAQERHLRLLHAAQVFPCKYCPATFYSSPGLTRHINKCHPSENRQVILLQVPVRPAC
Protein: IPT/TIG domain-containing protein (Q54TD1)
Organism: Dictyostelium discoideum (Social amoeba)
Interaction partners:
Sequence:
MKYIFNILIIIFISFISLNNALDLNNNQNIAAQQLLNQLYGVNTQTPCTNSAFTCDNGNNGYLILTGINTGSGSGVVITTSFGLFTDLKSITIGPNFFVSTAFWTDINKLTKLNFLSINHVNQAIPNNIQLPPSLNDVIFQKMSVPLPELFFSSGKIQNLNIEDSANGFKYPVTLSSCQPGLSFVYMIVTFYAPLPNNIEICPNLGAVYLIINNDKSDSQYTNFAFPYLGYLPISDLALYFRYTDQDKIQKWEFPDTVLNLPMLNYLTIEGRGLKFPQNNLIDLSKYTKGTTMDFTDVGFLDSCATFGCIKFPESSNINFKNHLLIMNNLDYTNLESVRIEGNNYVQPLPTPSTVQHSKVKSFSLINSEFTGSIPFTNNFYCKFNPNVLRIHSNKLSGNVPSCFKCYPPNDIGGIILPNNFNDFTLSSTPPSTCPTLSFNKNIPLIKTNNVSFITITGVDFGWTFNTLSPTPSSNVVTIDSIIPNTQIVLRIPQGDGTGKDLVAQFGYNLQSTTFTYSYEIPTVLPKYRYVQVGGNYLMVISGTGFSYVYQNIAIINSVLSNQTLAIQSTKNPSQDQFTFSSSTPFNGMTEATSFTLSVKVGSQVSNQVSLTYYKEVSMTVKPLSTIGGVVTFAGIFKVGNPSLVSITIGGSVCTVNAVNPTSVTFTYPVLSVGTYDLVLVLQSSYEFTTQVTISQAPAPTILNKFDWTLSNGAVVLMIFGSSFSYVEPNIVEINSTPFSILATASSTEPGYDNLILPASAHSSIPQGALFTVSVTTMGQRSASATFYLIKPISMMAYNLYTIGGEMTYPGSFSTSNITIATLKFDELDIPITSLSPTEISFKYPYRSGPGTLTLTLVIGTIRSSKVITIINTPTPTLMNKYYWTTLGNGDLALTFYGKWFTYYYKNIINIDGIDYDSTPATASSLDYSYPDEIKLLNSTPKSLVVGSPFQVHVKIGSQITNLIQFIFIKSVTIDVLPLQSIGGIISFGGSYGTSDKSIVTFSINDVPCSVISISPTTIQFQYPVNGAGTYQLIYFVGGFEYKTNVTYITSPPPQVIYKYEWTTDDRLIINGKWFGYYDSNVIVLNDDVYQVNSAVASSTNPGYDSISLSSFSPTSSLSIGQAFTIKVMVQGQSSNVITFNYIDSIKVDVKDLNTTGGIVSFTGMYGVTDKSLVTLSINGSSCSVNSVSLNLITFRYPSLSGSPGQYPLLINVGGFENTTTVQYVVPENPTIFNNYKWSSDKTEIIIYGTAFSYDNLNNIIINGATFTSTLAFGSEVSDAISFSIENLSIVEGDIFTVQIETGGLVSNIVSFNYIKEIYLSNEENLYSFGSVGALFAGKFGTSNNSIVSLSINGLECKVIKITPTNIKFSYPPLSIGSQETLINIGGLYYFTMLNVVAPPSPTLLNSYYWSSSDIIVFKGSWFDYFTPNRVYINGEGFESSVASLNNGNDEITFNDNSPTSDLLIGDEFTVIVESGGQTSNSVTFIYLKSILITTSELNSTGGDVKFNGEYHVSDKSLAVLTIDGYNCDIIELTTNSITFSYPAKPGGNFNLLLKIGGFEVSTTVTYKSQSTTGGQSTTGGQSTTGGQSTTSNPTNQPSTTDDDELSISSKLLAPFMLLKIITIISFILF
Protein: Prokineticin-1 (Endocrine-gland-derived vascular endothelial growth factor) (EG-VEGF) (Q14A28)
Organism: Mus musculus (Mouse)
Function: Potently contracts gastrointestinal (GI) smooth muscle. Induces proliferation, migration and fenestration (the formation of membrane discontinuities) in capillary endothelial cells. 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.
Subcellular location: Secreted {ECO:0000250|UniProtKB:P58294}.
Interaction partners:
- Prokineticin receptor 1
- Prokineticin receptor 2
Sequence:
MRGAVHIFIMLLLATASDCAVITGACERDIQCGAGTCCAISLWLRGLRLCTPLGREGEECHPGSHKIPFLRKRQHHTCPCSPSLLCSRFPDGRYRCFRDLKNANF
Protein: RRM domain-containing protein (A8DYR9)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MITGSGAGSPKGGAASLLQNLNPALLQQLGGGQNYQAVASLLSLINGQQGQQQQHQQQQNVLGILGTVLSALGKLTEGGDDASAKSSSEKPRHQALMTSPAPTATSSTSSSASHHHQQHQQQLSQQQQQQQHPQQQGLGNPLLGNPAMAAQNQFDAITMAQIAHQQQMLALQGFAVQQGAPSQQQQGLAGGMAGAKTTSPVAASLANHQQIALTPFAGGAAALDHFQAMQQYALLANLQATGGVGVQATTSAAQMVGNGDVKGPDGANLFIYHLPQDFGDSDLINTFAPFGGILSAKVFIDKVTNLSKCFGFVSYENAQSATNAISAMNGFQIGSKRLKVQLKVDRGNPYNR
Protein: Ras-related protein Rab-37 (EC 3.6.5.2) (Q9JKM7)
Organism: Mus musculus (Mouse)
Subcellular location: Cytoplasmic vesicle. Cell projection, cilium {ECO:0000269|PubMed:38536817}. Note=Secretory granules (PubMed:10722846). Located mainly in the connecting cilia between the outer segment and inner segment and also observed in the outer plexiform layer, inner plexiform layer, and ganglion cell layer of the retinas (PubMed:38536817). {ECO:0000269|PubMed:10722846, ECO:0000269|PubMed:38536817}.
Interaction partners:
Sequence:
MTGTPGAATAGDGEAPERSPPFSPNYDLTGKVMLLGDSGVGKTCFLIQFKDGAFLSGTFIATVGIDSRNKVVTVDGARVKLQIWDTAGQERFRSVTHAYYRDAQALLLLYDITNQSSFDNIRAWLTEIHEYAQRDVVIMLLGNKADVSSERVIRSEDGETLAREYGVPFMETSAKTGMNVELAFLAIAKELKYRAGRQPDEPSFQIRDYVESQKKRSSCCSFV