Descriptions

The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.

Autoinhibitory domains (AIDs)

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

Autoinhibited structure

Activated structure

1 structures for Q640N1

Entry ID Method Resolution Chain Position Source
AF-Q640N1-F1 Predicted AlphaFoldDB

51 variants for Q640N1

Variant ID(s) Position Change Description Diseaes Association Provenance
rs258828533 18 T>A No EVA
rs250492101 81 V>A No EVA
rs3389105279 131 K>* No EVA
rs3389105279 131 K>E No EVA
rs3389140680 132 P>T No EVA
rs3401592798 164 G>C No EVA
rs3389140738 180 L>I No EVA
rs3389150891 182 S>L No EVA
rs219910341 185 N>K No EVA
rs236460718 186 P>S No EVA
rs3389116982 188 A>T No EVA
rs216523670 217 P>S No EVA
rs3389147360 235 Q>R No EVA
rs8279653 242 E>A No EVA
rs3389129034 249 R>L No EVA
rs3389136961 251 K>Q No EVA
rs3389150871 290 P>L No EVA
rs3389140927 297 V>L No EVA
rs8279666 317 D>G No EVA
rs3389147347 333 K>Q No EVA
rs3389150857 333 K>R No EVA
rs3401867875 360 K>* No EVA
rs3389136920 361 G>S No EVA
rs3389139670 399 H>R No EVA
rs3389139655 400 G>V No EVA
rs3401958797 513 I>S No EVA
rs3401806242 516 L>P No EVA
rs3389143508 553 F>I No EVA
rs3389140864 577 R>H No EVA
rs3389112201 601 D>E No EVA
rs3389136904 692 D>N No EVA
rs3389150901 730 T>M No EVA
rs3401592865 736 R>Q No EVA
rs3402069528 737 A>D No EVA
rs3389134941 753 L>M No EVA
rs3389139637 762 Y>D No EVA
rs3389147353 783 A>P No EVA
rs3389134857 845 R>S No EVA
rs3389143362 863 S>P No EVA
rs3401173171 925 V>E No EVA
rs3389134868 966 A>V No EVA
rs8279706 975 R>Q No EVA
rs3389112214 998 P>S No EVA
rs248241499 1015 Q>R No EVA
rs3389150865 1021 R>W No EVA
rs218689645 1039 P>L No EVA
rs3389134873 1039 P>T No EVA
rs3389116968 1040 T>I No EVA
rs3389140688 1046 P>S No EVA
rs13471189 1057 P>L No EVA
rs8279707 1115 L>F No EVA

No associated diseases with Q640N1

1 regional properties for Q640N1

Type Name Position InterPro Accession
domain GPCR, rhodopsin-like, 7TM 65 - 316 IPR017452

Functions

Description
EC Number
Subcellular Localization
  • [Isoform 1]: Secreted
  • ;
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

3 GO annotations of cellular component

Name Definition
cytoplasm The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
extracellular space That part of a multicellular organism outside the cells proper, usually taken to be outside the plasma membranes, and occupied by fluid.
nucleus A membrane-bounded organelle of eukaryotic cells in which chromosomes are housed and replicated. In most cells, the nucleus contains all of the cell's chromosomes except the organellar chromosomes, and is the site of RNA synthesis and processing. In some species, or in specialized cell types, RNA metabolism or DNA replication may be absent.

6 GO annotations of molecular function

Name Definition
calmodulin binding Binding to calmodulin, a calcium-binding protein with many roles, both in the calcium-bound and calcium-free states.
carboxypeptidase activity Catalysis of the hydrolysis of a single C-terminal amino acid residue from a polypeptide chain.
collagen binding Binding to collagen, a group of fibrous proteins of very high tensile strength that form the main component of connective tissue in animals. Collagen is highly enriched in glycine (some regions are 33% glycine) and proline, occurring predominantly as 3-hydroxyproline (about 20%).
DNA-binding transcription repressor activity, RNA polymerase II-specific A DNA-binding transcription factor activity that represses or decreases the transcription of specific gene sets transcribed by RNA polymerase II.
RNA polymerase II transcription regulatory region sequence-specific DNA binding Binding to a specific sequence of DNA that is part of a regulatory region that controls the transcription of a gene or cistron by RNA polymerase II.
zinc ion binding Binding to a zinc ion (Zn).

4 GO annotations of biological process

Name Definition
negative regulation of transcription by RNA polymerase II Any process that stops, prevents, or reduces the frequency, rate or extent of transcription mediated by RNA polymerase II.
proteolysis The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their peptide bonds.
regulation of collagen fibril organization Any process that modulates the frequency, rate or extent of collagen fibril organization.
regulation of DNA-templated transcription Any process that modulates the frequency, rate or extent of cellular DNA-templated transcription.

16 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
P04836 CPE Carboxypeptidase E Bos taurus (Bovine) PR
Q2KJ83 CPN1 Carboxypeptidase N catalytic chain Bos taurus (Bovine) PR
Q8QGP3 CPZ Carboxypeptidase Z Gallus gallus (Chicken) PR
O75976 CPD Carboxypeptidase D Homo sapiens (Human) PR
Q8N436 CPXM2 Inactive carboxypeptidase-like protein X2 Homo sapiens (Human) PR
Q66K79 CPZ Carboxypeptidase Z Homo sapiens (Human) PR
Q96SM3 CPXM1 Probable carboxypeptidase X1 Homo sapiens (Human) PR
P14384 CPM Carboxypeptidase M Homo sapiens (Human) PR
Q8IUX7 AEBP1 Adipocyte enhancer-binding protein 1 Homo sapiens (Human) PR
Q80V42 Cpm Carboxypeptidase M Mus musculus (Mouse) PR
Q9D2L5 Cpxm2 Inactive carboxypeptidase-like protein X2 Mus musculus (Mouse) PR
Q9Z100 Cpxm1 Probable carboxypeptidase X1 Mus musculus (Mouse) PR
Q9JJN5 Cpn1 Carboxypeptidase N catalytic chain Mus musculus (Mouse) PR
O89001 Cpd Carboxypeptidase D Mus musculus (Mouse) PR
Q9EQV8 Cpn1 Carboxypeptidase N catalytic chain Rattus norvegicus (Rat) PR
A2RUV9 Aebp1 Adipocyte enhancer-binding protein 1 Rattus norvegicus (Rat) PR
10 20 30 40 50 60
MAPVRTASLL CGLLALLTLC PEGNPQTVLT DDEIEEFLEG FLSELETQSP PREDDVEVQP
70 80 90 100 110 120
LPEPTQRPRK SKAGGKQRAD VEVPPEKNKD KEKKGKKDKG PKATKPLEGS TRPTKKPKEK
130 140 150 160 170 180
PPKATKKPKE KPPKATKKPK EKPPKATKKP KEKPPKATKR PSAGKKFSTV APLETLDRLL
190 200 210 220 230 240
PSPSNPSAQE LPQKRDTPFP NAWQGQGEET QVEAKQPRPE PEEETEMPTL DYNDQIEKED
250 260 270 280 290 300
YEDFEYIRRQ KQPRPTPSRR RLWPERPEEK TEEPEERKEV EPPLKPLLPP DYGDSYVIPN
310 320 330 340 350 360
YDDLDYYFPH PPPQKPDVGQ EVDEEKEEMK KPKKEGSSPK EDTEDKWTVE KNKDHKGPRK
370 380 390 400 410 420
GEELEEEWAP VEKIKCPPIG MESHRIEDNQ IRASSMLRHG LGAQRGRLNM QAGANEDDYY
430 440 450 460 470 480
DGAWCAEDES QTQWIEVDTR RTTRFTGVIT QGRDSSIHDD FVTTFFVGFS NDSQTWVMYT
490 500 510 520 530 540
NGYEEMTFYG NVDKDTPVLS ELPEPVVARF IRIYPLTWNG SLCMRLEVLG CPVTPVYSYY
550 560 570 580 590 600
AQNEVVTTDS LDFRHHSYKD MRQLMKAVNE ECPTITRTYS LGKSSRGLKI YAMEISDNPG
610 620 630 640 650 660
DHELGEPEFR YTAGIHGNEV LGRELLLLLM QYLCQEYRDG NPRVRNLVQD TRIHLVPSLN
670 680 690 700 710 720
PDGYEVAAQM GSEFGNWALG LWTEEGFDIF EDFPDLNSVL WAAEEKKWVP YRVPNNNLPI
730 740 750 760 770 780
PERYLSPDAT VSTEVRAIIS WMEKNPFVLG ANLNGGERLV SYPYDMARTP SQEQLLAEAL
790 800 810 820 830 840
AAARGEDDDG VSEAQETPDH AIFRWLAISF ASAHLTMTEP YRGGCQAQDY TSGMGIVNGA
850 860 870 880 890 900
KWNPRSGTFN DFSYLHTNCL ELSVYLGCDK FPHESELPRE WENNKEALLT FMEQVHRGIK
910 920 930 940 950 960
GVVTDEQGIP IANATISVSG INHGVKTASG GDYWRILNPG EYRVTAHAEG YTSSAKICNV
970 980 990 1000 1010 1020
DYDIGATQCN FILARSNWKR IREILAMNGN RPILRVDPSR PMTPQQRRMQ QRRLQYRLRM
1030 1040 1050 1060 1070 1080
REQMRLRRLN STAGPATSPT PALMPPPSPT PAITLRPWEV LPTTTAGWEE SETETYTEVV
1090 1100 1110 1120
TEFETEYGTD LEVEEIEEEE EEEEEEMDTG LTFPLTTVET YTVNFGDF