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Conserved domains on  [gi|2462535635|ref|XP_054229808|]
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ras association domain-containing protein 9 isoform X1 [Homo sapiens]

Protein Classification

ubiquitin family protein( domain architecture ID 13006439)

ubiquitin family protein belongs to an diverse class of protein modifier and gene expression regulatory proteins that participate in a number of cellular processes

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
RA_RASSF9 cd16133
Ras-associating (RA) domain of N-terminal Ras-association domain family 9 (RASSF9); RASSF9, ...
 7-99 2.94e-61

Ras-associating (RA) domain of N-terminal Ras-association domain family 9 (RASSF9); RASSF9, also termed PAM COOH-terminal interactor protein 1 (P-CIP1), or peptidylglycine alpha-amidating monooxygenase COOH-terminal interactor, is a member of N-terminus RASSF7-10 protein family. RASSF7-10 has an RA domain at the N-terminus and lacks a conserved SARAH (Salvador/RASSF/Hpo) motif adjacent to the RA domain that is found in members of the RASSF1-6 family. The RA domain of the N-terminal RASSF proteins family has the beta-grasp ubiquitin-like fold with low sequence similarity to ubiquitin. RASSF9 was formerly known as PAM COOH-terminal interactor-1 (P-CIP1) because of its interaction with peptidylglycine alpha-amidating mono-oxygenase (PAM) and possibility of its role in regulating the trafficking of integral membrane PAM. RASSF9 is widely expressed in multiple organs such as testis, kidney, skeletal muscle, liver, lung, brain, and heart. Cloned RASSF9 showed preferential binding to N-Ras and K-Ras.


:

Pssm-ID: 340550  Cd Length: 93  Bit Score: 193.14  E-value: 2.94e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535635   7 EIVVWVCQEEKLVCGLTKRTTSADVIQALLEEHEATFGEKRFLLGKPSDYCIIEKWRGSERVLPPLTRILKLWKAWGDEQ 86
Cdd:cd16133     1 EIVVWVCQEEKVVCGLTKHTTCADVIQALLEEHEATFGEKRFLLGQPSDYCIVEKWRGFERVLPPLTKILRLWKAWGDEQ 80

                          90
                  ....*....|...
gi 2462535635  87 PNMQFVLVKADAF 99
Cdd:cd16133    81 PNLQFVLVKADAF 93
 
Name Accession Description Interval E-value
RA_RASSF9 cd16133
Ras-associating (RA) domain of N-terminal Ras-association domain family 9 (RASSF9); RASSF9, ...
 7-99 2.94e-61

Ras-associating (RA) domain of N-terminal Ras-association domain family 9 (RASSF9); RASSF9, also termed PAM COOH-terminal interactor protein 1 (P-CIP1), or peptidylglycine alpha-amidating monooxygenase COOH-terminal interactor, is a member of N-terminus RASSF7-10 protein family. RASSF7-10 has an RA domain at the N-terminus and lacks a conserved SARAH (Salvador/RASSF/Hpo) motif adjacent to the RA domain that is found in members of the RASSF1-6 family. The RA domain of the N-terminal RASSF proteins family has the beta-grasp ubiquitin-like fold with low sequence similarity to ubiquitin. RASSF9 was formerly known as PAM COOH-terminal interactor-1 (P-CIP1) because of its interaction with peptidylglycine alpha-amidating mono-oxygenase (PAM) and possibility of its role in regulating the trafficking of integral membrane PAM. RASSF9 is widely expressed in multiple organs such as testis, kidney, skeletal muscle, liver, lung, brain, and heart. Cloned RASSF9 showed preferential binding to N-Ras and K-Ras.


Pssm-ID: 340550  Cd Length: 93  Bit Score: 193.14  E-value: 2.94e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535635   7 EIVVWVCQEEKLVCGLTKRTTSADVIQALLEEHEATFGEKRFLLGKPSDYCIIEKWRGSERVLPPLTRILKLWKAWGDEQ 86
Cdd:cd16133     1 EIVVWVCQEEKVVCGLTKHTTCADVIQALLEEHEATFGEKRFLLGQPSDYCIVEKWRGFERVLPPLTKILRLWKAWGDEQ 80

                          90
                  ....*....|...
gi 2462535635  87 PNMQFVLVKADAF 99
Cdd:cd16133    81 PNLQFVLVKADAF 93
RA smart00314
Ras association (RalGDS/AF-6) domain; RasGTP effectors (in cases of AF6, canoe and RalGDS); ...
 2-97 6.69e-15

Ras association (RalGDS/AF-6) domain; RasGTP effectors (in cases of AF6, canoe and RalGDS); putative RasGTP effectors in other cases. Kalhammer et al. have shown that not all RA domains bind RasGTP. Predicted structure similar to that determined, and that of the RasGTP-binding domain of Raf kinase. Predicted RA domains in PLC210 and nore1 found to bind RasGTP. Included outliers (Grb7, Grb14, adenylyl cyclases etc.)


Pssm-ID: 214612  Cd Length: 90  Bit Score: 69.63  E-value: 6.69e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535635    2 DSEEKEIVV-WVCQEEKLVCGLTKRTTSADVIQALLEEHEATfgekrfllGKPSDYCIIEKW-RGSERVLPPLTRILKLW 79
Cdd:smart00314   1 DTFVLRVYVdDLPGGTYKTLRVSSRTTARDVIQQLLEKFHLT--------DDPEEYVLVEVLpDGKERVLPDDENPLQLQ 72

                           90
                   ....*....|....*...
gi 2462535635   80 KAWGDEQPNMQFVLVKAD 97
Cdd:smart00314  73 KLWPRRGPNLRFVLRKRD 90
 
Name Accession Description Interval E-value
RA_RASSF9 cd16133
Ras-associating (RA) domain of N-terminal Ras-association domain family 9 (RASSF9); RASSF9, ...
 7-99 2.94e-61

Ras-associating (RA) domain of N-terminal Ras-association domain family 9 (RASSF9); RASSF9, also termed PAM COOH-terminal interactor protein 1 (P-CIP1), or peptidylglycine alpha-amidating monooxygenase COOH-terminal interactor, is a member of N-terminus RASSF7-10 protein family. RASSF7-10 has an RA domain at the N-terminus and lacks a conserved SARAH (Salvador/RASSF/Hpo) motif adjacent to the RA domain that is found in members of the RASSF1-6 family. The RA domain of the N-terminal RASSF proteins family has the beta-grasp ubiquitin-like fold with low sequence similarity to ubiquitin. RASSF9 was formerly known as PAM COOH-terminal interactor-1 (P-CIP1) because of its interaction with peptidylglycine alpha-amidating mono-oxygenase (PAM) and possibility of its role in regulating the trafficking of integral membrane PAM. RASSF9 is widely expressed in multiple organs such as testis, kidney, skeletal muscle, liver, lung, brain, and heart. Cloned RASSF9 showed preferential binding to N-Ras and K-Ras.


Pssm-ID: 340550  Cd Length: 93  Bit Score: 193.14  E-value: 2.94e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535635   7 EIVVWVCQEEKLVCGLTKRTTSADVIQALLEEHEATFGEKRFLLGKPSDYCIIEKWRGSERVLPPLTRILKLWKAWGDEQ 86
Cdd:cd16133     1 EIVVWVCQEEKVVCGLTKHTTCADVIQALLEEHEATFGEKRFLLGQPSDYCIVEKWRGFERVLPPLTKILRLWKAWGDEQ 80

                          90
                  ....*....|...
gi 2462535635  87 PNMQFVLVKADAF 99
Cdd:cd16133    81 PNLQFVLVKADAF 93
RA_RASSF7_like cd16123
Ras-associating (RA) domain found in Ras-association domain family members, RASSF7, RASSF8, ...
 7-95 5.06e-37

Ras-associating (RA) domain found in Ras-association domain family members, RASSF7, RASSF8, RASSF9, and RASSF10; The RASSF family of proteins shares a conserved RalGDS/AF6 Ras association (RA) domain either in the C-terminus (RASSF1-6) or N-terminus (RASSF7-10). RASSF7-10 lacks a conserved SARAH (Salvador/RASSF/Hpo) motif adjacent to the RA domain that is found in members of the RASSF1-6 family. The structural differences between the C-terminus and N-terminus RASSF subgroups have led to the suggestion that they are two distinct families. RA domain has the beta-grasp ubiquitin-like (Ubl) fold with low sequence similarity to ubiquitin (Ub). Ras proteins are small GTPases that are involved in cellular signal transduction. The N-terminus RASSF proteins are potential Ras effectors that have been linked to key biological processes, including cell death, proliferation, microtubule stability, promoter methylation, vesicle trafficking and response to hypoxia.


Pssm-ID: 340540  Cd Length: 81  Bit Score: 129.67  E-value: 5.06e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535635   7 EIVVWVCQEEKLVCGLTKRTTSADVIQALLEEHEatfgekrfLLGKPSDYCIIEKWRGSERVLPPLTRILKLWKAWGDEQ 86
Cdd:cd16123     1 ELKVWVDGEERVVSGVTERTTCQDVIYALAQATG--------QTNDTGRYVLVERWRGIERPLPPRTRILKVWKAWGEEQ 72


                  ....*....
gi 2462535635  87 PNMQFVLVK 95
Cdd:cd16123    73 SNVQFVLRR 81
RA_RASSF10 cd16132
Ras-associating (RA) domain found in N-terminal Ras-association domain family 10 (RASSF10); ...
 7-98 4.45e-36

Ras-associating (RA) domain found in N-terminal Ras-association domain family 10 (RASSF10); RASSF10 is a member of a family of N-terminus RASSF7-10 proteins. RASSF7-10 has an RA domain at the N-terminus and lacks a conserved SARAH (Salvador/RASSF/Hpo) motif adjacent to the RA domain that is found in members of the RASSF1-6 family. RA domain of N-terminal RASSF protein family has the beta-grasp ubiquitin-like fold with low sequence similarity to ubiquitin. RASSF10 is expressed in a wide variety of tissues and its expression in human thyroid, pancreas, placenta, heart, lung and kidney has been observed. RASSF10 is the most frequently methylated of the N-terminal RASSFs in some cancers such as in childhood acute lymphoblastic leukemia and both, thyroid cancer cell lines and primary thyroid carcinomas.


Pssm-ID: 340549  Cd Length: 102  Bit Score: 127.71  E-value: 4.45e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535635   7 EIVVWVCQEEKLVCGLTKRTTSADVIQALLEEHEATFGEKR---------FLLGKPSDYCIIEKWRGSERVLPPLTRILK 77
Cdd:cd16132     1 KISVWLCQEEKLVSGLSRRTTCADVVRVLLEDQNRSQQEEEeeegerdggMLSGPPQSYCIVEKWRGFERILPNKTKILR 80

                          90       100
                  ....*....|....*....|.
gi 2462535635  78 LWKAWGDEQPNMQFVLVKADA 98
Cdd:cd16132    81 LWAAWGEEQENVRFVLVRSEA 101
RA smart00314
Ras association (RalGDS/AF-6) domain; RasGTP effectors (in cases of AF6, canoe and RalGDS); ...
 2-97 6.69e-15

Ras association (RalGDS/AF-6) domain; RasGTP effectors (in cases of AF6, canoe and RalGDS); putative RasGTP effectors in other cases. Kalhammer et al. have shown that not all RA domains bind RasGTP. Predicted structure similar to that determined, and that of the RasGTP-binding domain of Raf kinase. Predicted RA domains in PLC210 and nore1 found to bind RasGTP. Included outliers (Grb7, Grb14, adenylyl cyclases etc.)


Pssm-ID: 214612  Cd Length: 90  Bit Score: 69.63  E-value: 6.69e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535635    2 DSEEKEIVV-WVCQEEKLVCGLTKRTTSADVIQALLEEHEATfgekrfllGKPSDYCIIEKW-RGSERVLPPLTRILKLW 79
Cdd:smart00314   1 DTFVLRVYVdDLPGGTYKTLRVSSRTTARDVIQQLLEKFHLT--------DDPEEYVLVEVLpDGKERVLPDDENPLQLQ 72

                           90
                   ....*....|....*...
gi 2462535635   80 KAWGDEQPNMQFVLVKAD 97
Cdd:smart00314  73 KLWPRRGPNLRFVLRKRD 90
RA_RASSF8 cd16134
Ras-associating (RA) domain found in N-terminal Ras-association domain family 8 (RASSF8); ...
 7-93 6.84e-13

Ras-associating (RA) domain found in N-terminal Ras-association domain family 8 (RASSF8); RASSF8, also termed carcinoma-associated protein HOJ-1, is a member of the N-terminus RASSF7-10 protein family. RASSF7-10 has an RA-domain at the N-terminus and lacks a conserved SARAH (Salvador/RASSF/Hpo) motif adjacent to the RA domain that is found in members of the RASSF1-6 family. The RA domain of N-terminal RASSF proteins family has the beta-grasp ubiquitin-like fold with low sequence similarity to ubiquitin. RASSF8 has been described as a potential tumor suppressor. RASSF8 might have a role in the regulation of cell-cell adhesion and cell growth.


Pssm-ID: 340551  Cd Length: 82  Bit Score: 63.61  E-value: 6.84e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535635   7 EIVVWVCQEEKLVCGLTKRTTSADVIQALLEeheATfgekrfllGKPSDYCIIEKWRGSERVLPPLTRILKLWKAWGDEQ 86
Cdd:cd16134     1 ELKVWVDGIQRVVCGVTEVTTCQEVVIALAQ---AT--------GRTGRFTLIEKWRNTERLLAPHENPLKVLNKWGQYA 69


                  ....*..
gi 2462535635  87 PNMQFVL 93
Cdd:cd16134    70 SDVQFIL 76
RA_RASSF7 cd16135
Ras-associating (RA) domain found in N-terminal Ras-association domain family 7 (RASSF7); ...
 7-93 2.38e-07

Ras-associating (RA) domain found in N-terminal Ras-association domain family 7 (RASSF7); RASSF7, also termed HRAS1-related cluster protein 1, is a member of the N-terminus RASSF7-10 protein family. RASSF7-10 has an RA-domain at the N-terminus and lacks a conserved SARAH (Salvador/RASSF/Hpo) motif adjacent to the RA domain that is found in members of the RASSF1-6 family. The RA domain of N-terminal RASSF protein family has the beta-grasp ubiquitin-like fold with low sequence similarity to ubiquitin. RASSF7 is a potential Ras effector as its function has been linked to some key biological processes including the regulation of cell death and proliferation; for example, RASSF7 is up-regulated in pancreatic cancer.


Pssm-ID: 340552  Cd Length: 83  Bit Score: 48.02  E-value: 2.38e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535635   7 EIVVWVCQEEKLVCGLTKRTTSADVIQALLEEheatfgekrflLGKPSDYCIIEKWRGSERVLPPLTRILKLWKAWGDEQ 86
Cdd:cd16135     2 ELKVWVDGIQRVVCGVSEQTTCQEVVIALAQA-----------IGQTGRYVLIQKLRDKERQLLANECPLEALAKCGQYA 70


                  ....*..
gi 2462535635  87 PNMQFVL 93
Cdd:cd16135    71 NDVQFIL 77
RA cd17043
Ras-associating (RA) domain, structurally similar to a beta-grasp ubiquitin-like fold; RA ...
 23-93 8.58e-06

Ras-associating (RA) domain, structurally similar to a beta-grasp ubiquitin-like fold; RA domain-containing proteins function by interacting with Ras proteins directly or indirectly and are involved in various functions ranging from tumor suppression to being oncoproteins. Ras proteins are small GTPases that are involved in cellular signal transduction. The RA domain has the beta-grasp ubiquitin-like (Ubl) fold with low sequence similarity to ubiquitin (Ub); Ub is a protein modifier in eukaryotes that is involved in various cellular processes, including transcriptional regulation, cell cycle control, and DNA repair. RA-containing proteins include RalGDS, AF6, RIN, RASSF1, SNX27, CYR1, STE50, and phospholipase C epsilon.


Pssm-ID: 340563  Cd Length: 87  Bit Score: 43.85  E-value: 8.58e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462535635  23 TKRTTSADVIQALLEEHeatfgekrFLLGKPSDYCIIEKW--RGSERVLPPLTRILKLWKAWGDEQPNMQFVL 93
Cdd:cd17043    21 SSTTTAREVVQLLLEKY--------GLEEDPEDYSLYEVSekQETERVLHDDECPLLIQLEWGPQGTEFRFVL 85
RA_ASPP1_2 cd16125
Ras-associating (RA) domain found in apoptosis-stimulating protein of p53 (ASPP) 1 and 2; The ...
 22-93 1.32e-04

Ras-associating (RA) domain found in apoptosis-stimulating protein of p53 (ASPP) 1 and 2; The ASPP protein (apoptosis-stimulating protein of p53; also called ankyrin repeat-, Src homology 3 domain- and Pro-rich region-containing protein) plays a critical role in regulating apoptosis. The ASPP family consists of three members, ASPP1, ASPP2 and iASPP, all of which bind to p53 and regulate p53-mediated apoptosis. ASPP1 and ASPP2, have a RA domain at their N-terminus and have pro-apoptotic functions, while iASPP is involved in anti-apoptotic responses. RA domain-containing proteins function by interacting with Ras proteins directly or indirectly and are involved in several different functions ranging from tumor suppression to being oncoproteins. Ras proteins are small GTPases that are involved in cellular signal transduction. The RA domain has the beta-grasp ubiquitin-like fold with low sequence similarity to ubiquitin.


Pssm-ID: 340542  Cd Length: 80  Bit Score: 40.36  E-value: 1.32e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462535635  22 LTKRTTSADVIQALLEEHEatfgekrfllgkpSDYCIIEKWRGSERVLPPLTRILKLWKAWGDEQPNMQFVL 93
Cdd:cd16125    19 ITPETTCQDVVDCCKEPGE-------------ENCHLVEVWRGCERPLPEEENPYEILQQWGSHRDEVKFFL 77
RA_ASPP2 cd17225
Ras-associating (RA) domain found in apoptosis-stimulating protein of p53 protein 2 (ASPP2); ...
 22-93 5.92e-03

Ras-associating (RA) domain found in apoptosis-stimulating protein of p53 protein 2 (ASPP2); ASPP2, also termed Bcl2-binding protein (Bbp), or renal carcinoma antigen NY-REN-51, or tumor suppressor p53-binding protein 2 (53BP2), or p53-binding protein 2 (p53BP2), is a member of ASPP protein family and it functions as a tumor suppressor. ASPP2 binds to p53 and enhances p53-mediated transcription of proapoptotic genes. ASSP2 contains a RA domain at the N-terminus. The RA domain is a ubiquitin-like domain and RA domain-containing proteins are involved in several different functions ranging from tumor suppression to being oncoproteins. All p53 amino acids that are important for ASPP2 binding are mutated in human cancer, and ASPP2 is frequently downregulated in these tumor cells.


Pssm-ID: 340745  Cd Length: 80  Bit Score: 35.55  E-value: 5.92e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462535635  22 LTKRTTSADVIQALLEEHEatfgekrfllgkpSDYCIIEKWRGSERVLPPLTRILKLWKAWGDEQPNMQFVL 93
Cdd:cd17225    19 ITPETTCRDVVELCKEPGE-------------TDCHLAEVWRGSERPVADNERMLDVLQQWGAQRNEVRFFL 77
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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