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Conserved domains on  [gi|545687000|ref|NP_001269983|]
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stathmin-4 isoform 3 [Homo sapiens]

Protein Classification

stathmin family protein( domain architecture ID 10467180)

stathmin family protein is a small regulatory phosphoprotein, similar to human stathmin that is involved in the regulation of the microtubule filament system by destabilizing microtubules

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Stathmin pfam00836
Stathmin family; The Stathmin family of proteins play an important role in the regulation of ...
49-183 7.12e-48

Stathmin family; The Stathmin family of proteins play an important role in the regulation of the microtubule cytoskeleton. They regulate microtubule dynamics by promoting depolymerization of microtubules and/or preventing polymerization of tubulin heterodimers.


:

Pssm-ID: 425897 [Multi-domain]  Cd Length: 135  Bit Score: 152.48  E-value: 7.12e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545687000   49 DMEVIELNKCTSGQSFEVILKPPSFDGVPEFNASlPRRRDPSLEEIQKKLEAAEERRKYQEAELLKHLAEKREHEREVIQ 128
Cdd:pfam00836   2 DTEVKELEKRASGQAFEVILKPPSANAPPKLSPT-PKKKDSSLEEIQKKLEAAEERRKSLEAQKLKQLAEKREKEEEALQ 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 545687000  129 KAIEENNNFIKMAKEKLAQKMESNKENREAHLAAMLERLQEKDKHAEEVRKNKEL 183
Cdd:pfam00836  81 KALEENNNFSKMAEEKLKQKMEAYKENREAQIAALKEKLKEHEKHVEEVRKNKEQ 135
 
Name Accession Description Interval E-value
Stathmin pfam00836
Stathmin family; The Stathmin family of proteins play an important role in the regulation of ...
49-183 7.12e-48

Stathmin family; The Stathmin family of proteins play an important role in the regulation of the microtubule cytoskeleton. They regulate microtubule dynamics by promoting depolymerization of microtubules and/or preventing polymerization of tubulin heterodimers.


Pssm-ID: 425897 [Multi-domain]  Cd Length: 135  Bit Score: 152.48  E-value: 7.12e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545687000   49 DMEVIELNKCTSGQSFEVILKPPSFDGVPEFNASlPRRRDPSLEEIQKKLEAAEERRKYQEAELLKHLAEKREHEREVIQ 128
Cdd:pfam00836   2 DTEVKELEKRASGQAFEVILKPPSANAPPKLSPT-PKKKDSSLEEIQKKLEAAEERRKSLEAQKLKQLAEKREKEEEALQ 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 545687000  129 KAIEENNNFIKMAKEKLAQKMESNKENREAHLAAMLERLQEKDKHAEEVRKNKEL 183
Cdd:pfam00836  81 KALEENNNFSKMAEEKLKQKMEAYKENREAQIAALKEKLKEHEKHVEEVRKNKEQ 135
PTZ00121 PTZ00121
MAEBL; Provisional
92-185 2.92e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 37.81  E-value: 2.92e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545687000   92 EEIQKKLEAAEERRKYQEAELLKHLAEKREHEREVIQKAIEENNNFIKMAKEKLAQKMESNKENREAHLAAMLERLQEKD 171
Cdd:PTZ00121 1467 EEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKK 1546
                          90
                  ....*....|....
gi 545687000  172 KhAEEVRKNKELKE 185
Cdd:PTZ00121 1547 K-ADELKKAEELKK 1559
 
Name Accession Description Interval E-value
Stathmin pfam00836
Stathmin family; The Stathmin family of proteins play an important role in the regulation of ...
49-183 7.12e-48

Stathmin family; The Stathmin family of proteins play an important role in the regulation of the microtubule cytoskeleton. They regulate microtubule dynamics by promoting depolymerization of microtubules and/or preventing polymerization of tubulin heterodimers.


Pssm-ID: 425897 [Multi-domain]  Cd Length: 135  Bit Score: 152.48  E-value: 7.12e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545687000   49 DMEVIELNKCTSGQSFEVILKPPSFDGVPEFNASlPRRRDPSLEEIQKKLEAAEERRKYQEAELLKHLAEKREHEREVIQ 128
Cdd:pfam00836   2 DTEVKELEKRASGQAFEVILKPPSANAPPKLSPT-PKKKDSSLEEIQKKLEAAEERRKSLEAQKLKQLAEKREKEEEALQ 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 545687000  129 KAIEENNNFIKMAKEKLAQKMESNKENREAHLAAMLERLQEKDKHAEEVRKNKEL 183
Cdd:pfam00836  81 KALEENNNFSKMAEEKLKQKMEAYKENREAQIAALKEKLKEHEKHVEEVRKNKEQ 135
PTZ00121 PTZ00121
MAEBL; Provisional
92-185 2.92e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 37.81  E-value: 2.92e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545687000   92 EEIQKKLEAAEERRKYQEAELLKHLAEKREHEREVIQKAIEENNNFIKMAKEKLAQKMESNKENREAHLAAMLERLQEKD 171
Cdd:PTZ00121 1467 EEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKK 1546
                          90
                  ....*....|....
gi 545687000  172 KhAEEVRKNKELKE 185
Cdd:PTZ00121 1547 K-ADELKKAEELKK 1559
PRK12704 PRK12704
phosphodiesterase; Provisional
91-186 3.79e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 37.07  E-value: 3.79e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545687000  91 LEEIQKKLEAAEERRKYQEAELLKHLaeKREHEREVIQK--AIEENNNFIKMAKEKLAQKMESNkENREAHLAAMLERLQ 168
Cdd:PRK12704  44 LEEAKKEAEAIKKEALLEAKEEIHKL--RNEFEKELRERrnELQKLEKRLLQKEENLDRKLELL-EKREEELEKKEKELE 120
                         90
                 ....*....|....*...
gi 545687000 169 EKDKHAEEVRKNKELKEE 186
Cdd:PRK12704 121 QKQQELEKKEEELEELIE 138
PTZ00121 PTZ00121
MAEBL; Provisional
92-187 4.06e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 37.43  E-value: 4.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545687000   92 EEIQKKLEAAEERRKYQEAELLKHLAEKREHEREVIQKAIEENNNFIKMAKEKLAQKMESNKENREAHLAAMLERLQEK- 170
Cdd:PTZ00121 1299 EEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKk 1378
                          90       100
                  ....*....|....*....|..
gi 545687000  171 -----DKHAEEVRKNKELKEEA 187
Cdd:PTZ00121 1379 kadaaKKKAEEKKKADEAKKKA 1400
Nup88 pfam10168
Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal ...
86-184 8.36e-03

Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal two-thirds of the protein has no obvious structural motifs but is the region for binding to Nup98, one of the components of the nuclear pore. the C-terminal end is a predicted coiled-coil domain. Nup88 is overexpressed in tumor cells.


Pssm-ID: 431106  Cd Length: 713  Bit Score: 36.18  E-value: 8.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545687000   86 RRDPSLEEIQKKLEAAEERRKYQEAELlKHLAEKREHEREviqkaieennnfikMAkEKLAQKMESNKENREA---HLAA 162
Cdd:pfam10168 551 KHDLAREEIQKRVKLLKLQKEQQLQEL-QSLEEERKSLSE--------------RA-EKLAEKYEEIKDKQEKlmrRCKK 614
                          90       100       110
                  ....*....|....*....|....*....|.
gi 545687000  163 MLERLQEKD--------KHAEEVRK-NKELK 184
Cdd:pfam10168 615 VLQRLNSQLpvlsdaerEMKKELETiNEQLK 645
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.20
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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