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Conserved domains on  [gi|224451142|ref|NP_001138926|]
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stathmin isoform b [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 ...
 5-126 1.42e-50

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: 459956 [Multi-domain]  Cd Length: 136  Bit Score: 159.05  E-value: 1.42e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224451142    5 DIQVKELEKRASGQAFELILSPRSKESVPEFPLSPPKKKDLSLEEIQKKLEAAEERRKSHEAEVLKQLAEKREHEKEVLQ 84
Cdd:pfam00836   2 DTEVKELEKRASGQAFEVILKPPSVNAAPPKLSLSPKKKDSSLEEIQKKLEAAEERRKSLEAQKLKQLAEKREKEEEALQ 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 224451142   85 KAIEENNNFSKMAEEKLTHKMEANKENREAQMAAKLERLREK 126
Cdd:pfam00836  82 KADEENNNFSKMAEEKLKQKMEAYKENREAQIAALKEKLKEK 123
 
Name Accession Description Interval E-value
Stathmin pfam00836
Stathmin family; The Stathmin family of proteins play an important role in the regulation of ...
 5-126 1.42e-50

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: 459956 [Multi-domain]  Cd Length: 136  Bit Score: 159.05  E-value: 1.42e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224451142    5 DIQVKELEKRASGQAFELILSPRSKESVPEFPLSPPKKKDLSLEEIQKKLEAAEERRKSHEAEVLKQLAEKREHEKEVLQ 84
Cdd:pfam00836   2 DTEVKELEKRASGQAFEVILKPPSVNAAPPKLSLSPKKKDSSLEEIQKKLEAAEERRKSLEAQKLKQLAEKREKEEEALQ 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 224451142   85 KAIEENNNFSKMAEEKLTHKMEANKENREAQMAAKLERLREK 126
Cdd:pfam00836  82 KADEENNNFSKMAEEKLKQKMEAYKENREAQIAALKEKLKEK 123
PRK12704 PRK12704
phosphodiesterase; Provisional
 50-127 3.09e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 37.07  E-value: 3.09e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224451142  50 IQKKLEAAEERRKS------HEAEVLKQLAE----------KREHEKEVLQK--AIEENNNFSKMAEEKLTHKMEANkEN 111
Cdd:PRK12704  29 AEAKIKEAEEEAKRileeakKEAEAIKKEALleakeeihklRNEFEKELRERrnELQKLEKRLLQKEENLDRKLELL-EK 107

                         90
                 ....*....|....*.
gi 224451142 112 REAQMAAKLERLREKM 127
Cdd:PRK12704 108 REEELEKKEKELEQKQ 123
 
Name Accession Description Interval E-value
Stathmin pfam00836
Stathmin family; The Stathmin family of proteins play an important role in the regulation of ...
 5-126 1.42e-50

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: 459956 [Multi-domain]  Cd Length: 136  Bit Score: 159.05  E-value: 1.42e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224451142    5 DIQVKELEKRASGQAFELILSPRSKESVPEFPLSPPKKKDLSLEEIQKKLEAAEERRKSHEAEVLKQLAEKREHEKEVLQ 84
Cdd:pfam00836   2 DTEVKELEKRASGQAFEVILKPPSVNAAPPKLSLSPKKKDSSLEEIQKKLEAAEERRKSLEAQKLKQLAEKREKEEEALQ 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 224451142   85 KAIEENNNFSKMAEEKLTHKMEANKENREAQMAAKLERLREK 126
Cdd:pfam00836  82 KADEENNNFSKMAEEKLKQKMEAYKENREAQIAALKEKLKEK 123
Nup88 pfam10168
Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal ...
 41-127 2.69e-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 tumour cells.


Pssm-ID: 462975 [Multi-domain]  Cd Length: 713  Bit Score: 37.33  E-value: 2.69e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224451142   41 KKKDLSLEEIQKKLeaaeerrksheaevlKQLAEKREHEKEVLQKAIEENNNFSKMAeEKLTHKMEANKENREA---QMA 117
Cdd:pfam10168 550 KKHDLAREEIQKRV---------------KLLKLQKEQQLQELQSLEEERKSLSERA-EKLAEKYEEIKDKQEKlmrRCK 613

                          90
                  ....*....|
gi 224451142  118 AKLERLREKM 127
Cdd:pfam10168 614 KVLQRLNSQL 623
PRK12704 PRK12704
phosphodiesterase; Provisional
 50-127 3.09e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 37.07  E-value: 3.09e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224451142  50 IQKKLEAAEERRKS------HEAEVLKQLAE----------KREHEKEVLQK--AIEENNNFSKMAEEKLTHKMEANkEN 111
Cdd:PRK12704  29 AEAKIKEAEEEAKRileeakKEAEAIKKEALleakeeihklRNEFEKELRERrnELQKLEKRLLQKEENLDRKLELL-EK 107

                         90
                 ....*....|....*.
gi 224451142 112 REAQMAAKLERLREKM 127
Cdd:PRK12704 108 REEELEKKEKELEQKQ 123
 
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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