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Q9BPZ2 (SPI2B_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 102. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Spindlin-2B
Alternative name(s):
Spindlin-like protein 2B
Short name=SPIN-2
Short name=SPIN-2B
Gene names
Name:SPIN2B
Synonyms:SPIN2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length258 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Involved in the regulation of cell cycle progression, this activity is related to the inhibition of apoptosis following the removal of essential growth factors. Ref.1

Subcellular location

Nucleus Ref.1.

Tissue specificity

Detected in all the examined tissues with highest expression in liver, followed by heart, stomach, kidney, skeletal muscle, placenta, and pancreas.

Miscellaneous

Overexpression in murine myeloid cell line 32Dcl3 causes G2/M arrest.

Sequence similarities

Belongs to the SPIN/STSY family.

Ontologies

Keywords
   Biological processApoptosis
Cell cycle
   Cellular componentNucleus
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processapoptotic process

Inferred from electronic annotation. Source: UniProtKB-KW

cell cycle

Inferred from electronic annotation. Source: UniProtKB-KW

gamete generation

Inferred from electronic annotation. Source: InterPro

   Cellular_componentnucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 258258Spindlin-2B
PRO_0000181369

Sequences

Sequence LengthMass (Da)Tools
Q9BPZ2 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: CAD74289970B4BCD

FASTA25829,158
        10         20         30         40         50         60 
MKTPNAQEAE GQQTRAAAGR ATGSANMTKK KVSQKKQRGR PSSQPRRNIV GCRISHGWKE 

        70         80         90        100        110        120 
GDEPITQWKG TVLDQVPINP SLYLVKYDGI DCVYGLELHR DERVLSLKIL SDRVASSHIS 

       130        140        150        160        170        180 
DANLANTIIG KAVEHMFEGE HGSKDEWRGM VLAQAPIMKA WFYITYEKDP VLYMYQLLDD 

       190        200        210        220        230        240 
YKEGDLRIMP ESSESPPTER EPGGVVDGLI GKHVEYTKED GSKRIGMVIH QVEAKPSVYF 

       250 
IKFDDDFHIY VYDLVKKS 

« Hide

References

« Hide 'large scale' references
[1]"Functional cloning of SPIN-2, a nuclear anti-apoptotic protein with roles in cell cycle progression."
Fletcher B.S., Dragstedt C., Notterpek L., Nolan G.P.
Leukemia 16:1507-1518(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION.
[2]"The DNA sequence of the human X chromosome."
Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C. expand/collapse author list , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Mammary gland and Placenta.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF356353 mRNA. Translation: AAK37566.1.
AL022157 Genomic DNA. Translation: CAI42600.1.
BC000044 mRNA. Translation: AAH00044.1.
BC071974 mRNA. Translation: AAH71974.1.
CCDSCCDS35311.1.
RefSeqNP_001006682.1. NM_001006681.1.
NP_001006683.1. NM_001006682.1.
NP_001006684.1. NM_001006683.1.
XP_005262067.1. XM_005262010.1.
UniGeneHs.460717.
Hs.745094.

3D structure databases

ProteinModelPortalQ9BPZ2.
SMRQ9BPZ2. Positions 46-256.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid138877. 1 interaction.

PTM databases

PhosphoSiteQ9BPZ2.

Polymorphism databases

DMDM23822181.

Proteomic databases

MaxQBQ9BPZ2.
PaxDbQ9BPZ2.
PRIDEQ9BPZ2.

Protocols and materials databases

DNASU474343.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000275988; ENSP00000275988; ENSG00000186787.
ENST00000333933; ENSP00000335008; ENSG00000186787.
ENST00000374912; ENSP00000364047; ENSG00000186787.
GeneID474343.
KEGGhsa:474343.
UCSCuc004duy.3. human.

Organism-specific databases

CTD474343.
GeneCardsGC0XM057163.
HGNCHGNC:33147. SPIN2B.
HPAHPA000162.
MIM300517. gene.
neXtProtNX_Q9BPZ2.
PharmGKBPA162404530.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG40069.
HOGENOMHOG000293367.
HOVERGENHBG000686.
InParanoidQ9BPZ2.
OMAMTKKKAS.
PhylomeDBQ9BPZ2.
TreeFamTF332665.

Gene expression databases

BgeeQ9BPZ2.
CleanExHS_SPIN2B.
GenevestigatorQ9BPZ2.

Family and domain databases

InterProIPR003671. Spin_Ssty.
[Graphical view]
PANTHERPTHR10405. PTHR10405. 1 hit.
PfamPF02513. Spin-Ssty. 3 hits.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi474343.
NextBio111680.
PROQ9BPZ2.
SOURCESearch...

Entry information

Entry nameSPI2B_HUMAN
AccessionPrimary (citable) accession number: Q9BPZ2
Secondary accession number(s): Q7Z2M0
Entry history
Integrated into UniProtKB/Swiss-Prot: October 10, 2002
Last sequence update: June 1, 2001
Last modified: July 9, 2014
This is version 102 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome X

Human chromosome X: entries, gene names and cross-references to MIM