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Q8BGG7

- UBS3B_MOUSE

UniProt

Q8BGG7 - UBS3B_MOUSE

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Protein

Ubiquitin-associated and SH3 domain-containing protein B

Gene

Ubash3b

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Interferes with CBL-mediated down-regulation and degradation of receptor-type tyrosine kinases. Promotes accumulation of activated target receptors, such as T-cell receptors and EGFR, on the cell surface. Exhibits tyrosine phosphatase activity toward several substrates including EGFR, FAK, SYK, and ZAP70. Down-regulates proteins that are dually modified by both protein tyrosine phosphorylation and ubiquitination.4 Publications

Catalytic activityi

Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei379 – 3791
Active sitei380 – 3801Tele-phosphohistidine intermediate
Active sitei565 – 5651

GO - Molecular functioni

  1. protein tyrosine phosphatase activity Source: UniProtKB-EC

GO - Biological processi

  1. negative regulation of platelet aggregation Source: MGI
  2. negative regulation of protein kinase activity Source: MGI
  3. peptidyl-tyrosine dephosphorylation Source: MGI
  4. regulation of release of sequestered calcium ion into cytosol Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protein phosphatase

Names & Taxonomyi

Protein namesi
Recommended name:
Ubiquitin-associated and SH3 domain-containing protein B (EC:3.1.3.48)
Alternative name(s):
Cbl-interacting protein p70
Suppressor of T-cell receptor signaling 1
Short name:
STS-1
T-cell ubiquitin ligand 2
Short name:
TULA-2
Tyrosine-protein phosphatase STS1/TULA2
Gene namesi
Name:Ubash3b
Synonyms:Sts1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 9

Organism-specific databases

MGIiMGI:1920078. Ubash3b.

Subcellular locationi

Cytoplasm By similarity. Nucleus Curated

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-KW
  2. nucleus Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Disruption phenotypei

Mice display strikingly elevated levels of tyrosine phosphorylated, ubiquitinated proteins following TCR stimulation. They are prothrombotic and have shorter bleeding times, which is attributed to insufficient SYK dephosphorylation in platelets.2 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 638638Ubiquitin-associated and SH3 domain-containing protein BPRO_0000245509Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei9 – 91PhosphoserineBy similarity
Modified residuei12 – 121PhosphothreonineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ8BGG7.
PaxDbiQ8BGG7.
PRIDEiQ8BGG7.

PTM databases

PhosphoSiteiQ8BGG7.

Expressioni

Tissue specificityi

Detected in splenic T-cells and B-cells, total spleen, skeletal muscle, heart, lung, kidney, thymus, brain and liver (at protein level). Highly expressed in brain. Detected in heart, spleen, lung, liver, kidney and testis.2 Publications

Gene expression databases

BgeeiQ8BGG7.
CleanExiMM_UBASH3B.
ExpressionAtlasiQ8BGG7. baseline and differential.
GenevestigatoriQ8BGG7.

Interactioni

Subunit structurei

Homodimer. Interacts with JAK2 (in vitro). Interacts with CBL. Part of a complex containing CBL and activated EGFR. Interacts with ubiquitin and with mono-ubiquitinated proteins (By similarity).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
ZAP70P4340310EBI-8846415,EBI-1211276From a different organism.

Protein-protein interaction databases

IntActiQ8BGG7. 1 interaction.
STRINGi10090.ENSMUSP00000043865.

Structurei

Secondary structure

1
638
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi374 – 3796
Helixi384 – 3885
Helixi392 – 3954
Helixi421 – 4244
Helixi432 – 44716
Beta strandi454 – 4574
Helixi461 – 47313
Turni477 – 4793
Beta strandi482 – 4843
Helixi486 – 4883
Helixi492 – 4943
Beta strandi495 – 4995
Helixi506 – 5116
Helixi526 – 5283
Helixi535 – 55319
Turni554 – 5563
Beta strandi558 – 5647
Helixi568 – 5714
Turni572 – 5743
Helixi575 – 5773
Helixi584 – 5918
Beta strandi599 – 6046
Beta strandi606 – 6083
Beta strandi611 – 6144
Helixi631 – 6355

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2H0QX-ray1.82A/B/C373-633[»]
2IKQX-ray2.61A/B/M369-638[»]
3MBKX-ray1.35A/B373-636[»]
ProteinModelPortaliQ8BGG7.
SMRiQ8BGG7. Positions 15-67, 238-317, 373-636.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ8BGG7.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini23 – 6543UBAPROSITE-ProRule annotationAdd
BLAST
Domaini243 – 30866SH3PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni369 – 638270Protein tyrosine phosphataseAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi325 – 3284Poly-Ser

Sequence similaritiesi

Contains 1 SH3 domain.PROSITE-ProRule annotation
Contains 1 UBA domain.PROSITE-ProRule annotation

Keywords - Domaini

SH3 domain

Phylogenomic databases

eggNOGiNOG276661.
GeneTreeiENSGT00390000018249.
HOGENOMiHOG000012936.
HOVERGENiHBG018025.
InParanoidiQ8BGG7.
OMAiADECGTW.
OrthoDBiEOG7P5T0D.
PhylomeDBiQ8BGG7.
TreeFamiTF313334.

Family and domain databases

Gene3Di3.40.50.1240. 1 hit.
InterProiIPR013078. His_Pase_superF_clade-1.
IPR029033. His_PPase_superfam.
IPR001452. SH3_domain.
IPR009060. UBA-like.
IPR015940. UBA/transl_elong_EF1B_N_euk.
IPR000449. UBA/Ts_N.
[Graphical view]
PfamiPF00300. His_Phos_1. 1 hit.
PF14604. SH3_9. 1 hit.
PF00627. UBA. 1 hit.
[Graphical view]
SMARTiSM00326. SH3. 1 hit.
SM00165. UBA. 1 hit.
[Graphical view]
SUPFAMiSSF46934. SSF46934. 1 hit.
SSF50044. SSF50044. 1 hit.
SSF53254. SSF53254. 2 hits.
PROSITEiPS50002. SH3. 1 hit.
PS50030. UBA. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q8BGG7-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MAAREELYSK VTPRRDRLQR PGTVKHGSAL DVLLSMGFPR ARAQKALAST
60 70 80 90 100
GGRSVQAACD WLFSHVGDPF LDDPLPREYV LYLRPTGPLA QKLSDFWQQS
110 120 130 140 150
KQICGKNKAH NIFPHITLCQ FFMCEDSKVD ALGEALQTTV SRWKCKFSAP
160 170 180 190 200
LPLELYTSSN FIGLFVKEDS AEVLKKFAAD FAAEAASKTE VHVEPHKKQL
210 220 230 240 250
HVTLAYHFQA SHLPTLEKLA QNIDVKLGCD WVATIFSRDI RFANHETLQV
260 270 280 290 300
IYPYSPQNDD ELELVPGDFI FMSPMEQTST SEGWIYGTSL TTGCSGLLPE
310 320 330 340 350
NYITKADECS TWIFHGSYSI LNTVSSSSLA FGDGALERRQ YEDQGLGETT
360 370 380 390 400
PLTIICQPMQ PLRVNSQPGP QKRCLFVCRH GERMDVVFGK YWLSQCFDAK
410 420 430 440 450
GRYIRTNLNM PHSLPQRSGG FRDYEKDAPI TVFGCMQARL VGEALLESNT
460 470 480 490 500
VIDHVYCSPS LRCVQTAHNI LKGLQQDNHL KIRVEPGLFE WTKWVAGSTL
510 520 530 540 550
PAWIPPSELA AANLSVDTTY RPHIPVSKLA ISESYDTYIN RSFQVTKEII
560 570 580 590 600
SECKSKGNNI LIVAHASSLE ACTCQLQGLS PQNSKDFVQM VRKIPYLGFC
610 620 630
SCEELGETGI WQLTDPPILP LTHGPTGGFN WRETLLQE
Length:638
Mass (Da):71,443
Last modified:March 1, 2003 - v1
Checksum:i9B665F45AF208EF6
GO
Isoform 2 (identifier: Q8BGG7-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-122: Missing.

Show »
Length:516
Mass (Da):57,693
Checksum:i2F00BDB1F01C31FD
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti300 – 3001E → G in BAE30779. (PubMed:16141072)Curated
Sequence conflicti300 – 3001E → G in BAE30875. (PubMed:16141072)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 122122Missing in isoform 2. 1 PublicationVSP_019716Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB075602 mRNA. Translation: BAD06450.1.
AK013361 mRNA. Translation: BAC25403.1.
AK034450 mRNA. Translation: BAC28714.1.
AK035764 mRNA. Translation: BAC29178.1.
AK133948 mRNA. Translation: BAE21945.1.
AK151895 mRNA. Translation: BAE30779.1.
AK152013 mRNA. Translation: BAE30875.1.
AK154576 mRNA. Translation: BAE32688.1.
BC053436 mRNA. Translation: AAH53436.1.
CCDSiCCDS23085.1. [Q8BGG7-1]
RefSeqiNP_789830.1. NM_176860.5. [Q8BGG7-1]
XP_006510700.1. XM_006510637.1. [Q8BGG7-2]
UniGeneiMm.133615.

Genome annotation databases

EnsembliENSMUST00000044155; ENSMUSP00000043865; ENSMUSG00000032020. [Q8BGG7-1]
ENSMUST00000151485; ENSMUSP00000116038; ENSMUSG00000032020. [Q8BGG7-2]
GeneIDi72828.
KEGGimmu:72828.
UCSCiuc009pag.1. mouse. [Q8BGG7-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB075602 mRNA. Translation: BAD06450.1 .
AK013361 mRNA. Translation: BAC25403.1 .
AK034450 mRNA. Translation: BAC28714.1 .
AK035764 mRNA. Translation: BAC29178.1 .
AK133948 mRNA. Translation: BAE21945.1 .
AK151895 mRNA. Translation: BAE30779.1 .
AK152013 mRNA. Translation: BAE30875.1 .
AK154576 mRNA. Translation: BAE32688.1 .
BC053436 mRNA. Translation: AAH53436.1 .
CCDSi CCDS23085.1. [Q8BGG7-1 ]
RefSeqi NP_789830.1. NM_176860.5. [Q8BGG7-1 ]
XP_006510700.1. XM_006510637.1. [Q8BGG7-2 ]
UniGenei Mm.133615.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2H0Q X-ray 1.82 A/B/C 373-633 [» ]
2IKQ X-ray 2.61 A/B/M 369-638 [» ]
3MBK X-ray 1.35 A/B 373-636 [» ]
ProteinModelPortali Q8BGG7.
SMRi Q8BGG7. Positions 15-67, 238-317, 373-636.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi Q8BGG7. 1 interaction.
STRINGi 10090.ENSMUSP00000043865.

PTM databases

PhosphoSitei Q8BGG7.

Proteomic databases

MaxQBi Q8BGG7.
PaxDbi Q8BGG7.
PRIDEi Q8BGG7.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000044155 ; ENSMUSP00000043865 ; ENSMUSG00000032020 . [Q8BGG7-1 ]
ENSMUST00000151485 ; ENSMUSP00000116038 ; ENSMUSG00000032020 . [Q8BGG7-2 ]
GeneIDi 72828.
KEGGi mmu:72828.
UCSCi uc009pag.1. mouse. [Q8BGG7-1 ]

Organism-specific databases

CTDi 84959.
MGIi MGI:1920078. Ubash3b.

Phylogenomic databases

eggNOGi NOG276661.
GeneTreei ENSGT00390000018249.
HOGENOMi HOG000012936.
HOVERGENi HBG018025.
InParanoidi Q8BGG7.
OMAi ADECGTW.
OrthoDBi EOG7P5T0D.
PhylomeDBi Q8BGG7.
TreeFami TF313334.

Miscellaneous databases

EvolutionaryTracei Q8BGG7.
NextBioi 337005.
PROi Q8BGG7.
SOURCEi Search...

Gene expression databases

Bgeei Q8BGG7.
CleanExi MM_UBASH3B.
ExpressionAtlasi Q8BGG7. baseline and differential.
Genevestigatori Q8BGG7.

Family and domain databases

Gene3Di 3.40.50.1240. 1 hit.
InterProi IPR013078. His_Pase_superF_clade-1.
IPR029033. His_PPase_superfam.
IPR001452. SH3_domain.
IPR009060. UBA-like.
IPR015940. UBA/transl_elong_EF1B_N_euk.
IPR000449. UBA/Ts_N.
[Graphical view ]
Pfami PF00300. His_Phos_1. 1 hit.
PF14604. SH3_9. 1 hit.
PF00627. UBA. 1 hit.
[Graphical view ]
SMARTi SM00326. SH3. 1 hit.
SM00165. UBA. 1 hit.
[Graphical view ]
SUPFAMi SSF46934. SSF46934. 1 hit.
SSF50044. SSF50044. 1 hit.
SSF53254. SSF53254. 2 hits.
PROSITEi PS50002. SH3. 1 hit.
PS50030. UBA. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "NF-E2 inducible megakaryocyte specific novel gene."
    Nagata Y., Oda M., Haruta H., Todokoro K.
    Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Megakaryocyte.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
    Strain: C57BL/6J and NOD.
    Tissue: Bone marrow, Cerebellum, Dendritic cell, Diencephalon and Embryo.
  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] (ISOFORM 1).
    Tissue: Embryonic limb.
  4. "Identification, cDNA cloning, and targeted deletion of p70, a novel, ubiquitously expressed SH3 domain-containing protein."
    Carpino N., Kobayashi R., Zang H., Takahashi Y., Jou S.-T., Feng J., Nakajima H., Ihle J.N.
    Mol. Cell. Biol. 22:7491-7500(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 93-101; 199-215; 403-410; 482-493 AND 495-515, INTERACTION WITH JAK2, TISSUE SPECIFICITY.
  5. "Regulation of ZAP-70 activation and TCR signaling by two related proteins, Sts-1 and Sts-2."
    Carpino N., Turner S., Mekala D., Takahashi Y., Zang H., Geiger T.L., Doherty P., Ihle J.N.
    Immunity 20:37-46(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TISSUE SPECIFICITY.
  6. "The Sts proteins target tyrosine phosphorylated, ubiquitinated proteins within TCR signaling pathways."
    Carpino N., Chen Y., Nassar N., Oh H.W.
    Mol. Immunol. 46:3224-3231(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE.
  7. "A novel histidine tyrosine phosphatase, TULA-2, associates with Syk and negatively regulates GPVI signaling in platelets."
    Thomas D.H., Getz T.M., Newman T.N., Dangelmaier C.A., Carpino N., Kunapuli S.P., Tsygankov A.Y., Daniel J.L.
    Blood 116:2570-2578(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE.
  8. "Determination of the substrate specificity of protein-tyrosine phosphatase TULA-2 and identification of Syk as a TULA-2 substrate."
    Chen X., Ren L., Kim S., Carpino N., Daniel J.L., Kunapuli S.P., Tsygankov A.Y., Pei D.
    J. Biol. Chem. 285:31268-31276(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY.
  9. "The 1.35 A resolution structure of the phosphatase domain of the suppressor of T-cell receptor signaling protein in complex with sulfate."
    Jakoncic J., Sondgeroth B., Carpino N., Nassar N.
    Acta Crystallogr. F 66:643-647(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.35 ANGSTROMS) OF 373-636 IN COMPLEX WITH SULFATE, SUBUNIT, ACTIVE SITE.
  10. "A phosphatase activity of Sts-1 contributes to the suppression of TCR signaling."
    Mikhailik A., Ford B., Keller J., Chen Y., Nassar N., Carpino N.
    Mol. Cell 27:486-497(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.82 ANGSTROMS) OF 373-633, SUBUNIT, FUNCTION, PHOSPHATASE ACTIVITY, ACTIVE SITE.

Entry informationi

Entry nameiUBS3B_MOUSE
AccessioniPrimary (citable) accession number: Q8BGG7
Secondary accession number(s): Q3U8Z2, Q8BMW9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 11, 2006
Last sequence update: March 1, 2003
Last modified: October 29, 2014
This is version 102 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3