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Q4VA53

- PDS5B_MOUSE

UniProt

Q4VA53 - PDS5B_MOUSE

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Protein
Sister chromatid cohesion protein PDS5 homolog B
Gene
Pds5b, Aprin, As3, Kiaa0979
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at protein leveli

Functioni

Regulator of sister chromatid cohesion in mitosis which may stabilize cohesin complex association with chromatin. May couple sister chromatid cohesion during mitosis to DNA replication. Cohesion ensures that chromosome partitioning is accurate in both meiotic and mitotic cells and plays an important role in DNA repair. Plays a role in androgen-induced proliferative arrest in prostate cells By similarity.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi1247 – 125913A.T hook 1
Add
BLAST
DNA bindingi1285 – 129713A.T hook 2
Add
BLAST
DNA bindingi1370 – 138213A.T hook 3
Add
BLAST

GO - Molecular functioni

  1. DNA binding Source: InterPro

GO - Biological processi

  1. mitotic sister chromatid cohesion Source: UniProtKB
  2. negative regulation of cell proliferation Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Cell cycle, Cell division, Mitosis

Enzyme and pathway databases

ReactomeiREACT_196614. Establishment of Sister Chromatid Cohesion.
REACT_196634. Cohesin Loading onto Chromatin.
REACT_198961. Resolution of Sister Chromatid Cohesion.
REACT_207679. Separation of Sister Chromatids.

Names & Taxonomyi

Protein namesi
Recommended name:
Sister chromatid cohesion protein PDS5 homolog B
Alternative name(s):
Androgen-induced proliferation inhibitor
Androgen-induced prostate proliferative shutoff-associated protein AS3
Gene namesi
Name:Pds5b
Synonyms:Aprin, As3, Kiaa0979
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 5

Organism-specific databases

MGIiMGI:2140945. Pds5b.

Subcellular locationi

Nucleus By similarity By similarity

GO - Cellular componenti

  1. chromatin Source: Ensembl
  2. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 14461446Sister chromatid cohesion protein PDS5 homolog B
PRO_0000287425Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1136 – 11361N6-acetyllysine1 Publication
Modified residuei1162 – 11621Phosphoserine By similarity
Modified residuei1166 – 11661PhosphoserineBy similarity1 Publication
Modified residuei1176 – 11761Phosphoserine By similarity
Modified residuei1182 – 11821Phosphoserine By similarity
Modified residuei1191 – 11911Phosphoserine By similarity
Modified residuei1253 – 12531Phosphothreonine1 Publication
Modified residuei1255 – 12551Phosphoserine By similarityBy similarity
Modified residuei1257 – 12571Phosphoserine1 Publication
Modified residuei1281 – 12811Phosphoserine1 Publication
Modified residuei1356 – 13561Phosphoserine3 Publications
Modified residuei1365 – 13651Phosphothreonine By similarity
Modified residuei1368 – 13681Phosphothreonine By similarityBy similarity
Modified residuei1377 – 13771Phosphoserine By similarityBy similarity
Modified residuei1381 – 13811Phosphoserine By similarityBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ4VA53.
PaxDbiQ4VA53.
PRIDEiQ4VA53.

PTM databases

PhosphoSiteiQ4VA53.

Expressioni

Tissue specificityi

Expressed in prostate.1 Publication

Gene expression databases

ArrayExpressiQ4VA53.
BgeeiQ4VA53.
GenevestigatoriQ4VA53.

Interactioni

Subunit structurei

Interacts with the cohesin complex. Interacts with RAD21; the interaction is direct. Interacts with WAPAL (via FGF motifs) or CDCA5 (via the FGF motif); the interaction is direct, cohesin-dependent and competitive By similarity.

Protein-protein interaction databases

BioGridi221515. 2 interactions.
IntActiQ4VA53. 1 interaction.
MINTiMINT-5056218.

Structurei

3D structure databases

ProteinModelPortaliQ4VA53.
SMRiQ4VA53. Positions 68-94, 349-418.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati383 – 41937HEAT
Add
BLAST

Sequence similaritiesi

Belongs to the PDS5 family.
Contains 1 HEAT repeat.

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiNOG268017.
GeneTreeiENSGT00390000012488.
HOVERGENiHBG108241.
InParanoidiQ4VA53.
KOiK11267.
OrthoDBiEOG73Z2SD.
PhylomeDBiQ4VA53.
TreeFamiTF106415.

Family and domain databases

Gene3Di1.25.10.10. 4 hits.
InterProiIPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR017956. AT_hook_DNA-bd_motif.
[Graphical view]
SMARTiSM00384. AT_hook. 3 hits.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 5 hits.

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 11 Publication (identifier: Q4VA53-1) [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

MAHSKTRTND GKITYPPGVK EISDKISKEE MVRRLKMVVK TFMDMDQDSE     50
EEKELYLNLA LHLASDFFLK HPDKDVRLLV ACCLADIFRI YAPEAPYTSP 100
DKLKDIFMFI TRQLKGLEDT KSPQFNRYFY LLENIAWVKS YNICFELEDS 150
NEIFTQLYRT LFSVINNGHN QKVHMHMVDL MSSIICEGDT VSQELLDTVL 200
VNLVPAHKNL NKQAYDLAKA LLKRTAQAIE PYITNFFNQV LMLGKTSISD 250
LSEHVFDLIL ELYNIDSHLL LSVLPQLEFK LKSNDNEERL QVVKLLAKMF 300
GAKDSELASQ NKPLWQCYLG RFNDIHVPIR LECVKFASHC LMNHPDLAKD 350
LTEYLKVRSH DPEEAIRHDV IVSIVTAAKK DILLVNDHLL NFVRERTLDK 400
RWRVRKEAMM GLAQIYKKYS LQSAAGKDAA KQISWVKDKL LHIYYQNSID 450
DRLLVERIFA QYMVPHNLET TERMKCLYYL YATLDLNAVK ALNEMWKCQN 500
LLRHQVKDLL DLIKQPKTDA SVKAIFSKVM VITRNLPDPG KAQDFMKKFT 550
QVLEDDEKIR KQLEALVSPT CSCKQAEGCV REITKKLGNP KQPTNPFLEM 600
IKFLLERIAP VHIDTESISA LIKQVNKSID GTADDEDEGV PTDQAIRAGL 650
ELLKVLSFTH PISFHSAETF ESLLACLKMD DEKVAEAALQ IFKNTGSKIE 700
EDFPHIRSAL LPVLHHKSKK GPPRQAKYAI HCIHAIFSSK ETQFAQIFEP 750
LHKSLDPSNL EHLITPLVTI GHIALLAPDQ FAAPLKSLVA TFIVKDLLMN 800
DRLPGKKTTK LWVPDEEVSP ETMVKIQAIK MMVRWLLGMK NNHSKSGTST 850
LRLLTTILHS DGDLTEQGKI SKPDMSRLRL AAGSAIVKLA QEPCYHEIIT 900
LEQYQLCALA INDECYQVRQ VFAQKLHKGL SRLRLPLEYM AICALCAKDP 950
VKERRAHARQ CLVKNITVRR EYLKQHAAVS EKLLSLLPEY VVPYTIHLLA 1000
HDPDYVKVQD IEQLKDVKEC LWFVLEILMA KNENNSHAFI RKMVENIKQT 1050
KDAQGPDDTK MNEKLYTVCD VAMNIIMSKS TTYSLESPKD PVLPARFFTQ 1100
PDKNFSNTKN YLPPEMKSFF TPGKPKTANV LGAVNKPLSS AGKQSQTKSS 1150
RMETVSNASS SSNPSSPGRI KGRLDSSEMD HSENEDYTMS SPLPGKKSDK 1200
REDPDLSELE KPRSRKKAPV TDPEEKLGMD DLTKLVQEQK PKGSQRGRKR 1250
GRTASDSDEQ QWPEEKRHKE ELLENEDEQN SPPKKGKRGR PPKPLGGGTS 1300
KEEPTMKTSK KGNKKKLVPP VVDDDEEEER QIGNTEHKSK SKQHRTSKRA 1350
QQRAESPETS AVESTQSTPQ KGRGRPSKAP SPSQPPKKIR VGRSKQVATK 1400
ENDSSEEMDV LQASSPVSDD TTQEGAEEED ISVGNVRRRS SKRERR 1446
Length:1,446
Mass (Da):164,419
Last modified:July 5, 2005 - v1
Checksum:i3540041DE3C7FCBE
GO
Isoform 21 Publication (identifier: Q4VA53-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-529: Missing.
     1207-1230: SELEKPRSRKKAPVTDPEEKLGMD → VRVRCLVGRVMRLLIVIVLVIFAL
     1231-1446: Missing.

Note: No experimental confirmation available.

Show »
Length:701
Mass (Da):78,714
Checksum:iFAF6F0351AF7869B
GO
Isoform 31 Publication (identifier: Q4VA53-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1206-1206: L → LVR

Note: No experimental confirmation available.

Show »
Length:1,448
Mass (Da):164,674
Checksum:i80CFDE441169F45E
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 529529Missing in isoform 2. 1 Publication
VSP_052403Add
BLAST
Alternative sequencei1206 – 12061L → LVR in isoform 3. 1 Publication
VSP_052404
Alternative sequencei1207 – 123024SELEK…KLGMD → VRVRCLVGRVMRLLIVIVLV IFAL in isoform 2. 1 Publication
VSP_052405Add
BLAST
Alternative sequencei1231 – 1446216Missing in isoform 2. 1 Publication
VSP_052406Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti496 – 4961W → R in AAM52216. 1 Publication
Sequence conflicti966 – 9661I → T in AAM52216. 1 Publication
Sequence conflicti978 – 9781A → S in AAM52216. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY102267 mRNA. Translation: AAM52216.1.
AK041682 mRNA. Translation: BAC31031.1.
AK045159 mRNA. Translation: BAC32242.1.
AK048706 mRNA. Translation: BAC33427.1.
AK164853 mRNA. Translation: BAE37943.1.
BC096539 mRNA. Translation: AAH96539.1.
AK122414 mRNA. Translation: BAC65696.1.
CCDSiCCDS39412.1. [Q4VA53-1]
RefSeqiNP_780519.3. NM_175310.6. [Q4VA53-1]
XP_006504965.1. XM_006504902.1. [Q4VA53-3]
UniGeneiMm.32959.

Genome annotation databases

EnsembliENSMUST00000016569; ENSMUSP00000016569; ENSMUSG00000034021. [Q4VA53-1]
ENSMUST00000110486; ENSMUSP00000106112; ENSMUSG00000034021. [Q4VA53-2]
GeneIDi100710.
KEGGimmu:100710.
UCSCiuc009auh.2. mouse. [Q4VA53-1]
uc009aui.1. mouse. [Q4VA53-2]
uc009auj.2. mouse. [Q4VA53-3]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY102267 mRNA. Translation: AAM52216.1 .
AK041682 mRNA. Translation: BAC31031.1 .
AK045159 mRNA. Translation: BAC32242.1 .
AK048706 mRNA. Translation: BAC33427.1 .
AK164853 mRNA. Translation: BAE37943.1 .
BC096539 mRNA. Translation: AAH96539.1 .
AK122414 mRNA. Translation: BAC65696.1 .
CCDSi CCDS39412.1. [Q4VA53-1 ]
RefSeqi NP_780519.3. NM_175310.6. [Q4VA53-1 ]
XP_006504965.1. XM_006504902.1. [Q4VA53-3 ]
UniGenei Mm.32959.

3D structure databases

ProteinModelPortali Q4VA53.
SMRi Q4VA53. Positions 68-94, 349-418.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 221515. 2 interactions.
IntActi Q4VA53. 1 interaction.
MINTi MINT-5056218.

PTM databases

PhosphoSitei Q4VA53.

Proteomic databases

MaxQBi Q4VA53.
PaxDbi Q4VA53.
PRIDEi Q4VA53.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000016569 ; ENSMUSP00000016569 ; ENSMUSG00000034021 . [Q4VA53-1 ]
ENSMUST00000110486 ; ENSMUSP00000106112 ; ENSMUSG00000034021 . [Q4VA53-2 ]
GeneIDi 100710.
KEGGi mmu:100710.
UCSCi uc009auh.2. mouse. [Q4VA53-1 ]
uc009aui.1. mouse. [Q4VA53-2 ]
uc009auj.2. mouse. [Q4VA53-3 ]

Organism-specific databases

CTDi 23047.
MGIi MGI:2140945. Pds5b.
Rougei Search...

Phylogenomic databases

eggNOGi NOG268017.
GeneTreei ENSGT00390000012488.
HOVERGENi HBG108241.
InParanoidi Q4VA53.
KOi K11267.
OrthoDBi EOG73Z2SD.
PhylomeDBi Q4VA53.
TreeFami TF106415.

Enzyme and pathway databases

Reactomei REACT_196614. Establishment of Sister Chromatid Cohesion.
REACT_196634. Cohesin Loading onto Chromatin.
REACT_198961. Resolution of Sister Chromatid Cohesion.
REACT_207679. Separation of Sister Chromatids.

Miscellaneous databases

NextBioi 354602.
PROi Q4VA53.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q4VA53.
Bgeei Q4VA53.
Genevestigatori Q4VA53.

Family and domain databases

Gene3Di 1.25.10.10. 4 hits.
InterProi IPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR017956. AT_hook_DNA-bd_motif.
[Graphical view ]
SMARTi SM00384. AT_hook. 3 hits.
[Graphical view ]
SUPFAMi SSF48371. SSF48371. 5 hits.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "The AS3 proliferative arrest gene has an ancient eukaryotic heritage and shows highly conserved functional domains in mice."
    Geck P., Maffini M., Sonnenschein C., Soto A.M.
    Proc. Annu. Meet. Am. Assoc. Cancer Res. 43:987-987(2002)
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
    Strain: BALB/c.
    Tissue: Brain.
  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] (ISOFORM 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 625-1446 (ISOFORM 3), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1092-1446 (ISOFORM 1).
    Strain: C57BL/6J.
    Tissue: Cerebellum, Embryo, Head and Thymus.
  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).
    Strain: C57BL/6.
    Tissue: Brain.
  4. "Prediction of the coding sequences of mouse homologues of KIAA gene: II. The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
    Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S., Nakajima D., Nagase T., Ohara O., Koga H.
    DNA Res. 10:35-48(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 256-1446 (ISOFORM 1).
    Tissue: Brain.
  5. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1356, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic brain.
  6. "Comprehensive identification of phosphorylation sites in postsynaptic density preparations."
    Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.
    Mol. Cell. Proteomics 5:914-922(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1356, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain.
  7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1166; THR-1253; SER-1257; SER-1281 AND SER-1356, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  8. "Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
    Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
    Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.
  9. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-1136, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.

Entry informationi

Entry nameiPDS5B_MOUSE
AccessioniPrimary (citable) accession number: Q4VA53
Secondary accession number(s): Q3TNZ4
, Q7TSS4, Q80TM8, Q8BJ18, Q8BLH6, Q8BX77
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 15, 2007
Last sequence update: July 5, 2005
Last modified: September 3, 2014
This is version 81 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

Complete proteome, Reference proteome

Documents

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

External Data

Dasty 3

Similar proteinsi