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Q76I76

- SSH2_HUMAN

UniProt

Q76I76 - SSH2_HUMAN

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Protein

Protein phosphatase Slingshot homolog 2

Gene
SSH2, KIAA1725, SSH2L
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Protein phosphatase which regulates actin filament dynamics. Dephosphorylates and activates the actin binding/depolymerizing factor cofilin, which subsequently binds to actin filaments and stimulates their disassembly. Inhibitory phosphorylation of cofilin is mediated by LIMK1, which may also be dephosphorylated and inactivated by this protein.1 Publication

Catalytic activityi

Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.
[a protein]-serine/threonine phosphate + H2O = [a protein]-serine/threonine + phosphate.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei392 – 3921Phosphocysteine intermediate1 Publication

GO - Molecular functioni

  1. actin binding Source: UniProtKB
  2. DNA binding Source: InterPro
  3. phosphoprotein phosphatase activity Source: UniProtKB
  4. protein tyrosine/serine/threonine phosphatase activity Source: RefGenome
  5. protein tyrosine phosphatase activity Source: UniProtKB-EC

GO - Biological processi

  1. actin cytoskeleton organization Source: UniProtKB
  2. protein dephosphorylation Source: UniProtKB
  3. regulation of actin polymerization or depolymerization Source: RefGenome
  4. regulation of axonogenesis Source: RefGenome
  5. regulation of lamellipodium assembly Source: RefGenome
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protein phosphatase

Keywords - Ligandi

Actin-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Protein phosphatase Slingshot homolog 2 (EC:3.1.3.16, EC:3.1.3.48)
Alternative name(s):
SSH-like protein 2
Short name:
SSH-2L
Short name:
hSSH-2L
Gene namesi
Name:SSH2
Synonyms:KIAA1725, SSH2L
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 17

Organism-specific databases

HGNCiHGNC:30580. SSH2.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: RefGenome
  2. cytoskeleton Source: UniProtKB-SubCell
  3. extracellular space Source: UniProt
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi392 – 3921C → S: Abrogates phosphatase activity. 1 Publication

Organism-specific databases

PharmGKBiPA134861867.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 14231423Protein phosphatase Slingshot homolog 2PRO_0000094843Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei36 – 361Phosphoserine1 Publication
Modified residuei487 – 4871Phosphoserine1 Publication
Modified residuei1422 – 14221Phosphothreonine2 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ76I76.
PaxDbiQ76I76.
PRIDEiQ76I76.

PTM databases

PhosphoSiteiQ76I76.

Expressioni

Gene expression databases

ArrayExpressiQ76I76.
BgeeiQ76I76.
CleanExiHS_SSH2.
GenevestigatoriQ76I76.

Organism-specific databases

HPAiCAB017189.

Interactioni

Subunit structurei

Interacts with filamentous actin.1 Publication

Protein-protein interaction databases

BioGridi124548. 5 interactions.
STRINGi9606.ENSP00000269033.

Structurei

Secondary structure

1
1423
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi309 – 3124
Beta strandi315 – 3184
Helixi320 – 3234
Helixi326 – 3316
Beta strandi334 – 3396
Beta strandi342 – 3443
Beta strandi352 – 3565
Helixi368 – 3703
Helixi371 – 38313
Beta strandi387 – 3915
Beta strandi393 – 3975
Helixi398 – 41114
Helixi415 – 42511
Helixi433 – 44715

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2NT2X-ray2.10A/B/C305-449[»]
ProteinModelPortaliQ76I76.
SMRiQ76I76. Positions 307-448.

Miscellaneous databases

EvolutionaryTraceiQ76I76.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini307 – 447141Tyrosine-protein phosphataseAdd
BLAST

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG2453.
HOVERGENiHBG094002.
InParanoidiQ76I76.
KOiK05766.
OrthoDBiEOG7B8S33.
PhylomeDBiQ76I76.
TreeFamiTF319444.

Family and domain databases

Gene3Di1.10.10.60. 1 hit.
3.90.190.10. 1 hit.
InterProiIPR014876. DEK_C.
IPR000340. Dual-sp_phosphatase_cat-dom.
IPR020422. Dual-sp_phosphatase_subgr_cat.
IPR024950. DUSP.
IPR009057. Homeodomain-like.
IPR029021. Prot-tyrosine_phosphatase-like.
IPR000387. Tyr/Dual-sp_Pase.
IPR016130. Tyr_Pase_AS.
[Graphical view]
PANTHERiPTHR10159. PTHR10159. 1 hit.
PfamiPF08766. DEK_C. 1 hit.
PF00782. DSPc. 1 hit.
[Graphical view]
SMARTiSM00195. DSPc. 1 hit.
[Graphical view]
SUPFAMiSSF52799. SSF52799. 1 hit.
PROSITEiPS00383. TYR_PHOSPHATASE_1. 1 hit.
PS50056. TYR_PHOSPHATASE_2. 1 hit.
PS50054. TYR_PHOSPHATASE_DUAL. 1 hit.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q76I76-1) [UniParc]FASTAAdd to Basket

Also known as: L

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

MALVTVQRSP TPSTTSSPCA SEADSGEEEC RSQPRSISES FLTVKGAALF     50
LPRGNGSSTP RISHRRNKHA GDLQQHLQAM FILLRPEDNI RLAVRLESTY 100
QNRTRYMVVV STNGRQDTEE SIVLGMDFSS NDSSTCTMGL VLPLWSDTLI 150
HLDGDGGFSV STDNRVHIFK PVSVQAMWSA LQSLHKACEV ARAHNYYPGS 200
LFLTWVSYYE SHINSDQSSV NEWNAMQDVQ SHRPDSPALF TDIPTERERT 250
ERLIKTKLRE IMMQKDLENI TSKEIRTELE MQMVCNLREF KEFIDNEMIV 300
ILGQMDSPTQ IFEHVFLGSE WNASNLEDLQ NRGVRYILNV TREIDNFFPG 350
VFEYHNIRVY DEEATDLLAY WNDTYKFISK AKKHGSKCLV HCKMGVSRSA 400
STVIAYAMKE YGWNLDRAYD YVKERRTVTK PNPSFMRQLE EYQGILLASK 450
QRHNKLWRSH SDSDLSDHHE PICKPGLELN KKDITTSADQ IAEVKTMESH 500
PPIPPVFVEH MVPQDANQKG LCTKERMICL EFTSREFHAG QIEDELNLND 550
INGCSSGCCL NESKFPLDNC HASKALIQPG HVPEMANKFP DLTVEDLETD 600
ALKADMNVHL LPMEELTSPL KDPPMSPDPE SPSPQPSCQT EISDFSTDRI 650
DFFSALEKFV ELSQETRSRS FSHSRMEELG GGRNESCRLS VVEVAPSKVT 700
ADDQRSSSLS NTPHASEESS MDEEQSKAIS ELVSPDIFMQ SHSENAISVK 750
EIVTEIESIS QGVGQIQLKG DILPNPCHTP KKNSIHELLL ERAQTPENKP 800
GHMEQDEDSC TAQPELAKDS GMCNPEGCLT THSSIADLEE GEPAEGEQEL 850
QGSGMHPGAK WYPGSVRRAT LEFEERLRQE QEHHGAAPTC TSLSTRKNSK 900
NDSSVADLAP KGKSDEAPPE HSFVLKEPEM SKGKGKYSGS EAGSLSHSEQ 950
NATVPAPRVL EFDHLPDPQE GPGSDTGTQQ EGVLKDLRTV IPYQESETQA 1000
VPLPLPKRVE IIEYTHIVTS PNHTGPGSEI ATSEKSGEQG LRKVNMEKSV 1050
TVLCTLDENL NRTLDPNQVS LHPQVLPLPH SSSPEHNRPT DHPTSILSSP 1100
EDRGSSLSTA LETAAPFVSH TTHLLSASLD YLHPQTMVHL EGFTEQSSTT 1150
DEPSAEQVSW EESQESPLSS GSEVPYKDSQ LSSADLSLIS KLGDNTGELQ 1200
EKMDPLPVAC RLPHSSSSEN IKSLSHSPGV VKERAKEIES RVVFQAGLTK 1250
PSQMRRSASL AKLGYLDLCK DCLPEREPAS CESPHLKLLQ PFLRTDSGMH 1300
AMEDQESLEN PGAPHNPEPT KSFVEQLTTT ECIVQSKPVE RPLVQYAKEF 1350
GSSQQYLLPR AGLELTSSEG GLPVLQTQGL QCACPAPGLA VAPRQQHGRT 1400
HPLRRLKKAN DKKRTTNPFY NTM 1423
Length:1,423
Mass (Da):158,216
Last modified:July 5, 2004 - v1
Checksum:i23D0B59C97D6BE38
GO
Isoform 2 (identifier: Q76I76-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-36: MALVTVQRSP...EEECRSQPRS → MTLSTLARKR...VISQNAINQL
     179-195: SALQSLHKACEVARAHN → VDRDSRNKHCYVLLVEE
     196-1423: Missing.

Show »
Length:202
Mass (Da):22,470
Checksum:i027BBBE4C2D6FE7B
GO
Isoform 3 (identifier: Q76I76-3) [UniParc]FASTAAdd to Basket

Also known as: A

The sequence of this isoform differs from the canonical sequence as follows:
     179-195: SALQSLHKACEVARAHN → VDRDSRNKHCYVLLVEE
     196-1423: Missing.

Show »
Length:195
Mass (Da):21,685
Checksum:i21EB60284CB3E961
GO
Isoform 4 (identifier: Q76I76-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     449-449: S → R
     450-1423: Missing.

Note: No experimental confirmation available.

Show »
Length:449
Mass (Da):51,492
Checksum:iAFD156098A92A04D
GO

Sequence cautioni

The sequence AAH11636.2 differs from that shown. Reason: Erroneous initiation.
The sequence AAL92027.1 differs from that shown. Reason: Erroneous initiation.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti743 – 7431S → L.
Corresponds to variant rs2289629 [ dbSNP | Ensembl ].
VAR_051758
Natural varianti763 – 7631V → A.
Corresponds to variant rs6505140 [ dbSNP | Ensembl ].
VAR_051759
Natural varianti1300 – 13001H → Q.
Corresponds to variant rs8080046 [ dbSNP | Ensembl ].
VAR_051760

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 3636MALVT…SQPRS → MTLSTLARKRKAPLACTCSL GGPDMIPYFSANAVISQNAI NQL in isoform 2. VSP_016321Add
BLAST
Alternative sequencei179 – 19517SALQS…ARAHN → VDRDSRNKHCYVLLVEE in isoform 2 and isoform 3. VSP_016322Add
BLAST
Alternative sequencei196 – 14231228Missing in isoform 2 and isoform 3. VSP_016323Add
BLAST
Alternative sequencei449 – 4491S → R in isoform 4. VSP_016324
Alternative sequencei450 – 1423974Missing in isoform 4. VSP_016325Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB072358 mRNA. Translation: BAB84117.1.
AB072359 mRNA. Translation: BAB84118.1.
AB099290 mRNA. Translation: BAC97813.1.
BC008941 mRNA. Translation: AAH08941.1.
BC011636 mRNA. Translation: AAH11636.2. Different initiation.
BC068223 mRNA. Translation: AAH68223.1.
AF484838 mRNA. Translation: AAL92027.1. Different initiation.
AB051512 mRNA. Translation: BAB21816.1.
CCDSiCCDS11253.1. [Q76I76-1]
RefSeqiNP_001269058.1. NM_001282129.1.
NP_001269059.1. NM_001282130.1.
NP_001269060.1. NM_001282131.1.
NP_203747.2. NM_033389.3. [Q76I76-1]
UniGeneiHs.654754.

Genome annotation databases

EnsembliENST00000269033; ENSP00000269033; ENSG00000141298. [Q76I76-1]
GeneIDi85464.
KEGGihsa:85464.
UCSCiuc002heo.1. human. [Q76I76-1]
uc002hep.1. human. [Q76I76-4]
uc002her.3. human. [Q76I76-3]

Polymorphism databases

DMDMi74749833.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB072358 mRNA. Translation: BAB84117.1 .
AB072359 mRNA. Translation: BAB84118.1 .
AB099290 mRNA. Translation: BAC97813.1 .
BC008941 mRNA. Translation: AAH08941.1 .
BC011636 mRNA. Translation: AAH11636.2 . Different initiation.
BC068223 mRNA. Translation: AAH68223.1 .
AF484838 mRNA. Translation: AAL92027.1 . Different initiation.
AB051512 mRNA. Translation: BAB21816.1 .
CCDSi CCDS11253.1. [Q76I76-1 ]
RefSeqi NP_001269058.1. NM_001282129.1.
NP_001269059.1. NM_001282130.1.
NP_001269060.1. NM_001282131.1.
NP_203747.2. NM_033389.3. [Q76I76-1 ]
UniGenei Hs.654754.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2NT2 X-ray 2.10 A/B/C 305-449 [» ]
ProteinModelPortali Q76I76.
SMRi Q76I76. Positions 307-448.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 124548. 5 interactions.
STRINGi 9606.ENSP00000269033.

PTM databases

PhosphoSitei Q76I76.

Polymorphism databases

DMDMi 74749833.

Proteomic databases

MaxQBi Q76I76.
PaxDbi Q76I76.
PRIDEi Q76I76.

Protocols and materials databases

DNASUi 85464.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000269033 ; ENSP00000269033 ; ENSG00000141298 . [Q76I76-1 ]
GeneIDi 85464.
KEGGi hsa:85464.
UCSCi uc002heo.1. human. [Q76I76-1 ]
uc002hep.1. human. [Q76I76-4 ]
uc002her.3. human. [Q76I76-3 ]

Organism-specific databases

CTDi 85464.
GeneCardsi GC17M027952.
HGNCi HGNC:30580. SSH2.
HPAi CAB017189.
MIMi 606779. gene.
neXtProti NX_Q76I76.
PharmGKBi PA134861867.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG2453.
HOVERGENi HBG094002.
InParanoidi Q76I76.
KOi K05766.
OrthoDBi EOG7B8S33.
PhylomeDBi Q76I76.
TreeFami TF319444.

Miscellaneous databases

ChiTaRSi SSH2. human.
EvolutionaryTracei Q76I76.
GeneWikii SSH2.
GenomeRNAii 85464.
NextBioi 76121.
PROi Q76I76.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q76I76.
Bgeei Q76I76.
CleanExi HS_SSH2.
Genevestigatori Q76I76.

Family and domain databases

Gene3Di 1.10.10.60. 1 hit.
3.90.190.10. 1 hit.
InterProi IPR014876. DEK_C.
IPR000340. Dual-sp_phosphatase_cat-dom.
IPR020422. Dual-sp_phosphatase_subgr_cat.
IPR024950. DUSP.
IPR009057. Homeodomain-like.
IPR029021. Prot-tyrosine_phosphatase-like.
IPR000387. Tyr/Dual-sp_Pase.
IPR016130. Tyr_Pase_AS.
[Graphical view ]
PANTHERi PTHR10159. PTHR10159. 1 hit.
Pfami PF08766. DEK_C. 1 hit.
PF00782. DSPc. 1 hit.
[Graphical view ]
SMARTi SM00195. DSPc. 1 hit.
[Graphical view ]
SUPFAMi SSF52799. SSF52799. 1 hit.
PROSITEi PS00383. TYR_PHOSPHATASE_1. 1 hit.
PS50056. TYR_PHOSPHATASE_2. 1 hit.
PS50054. TYR_PHOSPHATASE_DUAL. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Control of actin reorganization by Slingshot, a family of phosphatases that dephosphorylate ADF/cofilin."
    Niwa R., Nagata-Ohashi K., Takeichi M., Mizuno K., Uemura T.
    Cell 108:233-246(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3 AND 4), FUNCTION, INTERACTION WITH ACTIN, MUTAGENESIS OF CYS-392.
  2. "Differential activities, subcellular distribution and tissue expression patterns of three members of Slingshot family phosphatases that dephosphorylate cofilin."
    Ohta Y., Kousaka K., Nagata-Ohashi K., Ohashi K., Muramoto A., Shima Y., Niwa R., Uemura T., Mizuno K.
    Genes Cells 8:811-824(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  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] (ISOFORMS 2 AND 3).
    Tissue: Brain and Lung.
  4. "Identification of genes expressed during myocardial development."
    Chan S.Y., Chan A.K.W., Cheung B.P.K., Liang Y., Leung M.P.
    Chin. Med. J. 116:1329-1332(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 282-409 (ISOFORMS 1/4).
  5. "Prediction of the coding sequences of unidentified human genes. XIX. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
    Nagase T., Kikuno R., Hattori A., Kondo Y., Okumura K., Ohara O.
    DNA Res. 7:347-355(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 382-1423 (ISOFORM 1).
    Tissue: Brain.
  6. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36 AND THR-1422, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  7. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-487 AND THR-1422, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  9. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. "Crystal structure of human slingshot phosphatase 2."
    Jung S.K., Jeong D.G., Yoon T.S., Kim J.H., Ryu S.E., Kim S.J.
    Proteins 68:408-412(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 305-448, ACTIVE SITE.

Entry informationi

Entry nameiSSH2_HUMAN
AccessioniPrimary (citable) accession number: Q76I76
Secondary accession number(s): Q8TDB5
, Q8WYL1, Q8WYL2, Q96F40, Q96H36, Q9C0D8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 22, 2005
Last sequence update: July 5, 2004
Last modified: July 9, 2014
This is version 103 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Miscellaneous

Tyrosine phosphatase activity has not been demonstrated for this protein to date.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 17
    Human chromosome 17: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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