Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q13322

- GRB10_HUMAN

UniProt

Q13322 - GRB10_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Growth factor receptor-bound protein 10

Gene

GRB10

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

Functioni

Adapter protein which modulates coupling of a number of cell surface receptor kinases with specific signaling pathways. Binds to, and suppress signals from, activated receptors tyrosine kinases, including the insulin (INSR) and insulin-like growth factor (IGF1R) receptors. The inhibitory effect can be achieved by 2 mechanisms: interference with the signaling pathway and increased receptor degradation. Delays and reduces AKT1 phosphorylation in response to insulin stimulation. Blocks association between INSR and IRS1 and IRS2 and prevents insulin-stimulated IRS1 and IRS2 tyrosine phosphorylation. Recruits NEDD4 to IGF1R, leading to IGF1R ubiquitination, increased internalization and degradation by both the proteasomal and lysosomal pathways. May play a role in mediating insulin-stimulated ubiquitination of INSR, leading to proteasomal degradation. Negatively regulates Wnt signaling by interacting with LRP6 intracellular portion and interfering with the binding of AXIN1 to LRP6. Positive regulator of the KDR/VEGFR-2 signaling pathway. May inhibit NEDD4-mediated degradation of KDR/VEGFR-2.4 Publications

Enzyme regulationi

Phosphorylation by mTORC1 stabilizes and activates GRB10 constituting a feedback pathway by which mTORC1 inhibits INSR-dependent signaling.1 Publication

GO - Molecular functioni

  1. insulin receptor binding Source: BHF-UCL
  2. SH3/SH2 adaptor activity Source: ProtInc

GO - Biological processi

  1. insulin-like growth factor receptor signaling pathway Source: Ensembl
  2. insulin receptor signaling pathway Source: BHF-UCL
  3. negative regulation of glucose import Source: BHF-UCL
  4. negative regulation of glycogen biosynthetic process Source: Ensembl
  5. negative regulation of insulin receptor signaling pathway Source: BHF-UCL
  6. negative regulation of phosphorylation Source: Ensembl
  7. negative regulation of Wnt signaling pathway Source: UniProtKB
  8. positive regulation of phosphorylation Source: Ensembl
  9. positive regulation of vascular endothelial growth factor receptor signaling pathway Source: UniProtKB
  10. response to insulin Source: BHF-UCL
Complete GO annotation...

Enzyme and pathway databases

ReactomeiREACT_111040. Signaling by SCF-KIT.
REACT_1661. SHC activation.
REACT_508. Signal attenuation.
REACT_570. IRS activation.
SignaLinkiQ13322.

Names & Taxonomyi

Protein namesi
Recommended name:
Growth factor receptor-bound protein 10
Alternative name(s):
GRB10 adapter protein
Insulin receptor-binding protein Grb-IR
Gene namesi
Name:GRB10
Synonyms:GRBIR, KIAA0207
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 7

Organism-specific databases

HGNCiHGNC:4564. GRB10.

Subcellular locationi

Cytoplasm By similarity
Note: When complexed with NEDD4 and IGF1R, follows IGF1R internalization, remaining associated with early endosomes. Uncouples from IGF1R-containing endosomes before the sorting of the receptor to the lysosomal compartment (By similarity).By similarity

GO - Cellular componenti

  1. cytoplasm Source: ProtInc
  2. cytosol Source: Reactome
  3. plasma membrane Source: ProtInc
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi104 – 1041S → G: No effect on phosphorylation. 1 Publication
Mutagenesisi134 – 1341S → A: No effect on YWHAE-binding. 1 Publication
Mutagenesisi136 – 1361P → A: No effect on NEDD4-binding; when associated with A-139 and A-141. 1 Publication
Mutagenesisi139 – 1391P → A: No effect on NEDD4-binding; when associated with A-136 and A-141. 1 Publication
Mutagenesisi141 – 1411P → S: No effect on NEDD4-binding; when associated with A-136 and A-139. 1 Publication
Mutagenesisi150 – 1501S → I: Loss of phosphorylation. 1 Publication
Mutagenesisi300 – 3001K → A: 2-fold loss of inositide-binding. 1 Publication
Mutagenesisi305 – 3051K → A: 5-fold loss of inositide-binding. 1 Publication
Mutagenesisi308 – 3081K → A: 5-fold loss of inositide-binding. 1 Publication
Mutagenesisi355 – 3551N → G: 5-fold loss of inositide-binding. 1 Publication
Mutagenesisi418 – 4181S → A: No net loss of phosphorylation, this may be due to a compensatory phosphorylation of T-422 in vitro. 1 Publication
Mutagenesisi428 – 4281S → A: Impairs YWHAE-binding. 1 Publication
Mutagenesisi476 – 4761S → A: Loss of phosphorylation. 1 Publication
Mutagenesisi520 – 5201R → K: No effect on NEDD4-binding. No effect on the disruption of the interaction between INSR and IRS1 and IRS2. 2 Publications

Organism-specific databases

PharmGKBiPA28960.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 594594Growth factor receptor-bound protein 10PRO_0000150346Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei67 – 671Phosphotyrosine; by TEC1 Publication
Modified residuei104 – 1041Phosphoserine1 Publication
Modified residuei150 – 1501Phosphoserine; by MTOR, MAPK1 and MAPK32 Publications
Modified residuei418 – 4181Phosphoserine; by MAPK1 and MAPK3; in vitro3 Publications
Modified residuei428 – 4281Phosphoserine; by MTOR and PKB/AKT12 Publications
Modified residuei431 – 4311PhosphoserineBy similarity
Modified residuei476 – 4761Phosphoserine; by MTOR, MAPK1 and MAPK32 Publications

Post-translational modificationi

Phosphorylated on serine residues upon EGF, FGF and PDGF stimulation (By similarity). Phosphorylated at Tyr-67 by TEC.By similarity6 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ13322.
PaxDbiQ13322.
PRIDEiQ13322.

PTM databases

PhosphoSiteiQ13322.

Expressioni

Tissue specificityi

Widely expressed in fetal and adult tissues, including fetal and postnatal liver, lung, kidney, skeletal muscle, heart, spleen, skin and brain.1 Publication

Gene expression databases

BgeeiQ13322.
CleanExiHS_GRB10.
ExpressionAtlasiQ13322. baseline and differential.
GenevestigatoriQ13322.

Organism-specific databases

HPAiCAB019423.
HPA027502.

Interactioni

Subunit structurei

Interacts with ligand-activated tyrosine kinase receptors, including FGFR1, INSR, IGF1R, MET and PDGFRB in a phosphotyrosine-dependent manner through the SH2 domain (By similarity). Poorly binds to the EGFR (By similarity). Directly interacts with MAP3K14/NIK and is recruited to the EGFR-ERBB2 complex. Interacts with GIGYF1/PERQ1 and GIGYF2/TNRC15 (By similarity). When unphosphorylated, interacts with AKT1 and when phosphorylated with YWHAE/14-3-3 epsilon. Interacts with NEDD4. Interacts with LRP6, thus interfering with the binding of AXIN1 to LRP6 (By similarity). Binds to activated NRAS.By similarity5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
EPHB1P547622EBI-80275,EBI-80252
INSRP062133EBI-80275,EBI-475899

Protein-protein interaction databases

BioGridi109144. 31 interactions.
DIPiDIP-31657N.
IntActiQ13322. 11 interactions.
MINTiMINT-1534184.
STRINGi9606.ENSP00000381793.

Structurei

Secondary structure

1
594
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi168 – 1747Combined sources
Beta strandi179 – 1846Combined sources
Helixi190 – 1989Combined sources
Beta strandi209 – 2157Combined sources
Turni216 – 2194Combined sources
Beta strandi220 – 2234Combined sources
Helixi230 – 2356Combined sources
Beta strandi242 – 2476Combined sources
Turni249 – 2524Combined sources
Helixi253 – 2564Combined sources
Helixi258 – 2603Combined sources
Beta strandi266 – 2694Combined sources
Helixi281 – 2855Combined sources
Beta strandi291 – 30010Combined sources
Beta strandi307 – 3159Combined sources
Beta strandi318 – 3247Combined sources
Helixi330 – 3323Combined sources
Beta strandi333 – 3375Combined sources
Beta strandi342 – 3498Combined sources
Helixi351 – 3544Combined sources
Beta strandi357 – 36610Combined sources
Beta strandi377 – 3837Combined sources
Helixi384 – 39916Combined sources
Helixi401 – 4077Combined sources
Helixi500 – 50910Combined sources
Beta strandi516 – 5216Combined sources
Beta strandi529 – 5357Combined sources
Beta strandi538 – 5469Combined sources
Beta strandi555 – 5584Combined sources
Beta strandi564 – 5663Combined sources
Helixi567 – 5748Combined sources
Beta strandi581 – 5833Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1NRVX-ray1.65A/B487-591[»]
3HK0X-ray2.60A/B164-415[»]
ProteinModelPortaliQ13322.
SMRiQ13322. Positions 167-409, 429-465, 487-593.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ13322.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini166 – 25085Ras-associatingPROSITE-ProRule annotationAdd
BLAST
Domaini290 – 399110PHPROSITE-ProRule annotationAdd
BLAST
Domaini493 – 57482SH2PROSITE-ProRule annotationAdd
BLAST

Domaini

The PH domain binds relatively non-specifically to several phosphoinositides, including PI5P, PI(4,5)P2, PI(3,4)P2 and PI(3,4,5)P3, with modest affinities.

Sequence similaritiesi

Belongs to the GRB7/10/14 family.Curated
Contains 1 PH domain.PROSITE-ProRule annotation
Contains 1 Ras-associating domain.PROSITE-ProRule annotation
Contains 1 SH2 domain.PROSITE-ProRule annotation

Keywords - Domaini

SH2 domain

Phylogenomic databases

eggNOGiNOG307156.
GeneTreeiENSGT00550000074537.
HOVERGENiHBG000468.
InParanoidiQ13322.
OMAiESTMGSE.
OrthoDBiEOG7SFHW7.
PhylomeDBiQ13322.
TreeFamiTF317511.

Family and domain databases

Gene3Di2.30.29.30. 1 hit.
3.30.505.10. 1 hit.
InterProiIPR015042. BPS-dom.
IPR001849. PH_domain.
IPR011993. PH_like_dom.
IPR000159. Ras-assoc.
IPR000980. SH2.
IPR029071. Ubiquitin-rel_dom.
[Graphical view]
PfamiPF08947. BPS. 1 hit.
PF00169. PH. 1 hit.
PF00788. RA. 1 hit.
PF00017. SH2. 1 hit.
[Graphical view]
PRINTSiPR00401. SH2DOMAIN.
SMARTiSM00233. PH. 1 hit.
SM00314. RA. 1 hit.
SM00252. SH2. 1 hit.
[Graphical view]
SUPFAMiSSF54236. SSF54236. 1 hit.
SSF55550. SSF55550. 1 hit.
PROSITEiPS50003. PH_DOMAIN. 1 hit.
PS50200. RA. 1 hit.
PS50001. SH2. 1 hit.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. Align

Note: Additional isoforms seem to exist, many of which involve splicing of 5' non-coding exons.

Isoform 3 (identifier: Q13322-1) [UniParc]FASTAAdd to Basket

Also known as: Zeta

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
MALAGCPDSF LHHPYYQDKV EQTPRSQQDP AGPGLPAQSD RLANHQEDDV
60 70 80 90 100
DLEALVNDMN ASLESLYSAC SMQSDTVPLL QNGQHARSQP RASGPPRSIQ
110 120 130 140 150
PQVSPRQRVQ RSQPVHILAV RRLQEEDQQF RTSSLPAIPN PFPELCGPGS
160 170 180 190 200
PPVLTPGSLP PSQAAAKQDV KVFSEDGTSK VVEILADMTA RDLCQLLVYK
210 220 230 240 250
SHCVDDNSWT LVEHHPHLGL ERCLEDHELV VQVESTMASE SKFLFRKNYA
260 270 280 290 300
KYEFFKNPMN FFPEQMVTWC QQSNGSQTQL LQNFLNSSSC PEIQGFLHVK
310 320 330 340 350
ELGKKSWKKL YVCLRRSGLY CSTKGTSKEP RHLQLLADLE DSNIFSLIAG
360 370 380 390 400
RKQYNAPTDH GLCIKPNKVR NETKELRLLC AEDEQTRTCW MTAFRLLKYG
410 420 430 440 450
MLLYQNYRIP QQRKALLSPF STPVRSVSEN SLVAMDFSGQ TGRVIENPAE
460 470 480 490 500
AQSAALEEGH AWRKRSTRMN ILGSQSPLHP STLSTVIHRT QHWFHGRISR
510 520 530 540 550
EESHRIIKQQ GLVDGLFLLR DSQSNPKAFV LTLCHHQKIK NFQILPCEDD
560 570 580 590
GQTFFSLDDG NTKFSDLIQL VDFYQLNKGV LPCKLKHHCI RVAL
Length:594
Mass (Da):67,231
Last modified:July 15, 1999 - v2
Checksum:i53A5F885E17C6C6B
GO
Isoform 1 (identifier: Q13322-2) [UniParc]FASTAAdd to Basket

Also known as: Beta

The sequence of this isoform differs from the canonical sequence as follows:
     283-328: Missing.

Show »
Length:548
Mass (Da):62,026
Checksum:iFCAA0792DBEB8AC3
GO
Isoform 2 (identifier: Q13322-3) [UniParc]FASTAAdd to Basket

Also known as: Gamma, Beta, SV-1

The sequence of this isoform differs from the canonical sequence as follows:
     1-58: Missing.

Show »
Length:536
Mass (Da):60,848
Checksum:i626377A169AE6530
GO
Isoform 4 (identifier: Q13322-4) [UniParc]FASTAAdd to Basket

Also known as: Epsilon

The sequence of this isoform differs from the canonical sequence as follows:
     1-17: MALAGCPDSFLHHPYYQ → MQAAGPLFRSK

Note: No experimental confirmation available.

Show »
Length:588
Mass (Da):66,487
Checksum:iB5EE8FA86A240D21
GO

Sequence cautioni

The sequence BAA13198.2 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti152 – 1521P → A in BAA13198. (PubMed:9039502)Curated
Sequence conflicti400 – 4001G → E in AAB08431. (PubMed:9006901)Curated
Sequence conflicti428 – 4281S → F in BAF82200. (PubMed:14702039)Curated
Sequence conflicti498 – 4981I → F in AAB08431. (PubMed:9006901)Curated
Sequence conflicti541 – 5411N → I in AAC50671. (PubMed:8798417)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti36 – 361P → L.
Corresponds to variant rs35647889 [ dbSNP | Ensembl ].
VAR_053112
Natural varianti95 – 951P → S.1 Publication
Corresponds to variant rs80244589 [ dbSNP | Ensembl ].
VAR_062864
Natural varianti558 – 5581D → H.
Corresponds to variant rs11768472 [ dbSNP | Ensembl ].
VAR_053113

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 5858Missing in isoform 2. 4 PublicationsVSP_001842Add
BLAST
Alternative sequencei1 – 1717MALAG…HPYYQ → MQAAGPLFRSK in isoform 4. 1 PublicationVSP_038784Add
BLAST
Alternative sequencei283 – 32846Missing in isoform 1. 2 PublicationsVSP_001843Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U34355 mRNA. Translation: AAA88819.1.
U66065 mRNA. Translation: AAC50671.1.
U69276 mRNA. Translation: AAB08431.1.
AF001534 mRNA. Translation: AAB81134.1.
AF000017 mRNA. Translation: AAC19748.1.
AB000731 mRNA. Translation: BAF76353.1.
AJ271366 mRNA. Translation: CAB96542.1.
D86962 mRNA. Translation: BAA13198.2. Different initiation.
AK289511 mRNA. Translation: BAF82200.1.
AF073378
, AF073363, AF073364, AF073365, AF073366, AF073367, AF073368, AF073369, AF073370, AF073371, AF073372, AF073373, AF073374, AF073375, AF073376, AF073377 Genomic DNA. Translation: AAC83655.1.
AF073378
, AF073363, AF073364, AF073365, AF073366, AF073367, AF073368, AF073369, AF073371, AF073372, AF073373, AF073374, AF073375, AF073376, AF073377 Genomic DNA. Translation: AAC83654.1.
AC005153 Genomic DNA. No translation available.
CH236955 Genomic DNA. Translation: EAL23897.1.
CH471128 Genomic DNA. Translation: EAW60964.1.
CH471128 Genomic DNA. Translation: EAW60965.1.
CH471128 Genomic DNA. Translation: EAW60967.1.
BC024285 mRNA. Translation: AAH24285.1.
CCDSiCCDS43582.1. [Q13322-1]
CCDS43583.1. [Q13322-3]
CCDS47586.1. [Q13322-2]
PIRiI39175.
RefSeqiNP_001001549.1. NM_001001549.2. [Q13322-2]
NP_001001550.1. NM_001001550.2. [Q13322-3]
NP_001001555.1. NM_001001555.2. [Q13322-3]
NP_005302.3. NM_005311.4. [Q13322-1]
XP_005271817.1. XM_005271760.1. [Q13322-1]
XP_005271818.1. XM_005271761.2. [Q13322-1]
XP_005271822.1. XM_005271765.1. [Q13322-3]
XP_005271823.1. XM_005271766.2. [Q13322-3]
XP_006715766.1. XM_006715703.1. [Q13322-1]
XP_006715767.1. XM_006715704.1. [Q13322-4]
XP_006715768.1. XM_006715705.1. [Q13322-3]
UniGeneiHs.164060.

Genome annotation databases

EnsembliENST00000335866; ENSP00000338543; ENSG00000106070. [Q13322-3]
ENST00000357271; ENSP00000349818; ENSG00000106070. [Q13322-2]
ENST00000398810; ENSP00000381790; ENSG00000106070. [Q13322-3]
ENST00000398812; ENSP00000381793; ENSG00000106070. [Q13322-1]
ENST00000401949; ENSP00000385770; ENSG00000106070. [Q13322-1]
ENST00000402497; ENSP00000385748; ENSG00000106070. [Q13322-3]
ENST00000402578; ENSP00000385189; ENSG00000106070. [Q13322-3]
ENST00000403097; ENSP00000385544; ENSG00000106070. [Q13322-4]
ENST00000406641; ENSP00000385366; ENSG00000106070. [Q13322-3]
ENST00000407526; ENSP00000385046; ENSG00000106070. [Q13322-3]
GeneIDi2887.
KEGGihsa:2887.
UCSCiuc003tph.3. human. [Q13322-1]
uc003tpj.2. human. [Q13322-2]
uc003tpl.2. human. [Q13322-4]

Polymorphism databases

DMDMi6166186.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U34355 mRNA. Translation: AAA88819.1 .
U66065 mRNA. Translation: AAC50671.1 .
U69276 mRNA. Translation: AAB08431.1 .
AF001534 mRNA. Translation: AAB81134.1 .
AF000017 mRNA. Translation: AAC19748.1 .
AB000731 mRNA. Translation: BAF76353.1 .
AJ271366 mRNA. Translation: CAB96542.1 .
D86962 mRNA. Translation: BAA13198.2 . Different initiation.
AK289511 mRNA. Translation: BAF82200.1 .
AF073378
, AF073363 , AF073364 , AF073365 , AF073366 , AF073367 , AF073368 , AF073369 , AF073370 , AF073371 , AF073372 , AF073373 , AF073374 , AF073375 , AF073376 , AF073377 Genomic DNA. Translation: AAC83655.1 .
AF073378
, AF073363 , AF073364 , AF073365 , AF073366 , AF073367 , AF073368 , AF073369 , AF073371 , AF073372 , AF073373 , AF073374 , AF073375 , AF073376 , AF073377 Genomic DNA. Translation: AAC83654.1 .
AC005153 Genomic DNA. No translation available.
CH236955 Genomic DNA. Translation: EAL23897.1 .
CH471128 Genomic DNA. Translation: EAW60964.1 .
CH471128 Genomic DNA. Translation: EAW60965.1 .
CH471128 Genomic DNA. Translation: EAW60967.1 .
BC024285 mRNA. Translation: AAH24285.1 .
CCDSi CCDS43582.1. [Q13322-1 ]
CCDS43583.1. [Q13322-3 ]
CCDS47586.1. [Q13322-2 ]
PIRi I39175.
RefSeqi NP_001001549.1. NM_001001549.2. [Q13322-2 ]
NP_001001550.1. NM_001001550.2. [Q13322-3 ]
NP_001001555.1. NM_001001555.2. [Q13322-3 ]
NP_005302.3. NM_005311.4. [Q13322-1 ]
XP_005271817.1. XM_005271760.1. [Q13322-1 ]
XP_005271818.1. XM_005271761.2. [Q13322-1 ]
XP_005271822.1. XM_005271765.1. [Q13322-3 ]
XP_005271823.1. XM_005271766.2. [Q13322-3 ]
XP_006715766.1. XM_006715703.1. [Q13322-1 ]
XP_006715767.1. XM_006715704.1. [Q13322-4 ]
XP_006715768.1. XM_006715705.1. [Q13322-3 ]
UniGenei Hs.164060.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1NRV X-ray 1.65 A/B 487-591 [» ]
3HK0 X-ray 2.60 A/B 164-415 [» ]
ProteinModelPortali Q13322.
SMRi Q13322. Positions 167-409, 429-465, 487-593.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 109144. 31 interactions.
DIPi DIP-31657N.
IntActi Q13322. 11 interactions.
MINTi MINT-1534184.
STRINGi 9606.ENSP00000381793.

PTM databases

PhosphoSitei Q13322.

Polymorphism databases

DMDMi 6166186.

Proteomic databases

MaxQBi Q13322.
PaxDbi Q13322.
PRIDEi Q13322.

Protocols and materials databases

DNASUi 2887.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000335866 ; ENSP00000338543 ; ENSG00000106070 . [Q13322-3 ]
ENST00000357271 ; ENSP00000349818 ; ENSG00000106070 . [Q13322-2 ]
ENST00000398810 ; ENSP00000381790 ; ENSG00000106070 . [Q13322-3 ]
ENST00000398812 ; ENSP00000381793 ; ENSG00000106070 . [Q13322-1 ]
ENST00000401949 ; ENSP00000385770 ; ENSG00000106070 . [Q13322-1 ]
ENST00000402497 ; ENSP00000385748 ; ENSG00000106070 . [Q13322-3 ]
ENST00000402578 ; ENSP00000385189 ; ENSG00000106070 . [Q13322-3 ]
ENST00000403097 ; ENSP00000385544 ; ENSG00000106070 . [Q13322-4 ]
ENST00000406641 ; ENSP00000385366 ; ENSG00000106070 . [Q13322-3 ]
ENST00000407526 ; ENSP00000385046 ; ENSG00000106070 . [Q13322-3 ]
GeneIDi 2887.
KEGGi hsa:2887.
UCSCi uc003tph.3. human. [Q13322-1 ]
uc003tpj.2. human. [Q13322-2 ]
uc003tpl.2. human. [Q13322-4 ]

Organism-specific databases

CTDi 2887.
GeneCardsi GC07M050657.
HGNCi HGNC:4564. GRB10.
HPAi CAB019423.
HPA027502.
MIMi 601523. gene.
neXtProti NX_Q13322.
PharmGKBi PA28960.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG307156.
GeneTreei ENSGT00550000074537.
HOVERGENi HBG000468.
InParanoidi Q13322.
OMAi ESTMGSE.
OrthoDBi EOG7SFHW7.
PhylomeDBi Q13322.
TreeFami TF317511.

Enzyme and pathway databases

Reactomei REACT_111040. Signaling by SCF-KIT.
REACT_1661. SHC activation.
REACT_508. Signal attenuation.
REACT_570. IRS activation.
SignaLinki Q13322.

Miscellaneous databases

ChiTaRSi GRB10. human.
EvolutionaryTracei Q13322.
GeneWikii GRB10.
GenomeRNAii 2887.
NextBioi 11401.
PROi Q13322.
SOURCEi Search...

Gene expression databases

Bgeei Q13322.
CleanExi HS_GRB10.
ExpressionAtlasi Q13322. baseline and differential.
Genevestigatori Q13322.

Family and domain databases

Gene3Di 2.30.29.30. 1 hit.
3.30.505.10. 1 hit.
InterProi IPR015042. BPS-dom.
IPR001849. PH_domain.
IPR011993. PH_like_dom.
IPR000159. Ras-assoc.
IPR000980. SH2.
IPR029071. Ubiquitin-rel_dom.
[Graphical view ]
Pfami PF08947. BPS. 1 hit.
PF00169. PH. 1 hit.
PF00788. RA. 1 hit.
PF00017. SH2. 1 hit.
[Graphical view ]
PRINTSi PR00401. SH2DOMAIN.
SMARTi SM00233. PH. 1 hit.
SM00314. RA. 1 hit.
SM00252. SH2. 1 hit.
[Graphical view ]
SUPFAMi SSF54236. SSF54236. 1 hit.
SSF55550. SSF55550. 1 hit.
PROSITEi PS50003. PH_DOMAIN. 1 hit.
PS50200. RA. 1 hit.
PS50001. SH2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Grb-IR: a SH2-domain-containing protein that binds to the insulin receptor and inhibits its function."
    Liu F., Roth R.A.
    Proc. Natl. Acad. Sci. U.S.A. 92:10287-10291(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Skeletal muscle.
  2. "Interaction of a GRB-IR splice variant (a human GRB10 homolog) with the insulin and insulin-like growth factor I receptors. Evidence for a role in mitogenic signaling."
    O'Neill T.J., Rose D.W., Pillay T.S., Hotta K., Olefsky J.M., Gustafson T.A.
    J. Biol. Chem. 271:22506-22513(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    Tissue: Skeletal muscle.
  3. "Human GRB-IR-beta/GRB10: splice variants of an insulin and growth factor receptor-binding protein with PH and SH2 domains."
    Frantz J.D., Giorgetti-Peraldi S., Ottinger E.A., Shoelson S.E.
    J. Biol. Chem. 272:2659-2667(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    Tissue: Cerebellum and Skeletal muscle.
  4. "Cloning, chromosome localization, expression, and characterization of an Src homology 2 and pleckstrin homology domain-containing insulin receptor binding protein hGrb10gamma."
    Dong L.Q., Du H., Porter S.G., Kolakowski L.F. Jr., Lee A.V., Mandarino L.J., Fan J., Yee D., Liu F.
    J. Biol. Chem. 272:29104-29112(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
  5. "Interaction of the Grb10 adapter protein with the Raf1 and MEK1 kinases."
    Nantel A., Mohammad-Ali K., Sherk J., Posner B.I., Thomas D.Y.
    J. Biol. Chem. 273:10475-10484(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
    Tissue: Brain.
  6. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PHOSPHORYLATION AT TYR-67.
  7. "Genomic structure of the gene for the SH2 and pleckstrin homology domain-containing protein GRB10 and evaluation of its role in Hirschsprung disease."
    Angrist M., Bolk S., Bentley K., Nallasamy S., Halushka M.K., Chakravarti A.
    Oncogene 17:3065-3070(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING (ISOFORM 3).
  8. "Human GRB10 is imprinted and expressed from the paternal and maternal allele in a highly tissue- and isoform-specific fashion."
    Blagitko N., Mergenthaler S., Schulz U., Wollmann H.A., Craigen W., Eggermann T., Ropers H.-H., Kalscheuer V.M.
    Hum. Mol. Genet. 9:1587-1595(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), ALTERNATIVE SPLICING, IMPRINTING.
    Tissue: Testis.
  9. "Prediction of the coding sequences of unidentified human genes. VI. The coding sequences of 80 new genes (KIAA0201-KIAA0280) deduced by analysis of cDNA clones from cell line KG-1 and brain."
    Nagase T., Seki N., Ishikawa K., Ohira M., Kawarabayasi Y., Ohara O., Tanaka A., Kotani H., Miyajima N., Nomura N.
    DNA Res. 3:321-329(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
    Tissue: Bone marrow.
  10. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Cerebellum.
  11. "The DNA sequence of human chromosome 7."
    Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L.
    , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
    Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  12. "Human chromosome 7: DNA sequence and biology."
    Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K., Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R., Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A., Kanematsu E., Gentles S.
    , Christopoulos C.C., Choufani S., Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H., Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J., Adams M.D., Tsui L.-C.
    Science 300:767-772(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  13. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  14. "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 2).
    Tissue: Kidney.
  15. "Phosphorylation of Grb10 by mitogen-activated protein kinase: identification of Ser150 and Ser476 of human Grb10zeta as major phosphorylation sites."
    Langlais P., Wang C., Dong L.Q., Carroll C.A., Weintraub S.T., Liu F.
    Biochemistry 44:8890-8897(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 415-425, PHOSPHORYLATION AT SER-150; SER-418 AND SER-476, MUTAGENESIS OF SER-104; SER-150; SER-418 AND SER-476.
  16. "Evidence against GRB10 as the gene responsible for Silver-Russell syndrome."
    McCann J.A., Zheng H., Islam A., Goodyer C.G., Polychronakos C.
    Biochem. Biophys. Res. Commun. 286:943-948(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY, IMPRINTING.
  17. "Grb10 inhibits insulin-stimulated insulin receptor substrate (IRS)-phosphatidylinositol 3-kinase/Akt signaling pathway by disrupting the association of IRS-1/IRS-2 with the insulin receptor."
    Wick K.R., Werner E.D., Langlais P., Ramos F.J., Dong L.Q., Shoelson S.E., Liu F.
    J. Biol. Chem. 278:8460-8467(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH INSR, MUTAGENESIS OF ARG-520.
  18. "NIK is a component of the EGF/heregulin receptor signaling complexes."
    Chen D., Xu L.G., Chen L., Li L., Zhai Z., Shu H.B.
    Oncogene 22:4348-4355(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MAP3K14, IDENTIFICATION IN A COMPLEX WITH EGFR AND ERBB2.
  19. "Grb10 prevents Nedd4-mediated vascular endothelial growth factor receptor-2 degradation."
    Murdaca J., Treins C., Monthouel-Kartmann M.N., Pontier-Bres R., Kumar S., Van Obberghen E., Giorgetti-Peraldi S.
    J. Biol. Chem. 279:26754-26761(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH NEDD4, MUTAGENESIS OF PRO-136; PRO-139; PRO-141 AND ARG-520.
  20. "Phosphorylation of grb10 regulates its interaction with 14-3-3."
    Urschel S., Bassermann F., Bai R.Y., Munch S., Peschel C., Duyster J.
    J. Biol. Chem. 280:16987-16993(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH YWHAE, PHOSPHORYLATION AT SER-428, MUTAGENESIS OF SER-134 AND SER-428.
  21. "Grb10 mediates insulin-stimulated degradation of the insulin receptor: a mechanism of negative regulation."
    Ramos F.J., Langlais P.R., Hu D., Dong L.Q., Liu F.
    Am. J. Physiol. 290:E1262-E1266(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: ROLE IN THE UBIQUITINATION OF INSR.
  22. "GRB10 binds to LRP6, the Wnt co-receptor and inhibits canonical Wnt signaling pathway."
    Tezuka N., Brown A.M., Yanagawa S.
    Biochem. Biophys. Res. Commun. 356:648-654(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  23. "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
    Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
    J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-418, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  24. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-104 AND SER-418, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  25. "Reciprocal imprinting of human GRB10 in placental trophoblast and brain: evolutionary conservation of reversed allelic expression."
    Monk D., Arnaud P., Frost J., Hills F.A., Stanier P., Feil R., Moore G.E.
    Hum. Mol. Genet. 18:3066-3074(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IMPRINTING.
  26. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  27. "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.
  28. "The mTOR-regulated phosphoproteome reveals a mechanism of mTORC1-mediated inhibition of growth factor signaling."
    Hsu P.P., Kang S.A., Rameseder J., Zhang Y., Ottina K.A., Lim D., Peterson T.R., Choi Y., Gray N.S., Yaffe M.B., Marto J.A., Sabatini D.M.
    Science 332:1317-1322(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-150; SER-428 AND SER-476 BY MTOR, ENZYME REGULATION.
  29. "Structural basis for dimerization of the Grb10 Src homology 2 domain. Implications for ligand specificity."
    Stein E.G., Ghirlando R., Hubbard S.R.
    J. Biol. Chem. 278:13257-13264(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 487-591.
  30. "Structural and functional studies of the Ras-associating and pleckstrin-homology domains of Grb10 and Grb14."
    Depetris R.S., Wu J., Hubbard S.R.
    Nat. Struct. Mol. Biol. 16:833-839(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 164-415, INTERACTION WITH NRAS AND PHOSPHOINOSITIDES, MUTAGENESIS OF LYS-300; LYS-305; LYS-308 AND ASN-355.
  31. Erratum
    Depetris R.S., Wu J., Hubbard S.R.
    Nat. Struct. Mol. Biol. 16:1331-1331(2009)
  32. "Imprinting of human GRB10 and its mutations in two patients with Russell-Silver syndrome."
    Yoshihashi H., Maeyama K., Kosaki R., Ogata T., Tsukahara M., Goto Y., Hata J., Matsuo N., Smith R.J., Kosaki K.
    Am. J. Hum. Genet. 67:476-482(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT SER-95, IMPRINTING.

Entry informationi

Entry nameiGRB10_HUMAN
AccessioniPrimary (citable) accession number: Q13322
Secondary accession number(s): A4D258
, A7VJ95, A8K0E6, D3DVM9, O00427, O00701, O75222, Q92606, Q92907, Q92948
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: July 15, 1999
Last modified: November 26, 2014
This is version 156 of the entry and version 2 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

The GRB10 locus is imprinted. During embryonic development, the expression in the brain and spinal cord is from the paternal allele, while in placental villous trophoblasts and skeletal muscle, it is from the maternal one. Expression is biallelic in most other tissues. Paternal expression in the brain is maintained throughout adulthood. Imprinting often is isoform-specific.
GRB10 is unlikely to be responsible for Silver-Russell syndrome (SRS).

Keywords - Technical termi

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

Documents

  1. Human chromosome 7
    Human chromosome 7: 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