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O75791 (GRAP2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 142. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
GRB2-related adapter protein 2
Alternative name(s):
Adapter protein GRID
GRB-2-like protein
Short name=GRB2L
GRBLG
GRBX
Grf40 adapter protein
Short name=Grf-40
Growth factor receptor-binding protein
Hematopoietic cell-associated adapter protein GrpL
P38
Protein GADS
SH3-SH2-SH3 adapter Mona
Gene names
Name:GRAP2
Synonyms:GADS, GRB2L, GRID
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length330 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Interacts with SLP-76 to regulate NF-AT activation. Binds to tyrosine-phosphorylated shc.

Subunit structure

Interacts with phosphorylated LIME1 upon TCR activation By similarity. Interacts with phosphorylated LAT and LAX1 upon TCR activation. Interacts with SHB. Interacts with PTPN23. Ref.13 Ref.14 Ref.15 Ref.21

Subcellular location

Nucleus. Cytoplasm. Endosome Ref.21.

Sequence similarities

Belongs to the GRB2/sem-5/DRK family.

Contains 1 SH2 domain.

Contains 2 SH3 domains.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Kcnma1Q084603EBI-740418,EBI-1633915From a different organism.
KITP107212EBI-740418,EBI-1379503
LCP2Q1309411EBI-740418,EBI-346946
PTPN23Q9H3S78EBI-740418,EBI-724478

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: O75791-1)

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.
Isoform 2 (identifier: O75791-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-39: MEAVAKFDFT...NQEEWFKAEL → MVSRRPLSTP...ELPRGLLHLC
     40-152: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 330330GRB2-related adapter protein 2
PRO_0000088208

Regions

Domain1 – 5656SH3 1
Domain58 – 14992SH2
Domain271 – 33060SH3 2

Amino acid modifications

Modified residue451Phosphotyrosine Ref.17 Ref.19
Modified residue1061N6-acetyllysine Ref.20
Modified residue2621Phosphothreonine Ref.16 Ref.17 Ref.18

Natural variations

Alternative sequence1 – 3939MEAVA…FKAEL → MVSRRPLSTPGRELTHGQGG WLLHHPGQPELPRGLLHLC in isoform 2.
VSP_055234
Alternative sequence40 – 152113Missing in isoform 2.
VSP_055235
Natural variant3191L → F. Ref.4
Corresponds to variant rs12759 [ dbSNP | Ensembl ].
VAR_012079

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified November 1, 1998. Version 1.
Checksum: 74F4C8D0EBB56D55

FASTA33037,909
        10         20         30         40         50         60 
MEAVAKFDFT ASGEDELSFH TGDVLKILSN QEEWFKAELG SQEGYVPKNF IDIQFPKWFH 

        70         80         90        100        110        120 
EGLSRHQAEN LLMGKEVGFF IIRASQSSPG DFSISVRHED DVQHFKVMRD NKGNYFLWTE 

       130        140        150        160        170        180 
KFPSLNKLVD YYRTNSISRQ KQIFLRDRTR EDQGHRGNSL DRRSQGGPHL SGAVGEEIRP 

       190        200        210        220        230        240 
SMNRKLSDHP PTLPLQQHQH QPQPPQYAPA PQQLQQPPQQ RYLQHHHFHQ ERRGGSLDIN 

       250        260        270        280        290        300 
DGHCGTGLGS EMNAALMHRR HTDPVQLQAA GRVRWARALY DFEALEDDEL GFHSGEVVEV 

       310        320        330 
LDSSNPSWWT GRLHNKLGLF PANYVAPMTR 

« Hide

Isoform 2 [UniParc].

Checksum: EC20AF61B4EFCD49
Show »

FASTA21724,382

References

« Hide 'large scale' references
[1]"Molecular cloning and expression of human grap-2, a novel leukocyte-specific SH2- and SH3-containing adaptor-like protein that binds to gab-1."
Qiu M., Hua S., Agrawal M., Li G., Cai J., Chan E., Zhou H., Luo Y., Liu M.
Biochem. Biophys. Res. Commun. 253:443-447(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]"GrpL, a Grb2-related adaptor protein, interacts with SLP-76 to regulate nuclear factor of activated T cell activation."
Law C.-L., Ewings M.K., Chaudhary P.M., Solow S.A., Yun T.J., Marshall A.J., Hood L., Clark E.A.
J. Exp. Med. 189:1243-1253(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[3]"Grf40, A novel Grb2 family member, is involved in T cell signaling through interaction with SLP-76 and LAT."
Asada H., Ishii N., Sasaki Y., Endo K., Kasai H., Tanaka N., Takeshita T., Tsuchiya S., Konno T., Sugamura K.
J. Exp. Med. 189:1383-1390(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[4]"GRID: a novel Grb-2-related adapter protein that interacts with the activated T cell costimulatory receptor CD28."
Ellis J.H., Ashman C., Burden M.N., Kilpatrick K.E., Morse M.A., Hamblin P.A.
J. Immunol. 164:5805-5814(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT PHE-319.
[5]"Genomic organization and restricted expression of the human Mona/Gads gene suggests regulation by two specific promoters."
Guyot B., Arnaud S., Phothirath P., Bourette R.P., Grasset M.F., Rigal D., Mouchiroud G.
Gene 290:173-179(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[6]Frearson J.
Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Blood.
[7]"Cloning of the human and mouse growth factor receptor binding protein like genes."
Kedra D., Dumanski J.P.
Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[8]"GrbX, new recruited signaling gene having homology with Grb2."
Teramoto T., Nagashima M., Terai S., Thorgeirsson S.S.
Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[9]"A genome annotation-driven approach to cloning the human ORFeome."
Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A., Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J., Beare D.M., Dunham I.
Genome Biol. 5:R84.1-R84.11(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[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. expand/collapse author list , 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: Thymus.
[11]"The DNA sequence of human chromosome 22."
Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M. expand/collapse author list , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H.
Nature 402:489-495(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[12]"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: Lung and Spleen.
[13]"Association of Grb2, Gads, and phospholipase C-gamma 1 with phosphorylated LAT tyrosine residues. Effect of LAT tyrosine mutations on T cell antigen receptor-mediated signaling."
Zhang W., Trible R.P., Zhu M., Liu S.K., McGlade C.J., Samelson L.E.
J. Biol. Chem. 275:23355-23361(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH LAT.
[14]"Shb links SLP-76 and Vav with the CD3 complex in Jurkat T cells."
Lindholm C.K., Henriksson M.L., Hallberg B., Welsh M.
Eur. J. Biochem. 269:3279-3288(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SHB.
[15]"Molecular cloning of a novel gene encoding a membrane-associated adaptor protein (LAX) in lymphocyte signaling."
Zhu M., Janssen E., Leung K., Zhang W.
J. Biol. Chem. 277:46151-46158(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH LAX1.
[16]"Profiling of tyrosine phosphorylation pathways in human cells using mass spectrometry."
Salomon A.R., Ficarro S.B., Brill L.M., Brinker A., Phung Q.T., Ericson C., Sauer K., Brock A., Horn D.M., Schultz P.G., Peters E.C.
Proc. Natl. Acad. Sci. U.S.A. 100:443-448(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-262, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[17]"Robust phosphoproteomic profiling of tyrosine phosphorylation sites from human T cells using immobilized metal affinity chromatography and tandem mass spectrometry."
Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M., Peters E.C.
Anal. Chem. 76:2763-2772(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-45 AND THR-262, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[18]"Phosphoproteome of resting human platelets."
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A.
J. Proteome Res. 7:526-534(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-262, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Platelet.
[19]"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 TYR-45, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[20]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-106, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[21]"Histidine domain-protein tyrosine phosphatase interacts with Grb2 and GrpL."
Tanase C.A.
PLoS ONE 5:E14339-E14339(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PTPN23, SUBCELLULAR LOCATION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF102694 mRNA. Translation: AAD04926.1.
AF129476 mRNA. Translation: AAD41782.1.
AF042380 mRNA. Translation: AAC69273.1.
AF236119 mRNA. Translation: AAF60319.1.
AF236120 mRNA. Translation: AAF60320.1.
AF121002 mRNA. Translation: AAF31758.1.
AY069959 mRNA. Translation: AAL58573.1.
Y18051 mRNA. Translation: CAA77021.1.
AJ011736 mRNA. Translation: CAA09757.1.
AF090456 mRNA. Translation: AAD13027.1.
CR456498 mRNA. Translation: CAG30384.1.
AK303470 mRNA. Translation: BAH13969.1.
Z82206 Genomic DNA. Translation: CAI42713.1.
BC025692 mRNA. Translation: AAH25692.1.
BC026002 mRNA. Translation: AAH26002.1.
CCDSCCDS13999.1.
PIRJE0376.
RefSeqNP_001278753.1. NM_001291824.1.
NP_001278754.1. NM_001291825.1.
NP_004801.1. NM_004810.3.
UniGeneHs.517499.

3D structure databases

ProteinModelPortalO75791.
SMRO75791. Positions 1-186, 273-328.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114799. 28 interactions.
DIPDIP-38435N.
IntActO75791. 19 interactions.
MINTMINT-140970.
STRING9606.ENSP00000339186.

PTM databases

PhosphoSiteO75791.

Proteomic databases

MaxQBO75791.
PaxDbO75791.
PRIDEO75791.

Protocols and materials databases

DNASU9402.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000344138; ENSP00000339186; ENSG00000100351.
ENST00000399090; ENSP00000382040; ENSG00000100351.
ENST00000407075; ENSP00000385607; ENSG00000100351.
GeneID9402.
KEGGhsa:9402.
UCSCuc003ayh.2. human.

Organism-specific databases

CTD9402.
GeneCardsGC22P040297.
HGNCHGNC:4563. GRAP2.
HPACAB022073.
HPA005788.
MIM604518. gene.
neXtProtNX_O75791.
PharmGKBPA28959.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG272892.
HOGENOMHOG000251625.
HOVERGENHBG005404.
InParanoidO75791.
KOK07366.
OMAQFPEWFH.
OrthoDBEOG75F4F6.
PhylomeDBO75791.
TreeFamTF354288.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
REACT_6900. Immune System.
SignaLinkO75791.

Gene expression databases

ArrayExpressO75791.
BgeeO75791.
CleanExHS_GRAP2.
GenevestigatorO75791.

Family and domain databases

Gene3D3.30.505.10. 1 hit.
InterProIPR000980. SH2.
IPR001452. SH3_domain.
[Graphical view]
PfamPF00017. SH2. 1 hit.
PF00018. SH3_1. 2 hits.
[Graphical view]
PRINTSPR00401. SH2DOMAIN.
PR00452. SH3DOMAIN.
SMARTSM00252. SH2. 1 hit.
SM00326. SH3. 2 hits.
[Graphical view]
SUPFAMSSF50044. SSF50044. 2 hits.
SSF55550. SSF55550. 1 hit.
PROSITEPS50001. SH2. 1 hit.
PS50002. SH3. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSGRAP2. human.
GeneWikiGRAP2.
GenomeRNAi9402.
NextBio35223.
PMAP-CutDBO75791.
PROO75791.
SOURCESearch...

Entry information

Entry nameGRAP2_HUMAN
AccessionPrimary (citable) accession number: O75791
Secondary accession number(s): B7Z8I3, O43726, Q9NRB7
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: November 1, 1998
Last modified: July 9, 2014
This is version 142 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 22

Human chromosome 22: entries, gene names and cross-references to MIM