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O60880 (SH21A_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 123. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
SH2 domain-containing protein 1A
Alternative name(s):
Duncan disease SH2-protein
Signaling lymphocytic activation molecule-associated protein
Short name=SLAM-associated protein
T-cell signal transduction molecule SAP
Gene names
Name:SH2D1A
Synonyms:DSHP, SAP
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length128 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Inhibitor of the SLAM self-association. Acts by blocking recruitment of the SH2-domain-containing signal-transduction molecule SHP-2 to a docking site in the SLAM cytoplasmic region. Mediates interaction between FYN and SLAMF1. May also regulate the activity of the neurotrophin receptors NTRK1, NTRK2 and NTRK3.

Subunit structure

Interacts with NTRK1, NTRK2 and NTRK3 By similarity. Interacts with CD84, CD244, LY9, SLAMF1 and FYN. Ref.10 Ref.11 Ref.20

Subcellular location

Cytoplasm Probable.

Tissue specificity

Expressed at a high level in thymus and lung, with a lower level of expression in spleen and liver. Expressed in peripheral blood leukocytes, including T-lymphocytes. Tends to be expressed at lower levels in peripheral blood leukocytes in patients with rheumatoid arthritis. Ref.3

Involvement in disease

Lymphoproliferative syndrome, X-linked, 1 (XLP1) [MIM:308240]: A rare immunodeficiency characterized by extreme susceptibility to infection with Epstein-Barr virus (EBV). Symptoms include severe or fatal mononucleosis, acquired hypogammaglobulinemia, pancytopenia and malignant lymphoma.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.1 Ref.14 Ref.16 Ref.17 Ref.18 Ref.19 Ref.20 Ref.21 Ref.23 Ref.24

Sequence similarities

Contains 1 SH2 domain.

Alternative products

This entry describes 6 isoforms produced by alternative splicing. [Align] [Select]
Isoform A (identifier: O60880-1)

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 B (identifier: O60880-2)

The sequence of this isoform differs from the canonical sequence as follows:
     68-128: TAPGVHKRYFRKIKNLISAFQKPDQGIVIPLQYPVEKKSSARSTQGTTGIREDPDVCLKAP → HFRSQIKA
Isoform C (identifier: O60880-3)

The sequence of this isoform differs from the canonical sequence as follows:
     47-128: YHGYIYTYRV...EDPDVCLKAP → QHLGYIKDISGK
Isoform D (identifier: O60880-4)

The sequence of this isoform differs from the canonical sequence as follows:
     114-116: Missing.
Isoform E (identifier: O60880-5)

The sequence of this isoform differs from the canonical sequence as follows:
     40-128: VYCLCVLYHG...EDPDVCLKAP → ITVTFIHTEC...RHCNTSAVSS
Isoform F (identifier: O60880-6)

The sequence of this isoform differs from the canonical sequence as follows:
     47-128: YHGYIYTYRV...EDPDVCLKAP → ISEARSRHCNTSAVSS

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 128128SH2 domain-containing protein 1A
PRO_0000097722

Regions

Domain6 – 10499SH2

Amino acid modifications

Modified residue891N6-acetyllysine Ref.12

Natural variations

Alternative sequence40 – 12889VYCLC…CLKAP → ITVTFIHTECPRQKQVLGVL SISEARSRHCNTSAVSS in isoform E.
VSP_004388
Alternative sequence47 – 12882YHGYI…CLKAP → QHLGYIKDISGK in isoform C.
VSP_004387
Alternative sequence47 – 12882YHGYI…CLKAP → ISEARSRHCNTSAVSS in isoform F.
VSP_004389
Alternative sequence68 – 12861TAPGV…CLKAP → HFRSQIKA in isoform B.
VSP_004386
Alternative sequence114 – 1163Missing in isoform D.
VSP_004390
Natural variant71Y → C in XLP1; reduced protein stability and reduced affinity for SLAMF1. Ref.14 Ref.17 Ref.20
VAR_048005
Natural variant81H → D in XLP1. Ref.19
VAR_048006
Natural variant161G → D in XLP1; abolishes interaction with SLAMF1. Ref.23
VAR_048007
Natural variant271G → S in XLP1. Ref.19
VAR_048008
Natural variant281S → R in XLP1; reduced protein stability. Ref.14 Ref.17 Ref.20
VAR_048009
Natural variant311L → P in XLP1; reduced protein stability and reduced affinity for SLAMF1 and FYN. Ref.17 Ref.21
VAR_048010
Natural variant321R → T in XLP1. Ref.1 Ref.16
VAR_005612
Natural variant331D → Y in XLP1. Ref.19
VAR_048011
Natural variant421C → W in XLP1; loss of interaction with CD84 and reduced affinity for SLAMF1. Ref.17 Ref.20
VAR_048012
Natural variant491G → V in XLP1. Ref.19
VAR_048013
Natural variant531T → I in XLP1; loss of interaction with CD48 and reduced affinity for SLAMF1 and loss of interaction with non-phosphorylated SLAMF1. Ref.14 Ref.17 Ref.20
VAR_048014
Natural variant541Y → C in XLP1; reduced protein stability and reduced affinity for SLAMF1 and FYN. Ref.17 Ref.21 Ref.24
VAR_048015
Natural variant551R → L in XLP1; reduced affinity for SLAMF1 and FYN. Ref.18 Ref.21
VAR_018307
Natural variant571S → P in one XLP1 patient; unknown pathological significance. Ref.22
VAR_048016
Natural variant681T → I in XLP1; loss of interaction with CD48 and strongly reduced affinity for SLAMF1. Ref.1 Ref.14 Ref.20
VAR_005613
Natural variant841I → T in XLP1; reduced protein stability. Ref.24
VAR_048017
Natural variant871F → S in XLP1; reduced protein stability and reduced affinity for SLAMF1 and FYN. Ref.17 Ref.21 Ref.24
VAR_048018
Natural variant991Q → P in XLP1; reduced protein stability and strongly reduced affinity for SLAMF1. Ref.14 Ref.17 Ref.20
VAR_048019
Natural variant1011P → L in XLP1; reduced protein stability and reduced affinity for SLAMF1. Ref.1 Ref.14 Ref.20
Corresponds to variant rs28935184 [ dbSNP | Ensembl ].
VAR_005614
Natural variant1021V → G in XLP1; reduced protein stability and strongly reduced affinity for SLAMF1. Ref.14 Ref.17 Ref.20
VAR_048020

Experimental info

Mutagenesis321R → Q: Strongly reduced affinity for SLAMF1. Ref.14

Secondary structure

.................... 128
Helix Strand Turn

Details...

Sequences

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

Last modified August 1, 1998. Version 1.
Checksum: 90234E7A6614EE3D

FASTA12814,187
        10         20         30         40         50         60 
MDAVAVYHGK ISRETGEKLL LATGLDGSYL LRDSESVPGV YCLCVLYHGY IYTYRVSQTE 

        70         80         90        100        110        120 
TGSWSAETAP GVHKRYFRKI KNLISAFQKP DQGIVIPLQY PVEKKSSARS TQGTTGIRED 


PDVCLKAP 

« Hide

Isoform B [UniParc].

Checksum: 49A81B180192072A
Show »

FASTA758,392
Isoform C [UniParc].

Checksum: 39720893ACB3518A
Show »

FASTA586,284
Isoform D [UniParc].

Checksum: 1E5EE8978D67E5D6
Show »

FASTA12513,928
Isoform E [UniParc].

Checksum: 5BA2292A94518C00
Show »

FASTA768,188
Isoform F [UniParc].

Checksum: 51B125509F7EB9C4
Show »

FASTA626,631

References

« Hide 'large scale' references
[1]"Host response to EBV infection in X-linked lymphoproliferative disease results from mutations in an SH2-domain encoding gene."
Coffey A.J., Brooksbank R.A., Brandau O., Oohashi T., Howell G.R., Bye J.M., Cahn A.P., Durham J., Heath P., Wray P., Pavitt R., Wilkinson J., Leversha M., Huckle E., Shaw-Smith C.J., Dunham A., Rhodes S., Schuster V. expand/collapse author list , Porta G., Yin L., Serafini P., Sylla B., Zollo M., Franco B., Bentley D.R.
Nat. Genet. 20:129-135(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS XLP1 THR-32; ILE-68 AND LEU-101.
[2]"The X-linked lymphoproliferative-disease gene product SAP regulates signals induced through the co-receptor SLAM."
Sayos J., Wu C., Morra M., Wang N., Zhang X., Allen D., van Schaik S., Notarangelo L., Geha R., Roncarolo M.G., Oettgen H., de Vries J.E., Aversa G., Terhorst C.
Nature 395:462-469(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"Decreased expression of signaling lymphocytic-activation molecule-associated protein (SAP) transcripts in T cells from patients with rheumatoid arthritis."
Takei M., Ishiwata T., Mitamura K., Fujiwara S., Sasaki K., Nishi T., Kuga T., Ookubo T., Horie T., Ryu J., Ohi H., Sawada S.
Int. Immunol. 13:559-565(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
[4]"The Duncan's disease gene is preferentially expressed in lymphoid cell lineages and undergoes high levels of alternative splicing."
Amemiya C.T., Halevi A.
Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA], ALTERNATIVE SPLICING.
[5]"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].
[6]"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y., LaBaer J.
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[7]"The DNA sequence of the human X chromosome."
Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C. expand/collapse author list , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[9]"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 A).
Tissue: Lung.
[10]"Cell surface receptors Ly-9 and CD84 recruit the X-linked lymphoproliferative disease gene product SAP."
Sayos J., Martin M., Chen A., Simarro M., Howie D., Morra M., Engel P., Terhorst C.
Blood 97:3867-3874(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CD84.
[11]"CD84 is up-regulated on a major population of human memory B cells and recruits the SH2 domain containing proteins SAP and EAT-2."
Tangye S.G., van de Weerdt B.C.M., Avery D.T., Hodgkin P.D.
Eur. J. Immunol. 32:1640-1649(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CD84.
[12]"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-89, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]"Crystal structures of the XLP protein SAP reveal a class of SH2 domains with extended, phosphotyrosine-independent sequence recognition."
Poy F., Yaffe M.B., Sayos J., Saxena K., Morra M., Sumegi J., Cantley L.C., Terhorst C., Eck M.J.
Mol. Cell 4:555-561(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.1 ANGSTROMS) OF 1-104.
[14]"A 'three-pronged' binding mechanism for the SAP/SH2D1A SH2 domain: structural basis and relevance to the XLP syndrome."
Hwang P.M., Li C., Morra M., Lillywhite J., Muhandiram D.R., Gertler F., Terhorst C., Kay L.E., Pawson T., Forman-Kay J.D., Li S.-C.
EMBO J. 21:314-323(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR IN COMPLEX WITH SLAMF1, CHARACTERIZATION OF VARIANTS XLP1 CYS-7; ARG-28; ILE-53; ILE-68; PRO-99; LEU-101 AND GLY-102, MUTAGENESIS OF ARG-32.
[15]"SAP couples Fyn to SLAM immune receptors."
Chan B., Lanyi A., Song H.K., Griesbach J., Simarro-Grande M., Poy F., Howie D., Sumegi J., Terhorst C., Eck M.J.
Nat. Cell Biol. 5:155-160(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 1-104 IN COMPLEX WITH SLAMF1 AND FYN.
[16]"SH2D1A mutation analysis for diagnosis of XLP in typical and atypical patients."
Yin L., Ferrand V., Lavoue M.-F., Hayoz D., Philippe N., Souillet G., Seri M., Giacchino R., Castagnola E., Hodgson S., Sylla B.S., Romeo G.
Hum. Genet. 105:501-505(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT XLP1 THR-32.
[17]"Correlation of mutations of the SH2D1A gene and Epstein-Barr virus infection with clinical phenotype and outcome in X-linked lymphoproliferative disease."
Sumegi J., Huang D., Lanyi A., Davis J.D., Seemayer T.A., Maeda A., Klein G., Seri M., Wakiguchi H., Purtilo D.T., Gross T.G.
Blood 96:3118-3125(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS XLP1 CYS-7; ARG-28; PRO-31; TRP-42; ILE-53; CYS-54; SER-87; PRO-99 AND GLY-102.
[18]"Defective NK cell activation in X-linked lymphoproliferative disease."
Benoit L., Wang X., Pabst H.F., Dutz J., Tan R.
J. Immunol. 165:3549-3553(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT XLP1 LEU-55.
[19]"SH2D1A mutations in Japanese males with severe Epstein-Barr virus-associated illnesses."
Sumazaki R., Kanegane H., Osaki M., Fukushima T., Tsuchida M., Matsukura H., Shinozaki K., Kimura H., Matsui A., Miyawaki T.
Blood 98:1268-1270(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS XLP1 ASP-8; SER-27; TYR-33 AND VAL-49.
[20]"Characterization of SH2D1A missense mutations identified in X-linked lymphoproliferative disease patients."
Morra M., Simarro-Grande M., Martin M., Chen A.S.-I., Lanyi A., Silander O., Calpe S., Davis J., Pawson T., Eck M.J., Sumegi J., Engel P., Li S.-C., Terhorst C.
J. Biol. Chem. 276:36809-36816(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION OF VARIANTS XLP1 CYS-7; ARG-28; TRP-42; ILE-53; ILE-68; PRO-99; LEU-101 AND GLY-102, INTERACTION WITH CD244; SLAMF1; CD48 AND LY9.
[21]"Disease-causing SAP mutants are defective in ligand binding and protein folding."
Li C., Iosef C., Jia C.Y.H., Gkourasas T., Han V.K.M., Li S.-C.
Biochemistry 42:14885-14892(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION OF VARIANTS XLP1 PRO-31; CYS-54; LEU-55 AND SER-87.
[22]"Fatal hemophagocytic lymphohistiocytosis associated with Epstein-Barr virus infection in a patient with a novel mutation in the signaling lymphocytic activation molecule-associated protein."
Halasa N.B., Whitlock J.A., McCurley T.L., Smith J.A., Zhu Q., Ochs H., Dermody T.S., Crowe J.E. Jr.
Clin. Infect. Dis. 37:E136-E141(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT PRO-57.
[23]"Characterization of a new disease-causing mutation of SH2D1A in a family with X-linked lymphoproliferative disease."
Erdos M., Uzvoelgyi E., Nemes Z., Toeroek O., Rakoczi E., Went-Suemegi N., Suemegi J., Marodi L.
Hum. Mutat. 25:506-506(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT XLP1 ASP-16, CHARACTERIZATION OF VARIANT XLP1 ASP-16.
[24]"Missense mutations in SH2D1A identified in patients with X-linked lymphoproliferative disease differentially affect the expression and function of SAP."
Hare N.J., Ma C.S., Alvaro F., Nichols K.E., Tangye S.G.
Int. Immunol. 18:1055-1065(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS XLP1 CYS-54; THR-84 AND SER-87, CHARACTERIZATION OF VARIANTS XLP1 CYS-54; THR-84 AND SER-87.
+Additional computationally mapped references.

Web resources

SH2D1Abase

SH2D1A mutation db

GeneReviews

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL023657 mRNA. Translation: CAA19222.1.
AF073019 mRNA. Translation: AAC62631.1.
AF072930 mRNA. Translation: AAC62630.1.
AB586694 mRNA. Translation: BAJ19023.1.
AF100539 mRNA. Translation: AAC79712.1.
AF100540 mRNA. Translation: AAC79713.1.
AF100541 mRNA. Translation: AAC79714.1.
AF100542 mRNA. Translation: AAC79715.1.
AF100543 mRNA. Translation: AAC79716.1.
AK311911 mRNA. Translation: BAG34852.1.
CR542031 mRNA. Translation: CAG46828.1.
CR542043 mRNA. Translation: CAG46840.1.
AL022718 Genomic DNA. Translation: CAA18777.1.
CH471107 Genomic DNA. Translation: EAX11848.1.
CH471107 Genomic DNA. Translation: EAX11849.1.
BC020732 mRNA. Translation: AAH20732.1.
RefSeqNP_001108409.1. NM_001114937.2.
NP_002342.1. NM_002351.4.
UniGeneHs.349094.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1D1ZX-ray1.40A/B/C/D1-104[»]
1D4TX-ray1.10A1-104[»]
1D4WX-ray1.80A/B1-104[»]
1KA6NMR-A1-128[»]
1KA7NMR-A1-128[»]
1M27X-ray2.50A1-104[»]
ProteinModelPortalO60880.
SMRO60880. Positions 1-104.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid110246. 15 interactions.
IntActO60880. 13 interactions.
MINTMINT-113697.
STRING9606.ENSP00000360181.

Chemistry

ChEMBLCHEMBL2321636.

PTM databases

PhosphoSiteO60880.

Proteomic databases

PaxDbO60880.
PRIDEO60880.

Protocols and materials databases

DNASU4068.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000360027; ENSP00000353126; ENSG00000183918. [O60880-4]
ENST00000371139; ENSP00000360181; ENSG00000183918. [O60880-1]
ENST00000477673; ENSP00000477094; ENSG00000183918. [O60880-5]
GeneID4068.
KEGGhsa:4068.
UCSCuc004euf.4. human. [O60880-1]
uc004euh.4. human. [O60880-4]

Organism-specific databases

CTD4068.
GeneCardsGC0XP123480.
HGNCHGNC:10820. SH2D1A.
MIM300490. gene.
308240. phenotype.
neXtProtNX_O60880.
Orphanet2442. X-linked lymphoproliferative disease.
PharmGKBPA35728.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG298713.
HOVERGENHBG003702.
InParanoidO60880.
KOK07990.
OMAQGIAMPL.
OrthoDBEOG72VH86.
PhylomeDBO60880.
TreeFamTF343096.

Enzyme and pathway databases

SignaLinkO60880.

Gene expression databases

BgeeO60880.
CleanExHS_SH2D1A.
GenevestigatorO60880.

Family and domain databases

Gene3D3.30.505.10. 1 hit.
InterProIPR000980. SH2.
IPR017289. SH2_prot_1A.
[Graphical view]
PfamPF00017. SH2. 1 hit.
[Graphical view]
PIRSFPIRSF037828. SH2_p1A. 1 hit.
PRINTSPR00401. SH2DOMAIN.
SMARTSM00252. SH2. 1 hit.
[Graphical view]
SUPFAMSSF55550. SSF55550. 1 hit.
PROSITEPS50001. SH2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceO60880.
GeneWikiSH2D1A.
GenomeRNAi4068.
NextBio15948.
PROO60880.
SOURCESearch...

Entry information

Entry nameSH21A_HUMAN
AccessionPrimary (citable) accession number: O60880
Secondary accession number(s): A8MSW0 expand/collapse secondary AC list , O95383, O95384, O95385, O95386, Q6FGS6, Q9UNR0
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: August 1, 1998
Last modified: April 16, 2014
This is version 123 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

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 X

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