Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q96QH2 (PRAM_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 85. 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:
PML-RARA-regulated adapter molecule 1

Short name=PRAM
Short name=PRAM-1
Gene names
Name:PRAM1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length718 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

May be involved in myeloid differentiation. May be involved in integrin signaling in neutrophils. Binds to PtdIns4P.

Subunit structure

Interacts with SKAP2, LCP2 and DBNL. May interact with LYN. Interacts with NEK6. Ref.1 Ref.4 Ref.7

Tissue specificity

Expressed in peripheral blood leukocytes and bone marrow. Expressed in monocytes, and to a lesser extent in granulocytes and lymphocytes. Not expressed in non hematopoietic tissues except in lung. Ref.1

Induction

Down-regulated by the PML-RARA oncogene, a fusion protein expressed in a vast majority of acute promyelocytic leukemia. Up-regulated by retinoic acid or arsenic trioxide in cells expressing PML-RARA. Ref.1 Ref.4

Domain

The SH3 domain binds to PtdIns4P.

Post-translational modification

May be phosphorylated on tyrosines. Ref.1

Sequence similarities

Contains 1 SH3 domain.

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

RNF32Q9H0A62EBI-2860740,EBI-724829

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q96QH2-1)

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: Q96QH2-2)

The sequence of this isoform differs from the canonical sequence as follows:
     70-117: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 718718PML-RARA-regulated adapter molecule 1
PRO_0000270171

Regions

Repeat70 – 81121
Repeat82 – 93122
Repeat94 – 105123
Repeat106 – 117124
Repeat118 – 129125
Repeat130 – 141126
Repeat142 – 153127
Repeat154 – 165128
Domain622 – 69675SH3
Region70 – 165968 X 12 AA repeats of K-P-P-[PQ]-P-[EQ]-[VAF]-T-D-L-P-K
Compositional bias27 – 511485Pro-rich

Natural variations

Alternative sequence70 – 11748Missing in isoform 2.
VSP_022178
Natural variant571K → Q. Ref.1
Corresponds to variant rs4804305 [ dbSNP | Ensembl ].
VAR_029808
Natural variant731Q → P.
Corresponds to variant rs4239541 [ dbSNP | Ensembl ].
VAR_029809
Natural variant761F → V.
Corresponds to variant rs4239540 [ dbSNP | Ensembl ].
VAR_029810
Natural variant1831G → E.
Corresponds to variant rs58466313 [ dbSNP | Ensembl ].
VAR_061692

Experimental info

Sequence conflict111S → N in AAH28012. Ref.3
Sequence conflict1241V → A in CAC17767. Ref.1

Sequences

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

Last modified April 5, 2011. Version 2.
Checksum: 212A6BA694578F2D

FASTA71879,245
        10         20         30         40         50         60 
MAHHLPAAME SHQDFRSIKA KFQASQPEPS DLPKKPPKPE FGKLKKFSQP ELSEHPKKAP 

        70         80         90        100        110        120 
LPEFGAVSLK PPQPQFTDLP KKPPPPEVTD LPKKPPPPEV TDLPKKPPPP EVTDLPKKPP 

       130        140        150        160        170        180 
PPEVTDLPKK PPPPEVTDLP KKPPPPEVTD LPKKPPPPEV TDLPKKPSKL ELSDLSKKFP 

       190        200        210        220        230        240 
QLGATPFPRK PLQPEVGEAP LKASLPEPGA PARKPLQPDE LSHPARPPSE PKSGAFPRKL 

       250        260        270        280        290        300 
WQPEAGEATP RSPQPELSTF PKKPAQPEFN VYPKKPPQPQ VGGLPKKSVP QPEFSEAAQT 

       310        320        330        340        350        360 
PLWKPQSSEP KRDSSAFPKK ASQPPLSDFP KKPPQPELGD LTRTSSEPEV SVLPKRPRPA 

       370        380        390        400        410        420 
EFKALSKKPP QPELGGLPRT SSEPEFNSLP RKLLQPERRG PPRKFSQPEP SAVLKRHPQP 

       430        440        450        460        470        480 
EFFGDLPRKP PLPSSASESS LPAAVAGFSS RHPLSPGFGA AGTPRWRSGG LVHSGGARPG 

       490        500        510        520        530        540 
LRPSHPPRRR PLPPASSLGH PPAKPPLPPG PVDMQSFRRP SAASIDLRRT RSAAGLHFQD 

       550        560        570        580        590        600 
RQPEDIPQVP DEIYELYDDV EPRDDSSPSP KGRDEAPSVQ QAARRPPQDP ALRKEKDPQP 

       610        620        630        640        650        660 
QQLPPMDPKL LKQLRKAEKA EREFRKKFKF EGEIVVHTKM MIDPNAKTRR GGGKHLGIRR 

       670        680        690        700        710 
GEILEVIEFT SNEEMLCRDP KGKYGYVPRT ALLPLETEVY DDVDFCDPLE NQPLPLGR 

« Hide

Isoform 2 [UniParc].

Checksum: 6C05FFBC05CE739F
Show »

FASTA67073,969

References

« Hide 'large scale' references
[1]"PRAM-1 is a novel adaptor protein regulated by retinoic acid (RA) and promyelocytic leukemia (PML)-RA receptor alpha in acute promyelocytic leukemia cells."
Moog-Lutz C., Peterson E.J., Lutz P.G., Eliason S., Cave-Riant F., Singer A., Di Gioia Y., Dmovski S., Kamens J., Cayre Y.E., Koretzky G.
J. Biol. Chem. 276:22375-22381(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INDUCTION, TISSUE SPECIFICITY, PHOSPHORYLATION, INTERACTION WITH SKAP2; LCP2 AND LYN, VARIANT GLN-57.
[2]"The DNA sequence and biology of human chromosome 19."
Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V. expand/collapse author list , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Blood.
[4]"PRAM-1 potentiates arsenic trioxide-induced JNK activation."
Denis F.M., Benecke A., Di Gioia Y., Touw I.P., Cayre Y.E., Lutz P.G.
J. Biol. Chem. 280:9043-9048(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH DBNL, INDUCTION.
[5]"Lipid-binding hSH3 domains in immune cell adapter proteins."
Heuer K., Sylvester M., Kliche S., Pusch R., Thiemke K., Schraven B., Freund C.
J. Mol. Biol. 361:94-104(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHOINOSITIDE-BINDING.
[6]"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[7]"Characterization of hNek6 interactome reveals an important role for its short N-terminal domain and colocalization with proteins at the centrosome."
Vaz Meirelles G., Ferreira Lanza D.C., da Silva J.C., Santana Bernachi J., Paes Leme A.F., Kobarg J.
J. Proteome Res. 9:6298-6316(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH NEK6.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ272324 mRNA. Translation: CAC17767.1.
AC092298 Genomic DNA. No translation available.
AC136469 Genomic DNA. No translation available.
BC028012 mRNA. Translation: AAH28012.1.
RefSeqNP_115528.4. NM_032152.4.
UniGeneHs.465812.

3D structure databases

ProteinModelPortalQ96QH2.
SMRQ96QH2. Positions 618-692.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid123894. 20 interactions.
IntActQ96QH2. 7 interactions.
STRING9606.ENSP00000255612.

PTM databases

PhosphoSiteQ96QH2.

Polymorphism databases

DMDM327478532.

Proteomic databases

PaxDbQ96QH2.
PRIDEQ96QH2.

Protocols and materials databases

DNASU84106.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000423345; ENSP00000408342; ENSG00000133246. [Q96QH2-2]
GeneID84106.
KEGGhsa:84106.
UCSCuc002mkd.3. human. [Q96QH2-2]

Organism-specific databases

CTD84106.
GeneCardsGC19M008554.
H-InvDBHIX0202846.
HGNCHGNC:30091. PRAM1.
HPAHPA050161.
MIM606466. gene.
neXtProtNX_Q96QH2.
PharmGKBPA142671137.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG12793.
HOGENOMHOG000168515.
HOVERGENHBG082165.
InParanoidQ96QH2.
OMAFQASQPE.
OrthoDBEOG75QR3T.
PhylomeDBQ96QH2.

Gene expression databases

ArrayExpressQ96QH2.
BgeeQ96QH2.
CleanExHS_PRAM1.
GenevestigatorQ96QH2.

Family and domain databases

InterProIPR001452. SH3_domain.
[Graphical view]
SMARTSM00326. SH3. 1 hit.
[Graphical view]
SUPFAMSSF50044. SSF50044. 1 hit.
ProtoNetSearch...

Other

GeneWikiPRAM1.
GenomeRNAi84106.
NextBio73367.
PROQ96QH2.
SOURCESearch...

Entry information

Entry namePRAM_HUMAN
AccessionPrimary (citable) accession number: Q96QH2
Secondary accession number(s): Q8N6W7
Entry history
Integrated into UniProtKB/Swiss-Prot: January 9, 2007
Last sequence update: April 5, 2011
Last modified: April 16, 2014
This is version 85 of the entry and version 2 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 19

Human chromosome 19: entries, gene names and cross-references to MIM